%% This BibTeX bibliography file was created using BibDesk. %% http://bibdesk.sourceforge.net/ %% Created for Eric Peterson at 2008-05-30 02:56:10 -0700 %% Saved with string encoding Western (ASCII) @article{grooth:1248, Author = {Bart G. de Grooth}, Date-Added = {2008-05-08 00:46:14 -0700}, Date-Modified = {2008-05-08 00:46:14 -0700}, Doi = {10.1119/1.19111}, Journal = {American Journal of Physics}, Keywords = {Brownian motion; teaching; fluctuations; digital simulation}, Number = {12}, Pages = {1248-1252}, Publisher = {AAPT}, Title = {A simple model for Brownian motion leading to the Langevin equation}, Url = {http://link.aip.org/link/?AJP/67/1248/1}, Volume = {67}, Year = {1999}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://link.aip.org/link/?AJP/67/1248/1}, Bdsk-Url-2 = {http://dx.doi.org/10.1119/1.19111}} @url{Ruiz:fv, Author = {Ruiz, M}, Date-Added = {2008-05-07 10:56:39 -0700}, Date-Modified = {2008-05-29 16:21:33 -0700}, Title = {Endomembrane system diagram}, Url = {http://commons.wikimedia.org/wiki/Image:Endomembrane\_system\_diagram.svg}, Bdsk-Url-1 = {http://commons.wikimedia.org/wiki/Image:Endomembrane_system_diagram.svg}} @article{Marsh:2001zl, Author = {Marsh, B J and Mastronarde, D N and Buttle, K F and Howell, K E and McIntosh, J R}, Date-Added = {2008-05-07 10:53:38 -0700}, Date-Modified = {2008-05-30 02:52:21 -0700}, Eprint = {http://www.pnas.org/cgi/reprint/98/5/2399.pdf}, Journal = {Proc Natl Acad Sci USA}, Number = {5}, Pages = {2399--2406}, Title = {Organellar relationships in the {Golgi} region of the pancreatic beta cell line, {HIT-T15}, visualized by high resolution electron tomography}, Volume = {98}, Year = {2001}, Bdsk-Url-1 = {http://www.pnas.org/cgi/content/abstract/98/5/2399}, Bdsk-Url-2 = {http://dx.doi.org/10.1073/pnas.051631998}} @book{Freeman:2008rt, Annote = {Includes index}, Author = {Freeman, S}, Date-Added = {2008-04-24 10:41:26 -0700}, Date-Modified = {2008-05-29 16:36:14 -0700}, Edition = {3rd}, Publisher = {Pearson/Benjamin Cummings}, Title = {Biological Science}, Year = {2008}} @article{Grunewald:2003lr, Abstract = {Electron cryotomography has unique potential for three-dimensional visualization of macromolecular complexes at work in their natural environment. This approach is based on reconstructing three-dimensional volumes from tilt series of electron micrographs of cells preserved in their native states by vitrification. Resolutions of 5-8 nm have already been achieved and the prospects for further improvement are good. Since many intracellular activities are conducted by complexes in the megadalton range with dimensions of 20-50 nm, current resolutions should suffice to identify many of them in tomograms. However, residual noise and the dense packing of cellular constituents hamper interpretation. Recently, tomographic data have been collected on vitrified eukaryotic cells (Medalia et al., Science (2002) in press). Their cytoplasm was found to be markedly less crowded than in the prokaryotes previously studied, in accord with differences in crowding between prokaryotic and eukaryotic cells documented by other (indirect) biophysical methods. The implications of this observation are twofold. First, complexes should be more easily identifiable in tomograms of eukaryotic cytoplasm. This applies both to recognizing known complexes and characterizing novel complexes. An example of the latter--a 5-fold symmetric particle is--given. Second, electron cryotomography offers an incisive probe to examine crowding in different cellular compartments.}, Author = {Grunewald, K and Medalia, O and Gross, A and Steven, A C and Baumeister, W}, Date-Added = {2008-04-22 18:45:08 -0700}, Date-Modified = {2008-05-29 17:22:18 -0700}, Journal = {Biophys Chem}, Keywords = {Electron tomography; Macromolecular crowding; Eukaryote/prokaryote distinction; Vitrification}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Grunewald/2003.pdf}, Number = {1--3}, Pages = {577--591}, Title = {Prospects of electron cryotomography to visualize macromolecular complexes inside cellular compartments: implications of crowding}, Title1 = {Special Issue in honor of John T. Edsall (1902-2002)}, Ty = {JOUR}, Volume = {100}, Year = {2003}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://www.sciencedirect.com/science/article/B6TFB-484CSNK-19/2/4d03f0843b4ca2555b89a44ed5d795f2}} @article{Bartesaghi:2005ck, Abstract = {Electron tomography allows for the determination of the three-dimensional structures of cells and tissues at resolutions significantly higher than that which is possible with optical microscopy. Electron tomograms contain, in principle, vast amounts of information on the locations and architectures of large numbers of subcellular assemblies and organelles. The development of reliable quantitative approaches for the analysis of features in tomograms is an important problem, and a challenging prospect due to the low signal-to-noise ratios that are inherent to biological electron microscopic images. This is, in part, a consequence of the tremendous complexity of biological specimens. We report on a new method for the automated segmentation of HIV particles and selected cellular compartments in electron tomograms recorded from fixed, plastic-embedded sections derived from HIV-infected human macrophages. Individual features in the tomogram are segmented using a novel robust algorithm that finds their boundaries as global minimal surfaces in a metric space defined by image features. The optimization is carried out in a transformed spherical domain with the center an interior point of the particle of interest, providing a proper setting for the fast and accurate minimization of the segmentation energy. This method provides tools for the semi-automated detection and statistical evaluation of HIV particles at different stages of assembly in the cells and presents opportunities for correlation with biochemical markers of HIV infection. The segmentation algorithm developed here forms the basis of the automated analysis of electron tomograms and will be especially useful given the rapid increases in the rate of data acquisition. It could also enable studies of much larger data sets, such as those which might be obtained from the tomographic analysis of HIV-infected cells from studies of large populations.}, Address = {Electrical and Computer Engineering Department, University of Minnesota, Minneapolis, MN 55455, USA. abarte@umn.edu}, Au = {Bartesaghi, A and Sapiro, G and Subramaniam, S}, Author = {Bartesaghi, A and Sapiro, G and Subramaniam, S}, Da = {20050929}, Date-Added = {2008-04-22 15:48:00 -0700}, Date-Modified = {2008-05-29 17:01:38 -0700}, Dcom = {20051027}, Edat = {2005/09/30 09:00}, Jid = {9886191}, Journal = {IEEE Trans Image Process}, Jt = {IEEE transactions on image processing : a publication of the IEEE Signal Processing Society}, Language = {eng}, Lr = {20061115}, Mh = {Algorithms; *Artificial Intelligence; Electrons/diagnostic use; HIV/*ultrastructure; Image Enhancement/*methods; Image Interpretation, Computer-Assisted/*methods; Imaging, Three-Dimensional/*methods; Microscopy, Electron, Scanning/*methods; Pattern Recognition, Automated/*methods; Reproducibility of Results; Sensitivity and Specificity; Tomography/*methods}, Mhda = {2005/10/28 09:00}, Mid = {NIHMS12604}, Number = {9}, Own = {NLM}, Pages = {1314--1323}, Pl = {United States}, Pmc = {PMC1698959}, Pmid = {16190467}, Pst = {ppublish}, Pt = {Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.}, Pubm = {Print}, Sb = {IM}, So = {IEEE Trans Image Process. 2005 Sep;14(9):1314-23.}, Stat = {MEDLINE}, Title = {An energy-based three-dimensional segmentation approach for the quantitative interpretation of electron tomograms.}, Volume = {14}, Year = {2005}} @book{Lodish:2000tv, Annote = {Includes bibliographical references and index}, Annote1 = {MODE OF ACCESS: World Wide Web: http://www.ncbi.nlm.nih.gov/books/bv.fcgi?call=bv.View..ShowTOC&rid=mcb.TOC}, Author = {Lodish, H and Berk, A and Zipursky, L S and Matsudaira, P and Baltimore, D and Darnell, J}, Date-Added = {2008-04-22 13:32:00 -0700}, Date-Modified = {2008-05-29 16:35:48 -0700}, Edition = {4th}, Publisher = {W.H. Freeman and Company}, Title = {Molecular Cell Biology}, Year = {2000}} @article{Zhong-can:1989yq, Author = {Zhong-can, O-Y and Helfrich, W }, Date-Added = {2008-04-17 17:05:53 -0700}, Date-Modified = {2008-05-29 16:53:33 -0700}, Journal = {Phys Rev A}, Month = {May}, Number = {10}, Numpages = {8}, Pages = {5280--5288}, Publisher = {American Physical Society}, Title = {Bending energy of vesicle membranes: General expressions for the first, second, and third variation of the shape energy and applications to spheres and cylinders}, Volume = {39}, Year = {1989}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://dx.doi.org/10.1103/PhysRevA.39.5280}} @article{Dong:2007la, Abstract = { The basic physical properties of homogeneous membranes are relatively well known, while the effects of inhomogeneities with membranes are very much an active field of study. In this paper, a biphasic lipid vesicle with membrane embedded proteins is investigated. To take into account the influences of the proteins, a simple phenomenological coupling between the local fraction of proteins and the mean curvature square is suggested. By minimizing the energy of system, the E-L equations and boundary conditions are obtained and solved analytically for vesicle with a simple shape. Besides, stability phase diagrams and stability factor are put forward by linear perturbation analysis. Our results show two different situations which are strongly dependent on the nature of the proteins: a regime of easy instability when the proteins are strongly coupled to the membrane and a regime of difficult instability.}, Author = {Dong, Ni and Huiji, Shi and Yajun, Yin and Lisha, Niu}, Date-Added = {2008-04-02 09:18:27 -0700}, Date-Modified = {2008-04-02 09:28:21 -0700}, Group = {Biomembranes; IBID}, Journal = {Journal of Biomechanics}, Keywords = {Inhomogeneous; Biphasic; Lipid vesicle; Stability}, Number = {7}, Pages = {1512--1517}, Title = {Stability of biphasic vesicles with membrane embedded proteins}, Ty = {JOUR}, Url = {http://www.sciencedirect.com/science/article/B6T82-4KNMB8C-1/2/38418da2c45065f01e0b697d5f6b93ed}, Volume = {40}, Year = {2007}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://www.sciencedirect.com/science/article/B6T82-4KNMB8C-1/2/38418da2c45065f01e0b697d5f6b93ed}} @article{Smith:1996rt, Abstract = {Single molecules of double-stranded DNA (dsDNA) were stretched with force-measuring laser tweezers. Under a longitudinal stress of approximately 65 piconewtons (pN), dsDNA molecules in aqueous buffer undergo a highly cooperative transition into a stable form with 5.8 angstroms rise per base pair, that is, 70% longer than B form dsDNA. When the stress was relaxed below 65 pN, the molecules rapidly and reversibly contracted to their normal contour lengths. This transition was affected by changes in the ionic strength of the medium and the water activity or by cross-linking of the two strands of dsDNA. Individual molecules of single-stranded DNA were also stretched giving a persistence length of 7.5 angstroms and a stretch modulus of 800 pN. The overstretched form may play a significant role in the energetics of DNA recombination.}, Address = {Institute of Molecular Biology, University of Oregon, Eugene 97403, USA.}, Au = {Smith, SB and Cui, Y and Bustamante, C}, Author = {Smith, S B and Cui, Y and Bustamante, C}, Da = {19960625}, Date-Added = {2008-02-21 13:34:11 -0800}, Date-Modified = {2008-02-21 13:34:24 -0800}, Dcom = {19960625}, Edat = {1996/02/09}, Gr = {GM-32543/GM/United States NIGMS}, Group = {Back Focal Plane}, Issn = {0036-8075 (Print)}, Jid = {0404511}, Journal = {Science}, Jt = {Science (New York, N.Y.)}, Language = {eng}, Lr = {20071114}, Mh = {Base Composition; Chemistry, Physical; DNA/*chemistry; DNA, Single-Stranded/*chemistry; Elasticity; *Nucleic Acid Conformation; Osmolar Concentration; Thermodynamics}, Mhda = {1996/02/09 00:01}, Number = {5250}, Own = {NLM}, Pages = {795--799}, Pl = {UNITED STATES}, Pmid = {8628994}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.}, Pubm = {Print}, Rn = {0 (DNA, Single-Stranded); 9007-49-2 (DNA)}, Sb = {IM}, So = {Science. 1996 Feb 9;271(5250):795-9. }, Stat = {MEDLINE}, Title = {Overstretching B-DNA: the elastic response of individual double-stranded and single-stranded DNA molecules}, Volume = {271}, Year = {1996}, Bdsk-File-1 = {YnBsaXN0MDDUAQIDBAUGCQpYJHZlcnNpb25UJHRvcFkkYXJjaGl2ZXJYJG9iamVjdHMSAAGGoNEHCFRyb290gAFfEA9OU0tleWVkQXJjaGl2ZXKoCwwXGBkdJCVVJG51bGzTDQ4PEBEUViRjbGFzc1dOUy5rZXlzWk5TLm9iamVjdHOAB6ISE4ACgAOiFRaABIAGWWFsaWFzRGF0YVxyZWxhdGl2ZVBhdGjSDRobHFdOUy5kYXRhgAVPEQGKAAAAAAGKAAIAAANoc3IAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAADBcRzJSCsAAABGbRcIMTk5Ni5wZGYAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAT5fdsPjJ70AAAAAAAAAAAAEAAMAAAkgAAAAAAAAAAAAAAAAAAAABVNtaXRoAAAQAAgAAMFxjUkAAAARAAgAAMPjmD0AAAABABgARm0XAEZrzwBGatUARmobAEZkaABAiUMAAgBAaHNyOlVzZXJzOmF0b21pY3BpcmF0ZTpEb2N1bWVudHM6Q2FsdGVjaDpBcnRpY2xlczpTbWl0aDoxOTk2LnBkZgAOABIACAAxADkAOQA2AC4AcABkAGYADwAIAAMAaABzAHIAEgA8VXNlcnMvYXRvbWljcGlyYXRlL0RvY3VtZW50cy9DYWx0ZWNoL0FydGljbGVzL1NtaXRoLzE5OTYucGRmABMAAS8AABUAAgAT//8AANIeHyAhWCRjbGFzc2VzWiRjbGFzc25hbWWjISIjXU5TTXV0YWJsZURhdGFWTlNEYXRhWE5TT2JqZWN0XxAjLi4vLi4vLi4vLi4vQXJ0aWNsZXMvU21pdGgvMTk5Ni5wZGbSHh8mJ6InI1xOU0RpY3Rpb25hcnkACAARABoAHwApADIANwA6AD8AQQBTAFwAYgBpAHAAeACDAIUAiACKAIwAjwCRAJMAnQCqAK8AtwC5AkcCTAJVAmACZAJyAnkCggKoAq0CsAAAAAAAAAIBAAAAAAAAACgAAAAAAAAAAAAAAAAAAAK9}} @article{Ghislain:1994vf, Author = {Lucien P. Ghislain and Neil A. Switz and Watt W. Webb}, Date-Added = {2008-02-21 12:00:05 -0800}, Date-Modified = {2008-02-21 12:01:02 -0800}, Doi = {10.1063/1.1144613}, Group = {Back Focal Plane}, Journal = {Review of Scientific Instruments}, Keywords = {MICROSPHERES; FORCES; TRAPPING; LASER BEAMS; EFFICIENCY; POLYSTYRENE; SENSORS; SPATIAL RESOLUTION}, Number = {9}, Pages = {2762-2768}, Publisher = {AIP}, Title = {Measurement of small forces using an optical trap}, Url = {http://link.aip.org/link/?RSI/65/2762/1}, Volume = {65}, Year = {1994}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://link.aip.org/link/?RSI/65/2762/1}, Bdsk-Url-2 = {http://dx.doi.org/10.1063/1.1144613}} @article{Visscher:1996qa, Abstract = {We describe the design and construction of two different types of multiple-beam optical tweezers, each equipped with nanometer-resolution position detectors. Multiple optical traps can be created either by splitting a laser beam in two parts, based on its polarization, or time-sharing a single beam among several different locations. The advantages and disadvantages of optical tweezers based on either scheme are discussed, along with details of specific implementations. Various ways to detect microscopic movements of an optically trapped object are presented and compared, including designs that are relatively insensitive to absolute location of a trapped particle within the field of view. Two of many possible applications for such instruments are illustrated: the detection of molecular steps by kinesin motor molecules, and determinations of the stiffness of single microtubules }, Author = {Visscher, K and Gross, S P and Block, S M}, Date-Added = {2008-02-21 11:56:49 -0800}, Date-Modified = {2008-05-29 16:51:17 -0700}, Group = {Back Focal Plane}, Journal = {IEEE J Sel Top Quant}, Keywords = {biological techniques, laser beams, light polarisation, molecular biophysics, optical focusing, proteins, radiation pressureconstruction, design, field of view, kinesin motor molecules, laser beam splitting, microscopic movements, molecular step detection, multiple-beam optical traps, multiple-beam optical tweezers, nanometer-resolution position detectors, nanometer-resolution position sensing, optically trapped object, polarization, single beam, single microtubule stiffness, time-sharing, trapped particle}, Number = {4}, Pages = {1066--1076}, Title = {Construction of multiple-beam optical traps with nanometer-resolution position sensing}, Volume = {2}, Year = {Dec 1996}, Bdsk-File-1 = {YnBsaXN0MDDUAQIDBAUGCQpYJHZlcnNpb25UJHRvcFkkYXJjaGl2ZXJYJG9iamVjdHMSAAGGoNEHCFRyb290gAFfEA9OU0tleWVkQXJjaGl2ZXKoCwwXGBkdJCVVJG51bGzTDQ4PEBEUViRjbGFzc1dOUy5rZXlzWk5TLm9iamVjdHOAB6ISE4ACgAOiFRaABIAGWWFsaWFzRGF0YVxyZWxhdGl2ZVBhdGjSDRobHFdOUy5kYXRhgAVPEQGUAAAAAAGUAAIAAANoc3IAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAADBcRzJSCsAAAE+NnkIMTk5Ni5wZGYAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAT4zGsPjEvtQREYgQ0FSTwAEAAMAAAkgAAAAAAAAAAAAAAAAAAAACFZpc3NjaGVyABAACAAAwXGNSQAAABEACAAAw+ODewAAAAEAGAE+NnkARmvPAEZq1QBGahsARmRoAECJQwACAENoc3I6VXNlcnM6YXRvbWljcGlyYXRlOkRvY3VtZW50czpDYWx0ZWNoOkFydGljbGVzOlZpc3NjaGVyOjE5OTYucGRmAAAOABIACAAxADkAOQA2AC4AcABkAGYADwAIAAMAaABzAHIAEgA/VXNlcnMvYXRvbWljcGlyYXRlL0RvY3VtZW50cy9DYWx0ZWNoL0FydGljbGVzL1Zpc3NjaGVyLzE5OTYucGRmAAATAAEvAAAVAAIAE///AADSHh8gIVgkY2xhc3Nlc1okY2xhc3NuYW1loyEiI11OU011dGFibGVEYXRhVk5TRGF0YVhOU09iamVjdF8QJi4uLy4uLy4uLy4uL0FydGljbGVzL1Zpc3NjaGVyLzE5OTYucGRm0h4fJieiJyNcTlNEaWN0aW9uYXJ5AAgAEQAaAB8AKQAyADcAOgA/AEEAUwBcAGIAaQBwAHgAgwCFAIgAigCMAI8AkQCTAJ0AqgCvALcAuQJRAlYCXwJqAm4CfAKDAowCtQK6Ar0AAAAAAAACAQAAAAAAAAAoAAAAAAAAAAAAAAAAAAACyg==}, Bdsk-Url-1 = {http://dx.doi.org/10.1109/2944.577338}} @article{Gittes:1998ph, Abstract = {The lateral position of an optically trapped object in a microscope can be monitored with a quadrant photodiode to within nanometers or better by measurement of intensity shifts in the back focal plane of the lens that is collimating the outgoing laser light. This detection is largely independent of the position of the trap in the field of view. We provide a model for the essential mechanism of this type of detection, giving a simple, closed-form analytic solution with simplifying assumptions. We identify intensity shifts as first-order far-field interference between the outgoing laser beam and scattered light from the trapped particle, where the latter is phase advanced owing to the Gouy phase anomaly. This interference also reflects momentum transfer to the particle, giving the spring constant of the trap. Our response formula is compared with the results of experiments.}, Au = {Gittes, F and Schmidt, CF}, Author = {Gittes, F and Schmidt, C F}, Da = {20071217}, Date-Added = {2008-02-21 11:53:34 -0800}, Date-Modified = {2008-02-21 12:01:54 -0800}, Edat = {2007/12/18 09:00}, Group = {Back Focal Plane}, Issn = {0146-9592 (Print)}, Jid = {7708433}, Journal = {Opt Lett}, Jt = {Optics letters}, Language = {eng}, Mhda = {2007/12/18 09:00}, Number = {1}, Own = {NLM}, Pages = {7--9}, Pii = {36510}, Pl = {United States}, Pmid = {18084394}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print}, So = {Opt Lett. 1998 Jan 1;23(1):7-9. }, Stat = {In-Data-Review}, Title = {Interference model for back-focal-plane displacement detection in optical tweezers}, Volume = {23}, Year = {1998}, Bdsk-File-1 = {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}} @article{Ghislain:93, Author = {Lucien P. Ghislain and Watt W. Webb}, Date-Added = {2008-02-21 11:52:39 -0800}, Date-Modified = {2008-02-21 12:01:30 -0800}, Group = {Back Focal Plane}, Journal = {Opt. Lett.}, Number = {19}, Pages = {1678}, Publisher = {OSA}, Title = {Scanning-force microscope based on an optical trap}, Url = {http://ol.osa.org/abstract.cfm?URI=ol-18-19-1678}, Volume = {18}, Year = {1993}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://ol.osa.org/abstract.cfm?URI=ol-18-19-1678}} @article{Svoboda:1994la, Abstract = {We measured the force-velocity curves of single kinesin molecules attached to silica beads moving in an in vitro motility assay. Optical trapping interferometry was used to track movement with subnanometer precision and to apply calibrated, pN-sized forces to the beads. Velocity decreased linearly with increasing force, and kinesin molecules moved against applied loads of up to 5-6 pN. Comparison of force-velocity curves at limiting and saturating ATP concentrations suggests that the load-dependent diminution in kinesin velocity may be due to a decrease in the net displacement per molecule of ATP hydrolyzed, not simply to a slowing of the ATP turnover rate; kinesin would therefore appear to be a loosely coupled motor.}, Address = {Rowland Institute for Science, Cambridge, Massachusetts 02142.}, Au = {Svoboda, K and Block, SM}, Author = {Svoboda, K and Block, S M}, Da = {19940711}, Date-Added = {2008-02-21 11:52:27 -0800}, Date-Modified = {2008-02-21 12:01:19 -0800}, Dcom = {19940711}, Edat = {1994/06/03}, Group = {Back Focal Plane}, Issn = {0092-8674 (Print)}, Jid = {0413066}, Journal = {Cell}, Jt = {Cell}, Language = {eng}, Lr = {20061115}, Mh = {Adenosine Triphosphate/metabolism; Animals; Biomechanics; Hydrolysis; Interferometry; Kinesin/chemistry/*metabolism; Kinetics; Silicon Dioxide; Thermodynamics}, Mhda = {1994/06/03 00:01}, Number = {5}, Own = {NLM}, Pages = {773--784}, Pii = {0092-8674(94)90060-4}, Pl = {UNITED STATES}, Pmid = {8205624}, Pst = {ppublish}, Pt = {Comparative Study; In Vitro; Journal Article; Research Support, Non-U.S. Gov't}, Pubm = {Print}, Rn = {56-65-5 (Adenosine Triphosphate); 7631-86-9 (Silicon Dioxide); EC 3.6.1.- (Kinesin)}, Sb = {IM}, So = {Cell. 1994 Jun 3;77(5):773-84.}, Stat = {MEDLINE}, Title = {Force and velocity measured for single kinesin molecules.}, Volume = {77}, Year = {1994}, Bdsk-File-1 = {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}} @article{Engelman:2005nx, Annote = {10.1038/nature04394}, Author = {Engelman, Donald M. }, Date-Added = {2008-02-05 11:50:50 -0800}, Date-Modified = {2008-02-05 11:50:50 -0800}, Isbn = {0028-0836}, Journal = {Nature}, M3 = {10.1038/nature04394}, Number = {7068}, Pages = {578--580}, Title = {Membranes are more mosaic than fluid}, Ty = {JOUR}, Url = {http://dx.doi.org/10.1038/nature04394}, Volume = {438}, Year = {2005}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://dx.doi.org/10.1038/nature04394}} @article{Kusumi:2005ly, Abstract = {Recent advancements in single-molecule tracking methods with nanometer-level precision now allow researchers to observe the movement, recruitment, and activation of single molecules in the plasma membrane in living cells. In particular, on the basis of the observations by high-speed single-particle tracking at a frame rate of 40,000 frames s(1), the partitioning of the fluid plasma membrane into submicron compartments throughout the cell membrane and the hop diffusion of virtually all the molecules have been proposed. This could explain why the diffusion coefficients in the plasma membrane are considerably smaller than those in artificial membranes, and why the diffusion coefficient is reduced upon molecular complex formation (oligomerization-induced trapping). In this review, we first describe the high-speed single-molecule tracking methods, and then we critically review a new model of a partitioned fluid plasma membrane and the involvement of the actin-based membrane-skeleton "fences" and anchored-transmembrane protein "pickets" in the formation of compartment boundaries.}, Address = {Kusumi Membrane Organizer Project, Exploratory Research for Advanced Technology Organization, Department of Biological Science and Institute for Advanced Research, Nagoya University, Nagoya 464-8602, Japan. akusumi@bio.nagoya-u.ac.jp}, Au = {Kusumi, A and Nakada, C and Ritchie, K and Murase, K and Suzuki, K and Murakoshi, H and Kasai, RS and Kondo, J and Fujiwara, T}, Author = {Kusumi, A and Nakada, C and Ritchie, K and Murase, K and Suzuki, K and Murakoshi, H and Kasai, R S and Kondo, J and Fujiwara, T}, Da = {20050511}, Date-Added = {2008-02-05 11:47:20 -0800}, Date-Modified = {2008-05-29 16:47:34 -0700}, Dcom = {20050728}, Edat = {2005/05/05 09:00}, Jid = {9211097}, Journal = {Annu Rev Biophys Biomol Struct}, Jt = {Annual review of biophysics and biomolecular structure}, Language = {eng}, Lr = {20060417}, Mh = {Actins/chemistry; Biophysics/*methods; Cell Membrane/*metabolism; Cholesterol/metabolism; Cytoskeleton/metabolism; Diffusion; Lipid Metabolism; Liposomes/metabolism; Membranes, Artificial; Microscopy, Video/*methods; Models, Biological; Models, Molecular; Neurons/metabolism; Time Factors}, Mhda = {2005/07/29 09:00}, Own = {NLM}, Pages = {351--378}, Pl = {United States}, Pmid = {15869394}, Pst = {ppublish}, Pt = {Journal Article; Review}, Pubm = {Print}, Rf = {82}, Rn = {0 (Actins); 0 (Liposomes); 0 (Membranes, Artificial); 57-88-5 (Cholesterol)}, Sb = {IM}, So = {Annu Rev Biophys Biomol Struct. 2005;34:351-78.}, Stat = {MEDLINE}, Title = {Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: high-speed single-molecule tracking of membrane molecules.}, Volume = {34}, Year = {2005}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://dx.doi.org/10.1146/annurev.biophys.34.040204.144637}} @article{Singer:1972zr, Abstract = {A fluid mosaic model is presented for the gross organization and structure of the proteins and lipids of biological membranes. The model is consistent with the restrictions imposed by thermodynamics. In this model, the proteins that are integral to the membrane are a heterogeneous set of globular molecules, each arranged in an amphipathic structure, that is, with the ionic and highly polar groups protruding from the membrane into the aqueous phase, and the nonpolar groups largely buried in the hydrophobic interior of the membrane. These globular molecules are partially embedded in a matrix of phospholipid. The bulk of the phospholipid is organized as a discontinuous, fluid bilayer, although a small fraction of the lipid may interact specifically with the membrane proteins. The fluid mosaic structure is therefore formally analogous to a two-dimensional oriented solution of integral proteins (or lipoproteins) in the viscous phospholipid bilayer solvent. Recent experiments with a wide variety of techniqes and several different membrane systems are described, all of which abet consistent with, and add much detail to, the fluid mosaic model. It therefore seems appropriate to suggest possible mechanisms for various membrane functions and membrane-mediated phenomena in the light of the model. As examples, experimentally testable mechanisms are suggested for cell surface changes in malignant transformation, and for cooperative effects exhibited in the interactions of membranes with some specific ligands. Note added in proof: Since this article was written, we have obtained electron microscopic evidence (69) that the concanavalin A binding sites on the membranes of SV40 virus-transformed mouse fibroblasts (3T3 cells) are more clustered than the sites on the membranes of normal cells, as predicted by the hypothesis represented in Fig. 7B. T-here has also appeared a study by Taylor et al. (70) showing the remarkable effects produced on lymphocytes by the addition of antibodies directed to their surface immunoglobulin molecules. The antibodies induce a redistribution and pinocytosis of these surface immunoglobulins, so that within about 30 minutes at 37 degrees C the surface immunoglobulins are completely swept out of the membrane. These effects do not occur, however, if the bivalent antibodies are replaced by their univalent Fab fragments or if the antibody experiments are carried out at 0 degrees C instead of 37 degrees C. These and related results strongly indicate that the bivalent antibodies produce an aggregation of the surface immunoglobulin molecules in the plane of the membrane, which can occur only if the immunoglobulin molecules are free to diffuse in the membrane. This aggregation then appears to trigger off the pinocytosis of the membrane components by some unknown mechanism. Such membrane transformations may be of crucial importance in the induction of an antibody response to an antigen, as well as iv other processes of cell differentiation.}, Au = {Singer, SJ and Nicolson, GL}, Author = {Singer, S J and Nicolson, G L}, Da = {19720411}, Date-Added = {2008-02-05 11:31:22 -0800}, Date-Modified = {2008-05-29 16:46:45 -0700}, Dcom = {19720411}, Edat = {1972/02/18}, Jid = {0404511}, Journal = {Science}, Jt = {Science (New York, N.Y.)}, Language = {eng}, Lr = {20070817}, Mh = {Agglutination; Amino Acid Sequence; Animals; Antigen-Antibody Reactions; Anura; Binding Sites; Biological Transport, Active; Calorimetry; Cell Membrane/*analysis/metabolism; Electron Spin Resonance Spectroscopy; Freeze Etching; Hemolysis; Humans; Lectins/pharmacology; Microscopy, Electron; Models, Structural; Oligosaccharides/*analysis; Phospholipids/*analysis; Protein Binding; Protein Conformation; Proteins/*analysis; Rabbits; Thermodynamics; X-Ray Diffraction}, Mhda = {1972/02/18 00:01}, Number = {23}, Own = {NLM}, Pages = {720--731}, Pl = {UNITED STATES}, Pmid = {4333397}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print}, Rn = {0 (Lectins); 0 (Oligosaccharides); 0 (Phospholipids); 0 (Proteins)}, Sb = {IM}, So = {Science. 1972 Feb 18;175(23):720-31.}, Stat = {MEDLINE}, Title = {The fluid mosaic model of the structure of cell membranes}, Volume = {175}, Year = {1972}} @article{Harlow:2001kx, Abstract = {Active zone material at the nervous system's synapses is situated next to synaptic vesicles that are docked at the presynaptic plasma membrane, and calcium channels that are anchored in the membrane. Here we use electron microscope tomography to show the arrangement and associations of structural components of this compact organelle at a model synapse, the frog's neuromuscular junction. Our findings indicate that the active zone material helps to dock the vesicles and anchor the channels, and that its architecture provides both a particular spatial relationship and a structural linkage between them. The structural linkage may include proteins that mediate the calcium-triggered exocytosis of neurotransmitter by the synaptic vesicles during synaptic transmission.}, Address = {Department of Neurobiology, Stanford University School of Medicine, California 94305, USA.}, Au = {Harlow, ML and Ress, D and Stoschek, A and Marshall, RM and McMahan, UJ}, Author = {Harlow, M L and Ress, D and Stoschek, A and Marshall, R M and McMahan, U J}, Da = {20010205}, Date-Added = {2008-02-01 11:46:49 -0800}, Date-Modified = {2008-05-29 16:34:40 -0700}, Dcom = {20010215}, Edat = {2001/02/24 12:00}, Jid = {0410462}, Journal = {Nature}, Jt = {Nature}, Language = {eng}, Lr = {20061115}, Mh = {Animals; Calcium Channels/physiology; Image Enhancement; Membrane Proteins/physiology/ultrastructure; Nerve Tissue Proteins/physiology/ultrastructure; Neuromuscular Junction/physiology/*ultrastructure; Organelles/physiology/ultrastructure; Presynaptic Terminals/physiology/ultrastructure; Rana pipiens; Synaptic Membranes/physiology/ultrastructure; Synaptic Vesicles/physiology/ultrastructure}, Mhda = {2001/03/03 10:01}, Number = {6819}, Own = {NLM}, Pages = {479--484}, Phst = {2000/09/14 {$[$}received{$]$}; 2000/11/24 {$[$}accepted{$]$}}, Pii = {35054000}, Pl = {England}, Pmid = {11206537}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.}, Pubm = {Print}, Rn = {0 (Calcium Channels); 0 (Membrane Proteins); 0 (Nerve Tissue Proteins)}, Sb = {IM}, So = {Nature. 2001 Jan 25;409(6819):479-84.}, Stat = {MEDLINE}, Title = {The architecture of active zone material at the frog's neuromuscular junction}, Volume = {409}, Year = {2001}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://dx.doi.org/10.1038/35054000}} @article{Gerlich:2001eu, Abstract = {Live-cell imaging technology using fluorescent proteins (green fluorescent protein and its homologues) has revolutionized the study of cellular dynamics. But tools that can quantitatively analyse complex spatiotemporal processes in live cells remain lacking. Here we describe a new technique--fast multi-colour four-dimensional imaging combined with automated and quantitative time-space reconstruction--to fill this gap. As a proof of principle, we apply this method to study the re-formation of the nuclear envelope in live cells. Four-dimensional imaging of three spectrally distinct fluorescent proteins is used to simultaneously visualize three different cellular compartments at high speed and with high spatial resolution. The highly complex data, comprising several thousand images from a single cell, were quantitatively reconstructed in time-space by software developed in-house. This analysis reveals quantitative and qualitative insights into the highly ordered topology of nuclear envelope formation, in correlation with chromatin expansion - results that would have been impossible to achieve by manual inspection alone. Our new technique will greatly facilitate study of the highly ordered dynamic architecture of eukaryotic cells.}, Address = {Intelligent Bioinformatics Systems Department, German Cancer Research Centre, 69120 Heidelberg, Germany.}, Au = {Gerlich, D and Beaudouin, J and Gebhard, M and Ellenberg, J and Eils, R}, Author = {Gerlich, D and Beaudouin, J and Gebhard, M and Ellenberg, J and Eils, R}, Da = {20010904}, Date-Added = {2008-01-31 09:05:43 -0500}, Date-Modified = {2008-01-31 09:05:43 -0500}, Dcom = {20011018}, Doi = {10.1038/ncb0901-852}, Edat = {2001/09/05 10:00}, Issn = {1465-7392 (Print)}, Jid = {100890575}, Journal = {Nat Cell Biol}, Jt = {Nature cell biology}, Language = {eng}, Lr = {20061115}, Mh = {Animals; Bacterial Proteins/analysis/genetics; Cell Line; Chromatin/*ultrastructure; *Image Processing, Computer-Assisted; Luminescent Proteins/*analysis/genetics; Microscopy, Fluorescence; Models, Structural; Nuclear Envelope/*ultrastructure; Rats; Recombinant Proteins/analysis; Time Factors; Transfection; Tubulin/analysis/genetics}, Mhda = {2001/10/19 10:01}, Number = {9}, Own = {NLM}, Pages = {852--855}, Pii = {ncb0901-852}, Pl = {England}, Pmid = {11533667}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't}, Pubm = {Print}, Rn = {0 (Bacterial Proteins); 0 (Chromatin); 0 (Luminescent Proteins); 0 (Recombinant Proteins); 0 (Tubulin); 0 (red fluorescent protein); 0 (yellow fluorescent protein, Bacteria)}, Sb = {IM}, So = {Nat Cell Biol. 2001 Sep;3(9):852-5.}, Stat = {MEDLINE}, Title = {Four-dimensional imaging and quantitative reconstruction to analyse complex spatiotemporal processes in live cells.}, Volume = {3}, Year = {2001}, Bdsk-Url-1 = {http://dx.doi.org/10.1038/ncb0901-852}} @article{Fertuck:1974nx, Abstract = {Exposed sternomastoid muscles of anaesthetized mice were bathed in (125)I-labeled alpha-bungarotoxin until all neurally evoked muscle contractions were eliminated. The distribution of label was then determined by electron microscope autoradiography. It was found that the label was localized at the top of the junctional folds, i.e., at the postjunctional membrane nearest the axon. Since the alpha-bungarotoxin had fully eliminated the physiological muscle response, these results indicate that the active acetylcholine receptor occupies a limited area of the junctional folds and is not distributed uniformly throughout this membrane. Specialized membrane densities seem to coincide with the labeled regions.}, Au = {Fertuck, HC and Salpeter, MM}, Author = {Fertuck, H C and Salpeter, M M}, Da = {19740731}, Date-Added = {2008-01-30 13:42:40 -0500}, Date-Modified = {2008-05-30 02:52:40 -0700}, Dcom = {19740731}, Edat = {1974/04/01}, Jid = {7505876}, Journal = {Proc Natl Acad Sci USA}, Jt = {Proceedings of the National Academy of Sciences of the United States of America}, Language = {eng}, Lr = {20070419}, Mh = {Animals; Autoradiography; Binding Sites; Bungarotoxins/*metabolism; Iodine Radioisotopes; Mice; Microscopy, Electron; Neuromuscular Junction/cytology/*metabolism; *Receptors, Cholinergic}, Mhda = {1974/04/01 00:01}, Number = {4}, Own = {NLM}, Pages = {1376--1378}, Pl = {UNITED STATES}, Pmid = {4524643}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print}, Rn = {0 (Bungarotoxins); 0 (Iodine Radioisotopes); 0 (Receptors, Cholinergic)}, Sb = {IM}, So = {Proc Natl Acad Sci U S A. 1974 Apr;71(4):1376-8.}, Stat = {MEDLINE}, Title = {Localization of acetylcholine receptor by {125I}-labeled alpha-bungarotoxin binding at mouse motor endplates}, Volume = {71}, Year = {1974}} @article{Koster:2003qd, Abstract = {The tubular morphology of intracellular membranous compartments is actively maintained through interactions with motor proteins and the cytoskeleton. Moving along cytoskeletal elements, motor proteins exert forces on the membranes to which they are attached, resulting in the formation of membrane tubes and tubular networks. To study the formation of membrane tubes by motor proteins, we developed an in vitro assay consisting of purified kinesin proteins directly linked to the lipids of giant unilamellar vesicles. When the vesicles are brought into contact with a network of immobilized microtubules, membrane tubes and tubular networks are formed. Through systematic variation of the kinesin concentration and membrane composition we study the mechanism involved. We show that a threshold concentration of motor proteins is needed and that a low membrane tension facilitates tube formation. Forces involved in tube formation were measured directly with optical tweezers and are shown to depend only on the tension and bending rigidity of the membrane. The forces were found to be higher than can be generated by individual motor proteins, indicating that multiple motors were working together to pull tubes. We propose a simple mechanism by which individual motor proteins can dynamically associate into clusters that provide the force needed for the formation of tubes, explaining why, in contrast to earlier findings [Roux, A., Cappello, G., Cartaud, J., Prost, J., Goud, B. & Bassereau, P. (2002) Proc. Natl. Acad. Sci. USA 99, 5394-5399], motor proteins do not need to be physically linked to each other to be able to pull tubes.}, Address = {Institute for Atomic and Molecular Physics, Foundation for Fundamental Research on Matter, Kruislaan 407, 1098 SJ, Amsterdam, The Netherlands.}, Au = {Koster, G and VanDuijn, M and Hofs, B and Dogterom, M}, Author = {Koster, G and VanDuijn, M and Hofs, B and Dogterom, M}, Da = {20031224}, Date-Added = {2008-01-30 12:32:23 -0500}, Date-Modified = {2008-05-30 02:52:59 -0700}, Dcom = {20040420}, Dep = {20031208}, Edat = {2003/12/10 05:00}, Jid = {7505876}, Journal = {Proc Natl Acad Sci USA}, Jt = {Proceedings of the National Academy of Sciences of the United States of America}, Language = {eng}, Lr = {20061115}, Mh = {Cell Membrane/*ultrastructure; Cytoskeleton/physiology/*ultrastructure; Lipid Bilayers/*chemistry; Models, Biological; Organelles/ultrastructure; Stress, Mechanical; Tubulin/*chemistry/ultrastructure}, Mhda = {2004/04/21 05:00}, Number = {26}, Own = {NLM}, Pages = {15583--15588}, Phst = {2003/12/08 {$[$}aheadofprint{$]$}}, Pii = {2531786100}, Pl = {United States}, Pmid = {14663143}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't}, Pubm = {Print-Electronic}, Rn = {0 (Lipid Bilayers); 0 (Tubulin)}, Sb = {IM}, So = {Proc Natl Acad Sci U S A. 2003 Dec 23;100(26):15583-8. Epub 2003 Dec 8.}, Stat = {MEDLINE}, Title = {Membrane tube formation from giant vesicles by dynamic association of motor proteins}, Volume = {100}, Year = {2003}, Bdsk-Url-1 = {http://dx.doi.org/10.1073/pnas.2531786100}} @article{Waterman-Storer:1999hl, Abstract = {Microtubules are involved in actin-based protrusion at the leading-edge lamellipodia of migrating fibroblasts. Here we show that the growth of microtubules induced in fibroblasts by removal of the microtubule destabilizer nocodazole activates Rac1 GTPase, leading to the polymerization of actin in lamellipodial protrusions. Lamellipodial protrusions are also activated by the rapid growth of a disorganized array of very short microtubules induced by the microtubule-stabilizing drug taxol. Thus, neither microtubule shortening nor long-range microtubule-based intracellular transport is required for activating protrusion. We suggest that the growth phase of microtubule dynamic instability at leading-edge lamellipodia locally activates Rac1 to drive actin polymerization and lamellipodial protrusion required for cell migration.}, Address = {Department of Biology, University of North Carolina, Chapel Hill 27599, USA. waterman@email.unc.edu}, Au = {Waterman-Storer, CM and Worthylake, RA and Liu, BP and Burridge, K and Salmon, ED}, Author = {Waterman-Storer, C M and Worthylake, R A and Liu, B P and Burridge, K and Salmon, E D}, Cin = {Nat Cell Biol. 1999 May;1(1):E12. PMID: 10559874}, Da = {19991207}, Date-Added = {2008-01-30 12:25:28 -0500}, Date-Modified = {2008-05-29 16:29:06 -0700}, Dcom = {19991207}, Edat = {1999/11/13 09:00}, Jid = {100890575}, Journal = {Nat Cell Biol}, Jt = {Nature cell biology}, Language = {eng}, Lr = {20061115}, Mh = {3T3 Cells/drug effects/physiology/ultrastructure; Actins/metabolism; Animals; Cell Movement/physiology; Kinetics; Mice; Microtubules/drug effects/*physiology/ultrastructure; Nocodazole/pharmacology; Paclitaxel/pharmacology; rac1 GTP-Binding Protein/*metabolism}, Mhda = {2001/03/23 10:01}, Number = {1}, Own = {NLM}, Pages = {45--50}, Pl = {ENGLAND}, Pmid = {10559863}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.}, Pubm = {Print}, Rn = {0 (Actins); 31430-18-9 (Nocodazole); 33069-62-4 (Paclitaxel); EC 3.6.5.2 (rac1 GTP-Binding Protein)}, Sb = {IM}, So = {Nat Cell Biol. 1999 May;1(1):45-50.}, Stat = {MEDLINE}, Title = {Microtubule growth activates {Rac1} to promote lamellipodial protrusion in fibroblasts}, Volume = {1}, Year = {1999}, Bdsk-Url-1 = {http://dx.doi.org/10.1038/9018}} @article{Razani:2001fp, Address = {Department of Molecular Pharmacology, The Albert Einstein Cancer Center, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, USA.}, Au = {Razani, B and Lisanti, MP}, Author = {Razani, B and Lisanti, M P}, Da = {20011107}, Date-Added = {2008-01-30 12:18:00 -0500}, Date-Modified = {2008-05-29 16:31:23 -0700}, Dcom = {20011227}, Edat = {2001/11/08 10:00}, Gr = {T32-GM07288/GM/United States NIGMS}, Jid = {0373226}, Journal = {Exp Cell Res}, Jt = {Experimental cell research}, Language = {eng}, Lr = {20071114}, Mh = {Animals; Caveolae/*metabolism; Caveolins/genetics/*metabolism; Cholesterol/metabolism; Endocytosis/physiology; Exocytosis/physiology; Membrane Microdomains/chemistry/metabolism; Models, Biological; Signal Transduction/physiology; Transport Vesicles/metabolism}, Mhda = {2002/01/05 10:01}, Number = {1}, Own = {NLM}, Pages = {36--44}, Pii = {S0014-4827(01)95372-8}, Pl = {United States}, Pmid = {11697880}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.; Review}, Pubm = {Print}, Rf = {79}, Rn = {0 (Caveolins); 57-88-5 (Cholesterol)}, Sb = {IM}, So = {Exp Cell Res. 2001 Nov 15;271(1):36-44.}, Stat = {MEDLINE}, Title = {Caveolins and caveol\ae: molecular and functional relationships.}, Volume = {271}, Year = {2001}, Bdsk-Url-1 = {http://dx.doi.org/10.1006/excr.2001.5372}} @article{Antonny:2003db, Abstract = {The small G-protein Sar1 and the cytosolic complexes Sec23/24 and Sec13/31 associate sequentially on endoplasmic reticulum membranes to form a protein coat named COPII, which drives the formation of transport vesicles. Using dynamic light scattering, we show that Sec23/24 and Sec13/31 can self-assemble in a stoichiometric manner in solution to form particles with hydrodynamic radii in the range of 40-60 nm. Self-assembly is favoured by lowering the pH, the ionic strength and/or the temperature. Electron microscopy reveals the formation of spherical particles 60-120 nm in diameter with a tight, rough mesh on their surfaces. We suggest that these structures, which represent a minimal COPII cage, mimic the molecular organization of the membrane-associated COPII coat.}, Address = {Institut de Pharmacologie Moleculaire et Cellulaire, CNRS, Valbonne, France. antonny@ipmc.cnrs.fr}, Au = {Antonny, B and Gounon, P and Schekman, R and Orci, L}, Author = {Antonny, B and Gounon, P and Schekman, R and Orci, L}, Da = {20030402}, Date-Added = {2008-01-30 12:18:00 -0500}, Date-Modified = {2008-05-29 16:30:44 -0700}, Dcom = {20030618}, Edat = {2003/04/03 05:00}, Jid = {100963049}, Journal = {EMBO Rep}, Jt = {EMBO reports}, Language = {eng}, Lr = {20061115}, Mh = {COP-Coated Vesicles/*metabolism/*ultrastructure; Carrier Proteins/metabolism/ultrastructure; Clathrin/metabolism/ultrastructure; Kinetics; Light; Membrane Proteins/metabolism/ultrastructure; Microscopy, Electron; Nuclear Pore Complex Proteins; Phospholipid Transfer Proteins; Saccharomyces cerevisiae Proteins/metabolism/ultrastructure; Scattering, Radiation}, Mhda = {2003/06/19 05:00}, Number = {4}, Own = {NLM}, Pages = {419--424}, Phst = {2003/01/24 {$[$}received{$]$}; 2003/02/26 {$[$}revised{$]$}; 2003/02/27 {$[$}accepted{$]$}}, Pii = {embor812}, Pl = {England}, Pmid = {12671686}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't}, Pubm = {Print}, Rn = {0 (Carrier Proteins); 0 (Clathrin); 0 (Membrane Proteins); 0 (Nuclear Pore Complex Proteins); 0 (Phospholipid Transfer Proteins); 0 (SEC13 protein, S cerevisiae); 0 (SEC23 protein, S cerevisiae); 0 (SEC24 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins)}, Sb = {IM}, So = {EMBO Rep. 2003 Apr;4(4):419-24.}, Stat = {MEDLINE}, Title = {Self-assembly of minimal {COPII} cages}, Volume = {4}, Year = {2003}, Bdsk-Url-1 = {http://dx.doi.org/10.1038/sj.embor.embor812}} @article{Unwin:2005eu, Abstract = {We present a refined model of the membrane-associated Torpedo acetylcholine (ACh) receptor at 4A resolution. An improved experimental density map was obtained from 342 electron images of helical tubes, and the refined structure was derived to an R-factor of 36.7% (R(free) 37.9%) by standard crystallographic methods, after placing the densities corresponding to a single molecule into an artificial unit cell. The agreement between experimental and calculated phases along the helical layer-lines was used to monitor progress in the refinement and to give an independent measure of the accuracy. The atomic model allowed a detailed description of the whole receptor in the closed-channel form, including the ligand-binding and intracellular domains, which have not previously been interpreted at a chemical level. We confirm that the two ligand-binding alpha subunits have a different extended conformation from the three other subunits in the closed channel, and identify several interactions on both pairs of subunit interfaces, and within the alpha subunits, which may be responsible for their "distorted" structures. The ACh-coordinating amino acid side-chains of the alpha subunits are far apart in the closed channel, indicating that a localised rearrangement, involving closure of loops B and C around the bound ACh molecule, occurs upon activation. A comparison of the structure of the alpha subunit with that of AChBP having ligand present, suggests how the localised rearrangement overcomes the distortions and initiates the rotational movements associated with opening of the channel. Both vestibules of the channel are strongly electronegative, providing a cation-stabilising environment at either entrance of the membrane pore. Access to the pore on the intracellular side is further influenced by narrow lateral windows, which would be expected to screen out electrostatically ions of the wrong charge and size.}, Address = {MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK. mas@mrc-lmb.cam.ac.uk}, Au = {Unwin, N}, Author = {Unwin, N}, Da = {20050209}, Date-Added = {2008-01-30 12:14:30 -0500}, Date-Modified = {2008-05-29 17:17:17 -0700}, Dcom = {20050328}, Dep = {20050125}, Edat = {2005/02/11 09:00}, Gr = {GM61941/GM/United States NIGMS}, Jid = {2985088R}, Journal = {J Mol Biol}, Jt = {Journal of molecular biology}, Language = {eng}, Lr = {20071114}, Mh = {Amino Acid Sequence; Animals; Binding Sites; Crystallography, X-Ray; Electrostatics; Ion Channel Gating; Models, Molecular; Molecular Sequence Data; Protein Binding; Protein Folding; Protein Structure, Quaternary; Protein Structure, Tertiary; Protein Subunits/chemistry/metabolism; Receptors, Nicotinic/*chemistry/metabolism; Sequence Alignment; *Torpedo/*metabolism}, Mhda = {2005/03/29 09:00}, Number = {4}, Own = {NLM}, Pages = {967--989}, Phst = {2004/10/20 {$[$}received{$]$}; 2004/12/09 {$[$}revised{$]$}; 2004/12/15 {$[$}accepted{$]$}; 2005/01/25 {$[$}aheadofprint{$]$}}, Pii = {S0022-2836(04)01601-8}, Pl = {England}, Pmid = {15701510}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.}, Pubm = {Print-Electronic}, Rn = {0 (Protein Subunits); 0 (Receptors, Nicotinic)}, Sb = {IM}, Si = {PDB/2BG9}, So = {J Mol Biol. 2005 Mar 4;346(4):967-89. Epub 2005 Jan 25.}, Stat = {MEDLINE}, Title = {Refined structure of the nicotinic acetylcholine receptor at 4 angstrom resolution}, Volume = {346}, Year = {2005}, Bdsk-Url-1 = {http://dx.doi.org/10.1016/j.jmb.2004.12.031}} @article{Vale:1988rm, Abstract = {Certain intracellular organelles such as the endoplasmic reticulum (Terasaki, M., L. B. Chen, and K. Fujiwara. 1986. J. Cell Biol. 103:1557-1568) and lysosomes (Swanson, J., A. Bushnell, and S. C. Silverstein. Proc. Natl. Acad. Sci. USA. 84:1921-1925) form tubular networks that are closely aligned with microtubules. Here we describe the formation of polygonal networks composed of interconnected membrane tubules that occurs when a preparation of microtubule affinity-purified squid kinesin is combined with microtubules and ATP on a glass surface. The membrane, which is a minor contaminant in the microtubule affinity-purified kinesin preparation, binds to microtubules translocating along kinesin-coated glass surfaces. Force exerted by kinesin upon the microtubule is transmitted to the membrane and a tubular extension of the membrane is produced. As the membrane tubule elongates, membrane tension exerts an opposing force upon the translocating microtubule that can alter its direction of movement by dissociating or partially dissociating the microtubule from the kinesin-coated surface. Membrane tubules that come in contact appear to fuse with one another, and thus give rise to two-dimensional polygonal networks of tubules that have similar features to endoplasmic reticulum networks in cells. Artificial liposomes composed of dimyristoylphosphatidylcholine and yolk phosphatidylglycerol also form stable tubular structures when subjected to shear forces, but do not interact with microtubules or form polygonal networks, suggesting that such phenomena may require membrane-associated proteins. These findings indicate that kinesin generates sufficient force to form tubular membrane extensions in vitro and suggest that this microtubule-based motility protein may also be responsible for creating tubular membrane networks within cells.}, Address = {Department of Pharmacology, University of California, San Francisco, 94143.}, Au = {Vale, RD and Hotani, H}, Author = {Vale, R D and Hotani, H}, Da = {19890119}, Date-Added = {2008-01-30 12:01:05 -0500}, Date-Modified = {2008-05-29 16:28:22 -0700}, Dcom = {19890119}, Edat = {1988/12/01}, Jid = {0375356}, Journal = {J Cell Biol}, Jt = {The Journal of cell biology}, Language = {eng}, Lr = {20051117}, Mh = {Animals; Cell-Free System; Decapodiformes; Endoplasmic Reticulum/physiology/ultrastructure; Intracellular Membranes/*physiology/ultrastructure; Kinesin; Liposomes; Microtubules/*physiology; Morphogenesis; Movement; Nerve Tissue Proteins/*physiology}, Mhda = {1988/12/01 00:01}, Number = {6 Pt 1}, Own = {NLM}, Pages = {2233--2241}, Pl = {UNITED STATES}, Pmid = {3143735}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print}, Rn = {0 (Liposomes); 0 (Nerve Tissue Proteins); EC 3.6.1.- (Kinesin)}, Sb = {IM}, So = {J Cell Biol. 1988 Dec;107(6 Pt 1):2233-41.}, Stat = {MEDLINE}, Title = {Formation of membrane networks in vitro by kinesin-driven microtubule movement.}, Volume = {107}, Year = {1988}} @article{Rodriguez-Boulan:2005zl, Abstract = {Experiments using mammalian epithelial cell lines have elucidated biosynthetic and recycling pathways for apical and basolateral plasma-membrane proteins, and have identified components that guide apical and basolateral proteins along these pathways. These components include apical and basolateral sorting signals, adaptors for basolateral signals, and docking and fusion proteins for vesicular trafficking. Recent live-cell-imaging studies provide a real-time view of sorting processes in epithelial cells, including key roles for actin, microtubules and motors in the organization of post-Golgi trafficking.}, Address = {Margaret Dyson Vision Research Institute, Weill Medical College of Cornell University, 1300 York Avenue, New York, New York 10021, USA. boulan@med.cornell.edu}, Au = {Rodriguez-Boulan, E and Kreitzer, G and Musch, A}, Author = {Rodriguez-Boulan, E and Kreitzer, G and Musch, A}, Da = {20050301}, Date-Added = {2008-01-30 12:01:05 -0500}, Date-Modified = {2008-05-29 16:27:18 -0700}, Dcom = {20050329}, Edat = {2005/03/02 09:00}, Jid = {100962782}, Journal = {Nat Rev Mol Cell Biol}, Jt = {Nature reviews. Molecular cell biology}, Language = {eng}, Lr = {20061115}, Mh = {Adaptor Proteins, Vesicular Transport/physiology; Animals; Cell Membrane/physiology; Cytoplasmic Vesicles/*physiology; Cytoskeleton/physiology; Dogs; Epithelium/*physiology; Kidney/physiology; Signal Transduction/*physiology}, Mhda = {2005/03/30 09:00}, Number = {3}, Own = {NLM}, Pages = {233--247}, Pii = {nrm1593}, Pl = {England}, Pmid = {15738988}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.; Review}, Pubm = {Print}, Rf = {159}, Rn = {0 (Adaptor Proteins, Vesicular Transport)}, Sb = {IM}, So = {Nat Rev Mol Cell Biol. 2005 Mar;6(3):233-47.}, Stat = {MEDLINE}, Title = {Organization of vesicular trafficking in epithelia}, Volume = {6}, Year = {2005}, Bdsk-Url-1 = {http://dx.doi.org/10.1038/nrm1593}} @article{Ledesma:2003sf, Abstract = {Proper nervous activities are gradually developing events. Reflecting this, embryonic neurons start differentiation by sprouting multiple extensions, neurites, which do not bear clear axonal or dendritic structural and molecular characteristics. Later in development one of these multiple neurites elongates further, generating a morphologically polarized neuron with a single long axon and many short dendrites. Still, despite such morphological differences these processes can switch destiny, further reflecting their immaturity. Final and irreversible axonal and dendritic commitment occurs after both axons and dendrites have elongated considerably. Recent evidence suggests that the transition from axonal immaturity to maturity reflects changes in the mechanisms used by neurons to control the precise membrane and cytoskeleton polarization. This chapter provides an overview of how these mechanisms contribute to the formation of an axon.}, Address = {Cavalieri Ottolenghi Scientific Institute, Universita degli Studi di Torino, Orbassano, Turin, Italy.}, Au = {Ledesma, MD and Dotti, CG}, Author = {Ledesma, M D and Dotti, C G}, Da = {20031001}, Date-Added = {2008-01-30 11:51:48 -0500}, Date-Modified = {2008-05-29 16:30:02 -0700}, Dcom = {20040311}, Edat = {2003/10/02 05:00}, Jid = {2985180R}, Journal = {Int Rev Cytol}, Jt = {International review of cytology}, Language = {eng}, Lr = {20041117}, Mh = {Animals; Axons/*physiology; Cell Membrane/*physiology; Cytoskeleton/*physiology; Growth Cones/*physiology; Humans; Membrane Fusion/physiology; Nervous System/embryology/growth \& development}, Mhda = {2004/03/12 05:00}, Own = {NLM}, Pages = {183--219}, Pl = {United States}, Pmid = {14518552}, Pst = {ppublish}, Pt = {Journal Article; Review}, Pubm = {Print}, Rf = {188}, Sb = {IM}, So = {Int Rev Cytol. 2003;227:183-219.}, Stat = {MEDLINE}, Title = {Membrane and cytoskeleton dynamics during axonal elongation and stabilization.}, Volume = {227}, Year = {2003}} @article{Sheetz:2001rz, Abstract = {The rates of mechanochemical processes, such as endocytosis, membrane extension and membrane resealing after cell wounding, are known to be controlled biochemically, through interaction with regulatory proteins. Here, I propose that these rates are also controlled physically, through an apparently continuous adhesion between plasma membrane lipids and cytoskeletal proteins.}, Address = {Department of Biological Sciences, PO Box 2408, Columbia University, Sherman Fairchild Center, 1212 Amsterdam Avenue, New York, NY 10027, USA. ms2001@columbia.edu}, Au = {Sheetz, MP}, Author = {Sheetz, M P}, Da = {20010502}, Date-Added = {2008-01-30 11:51:48 -0500}, Date-Modified = {2008-05-29 16:29:31 -0700}, Dcom = {20010628}, Edat = {2001/05/02 10:00}, Jid = {100962782}, Journal = {Nat Rev Mol Cell Biol}, Jt = {Nature reviews. Molecular cell biology}, Language = {eng}, Lr = {20041117}, Mh = {Cell Adhesion/physiology; Cell Membrane/*chemistry/*physiology; Cytoskeleton/*physiology; Endocytosis/physiology; Eukaryotic Cells/*cytology; Models, Biological}, Mhda = {2001/06/29 10:01}, Number = {5}, Own = {NLM}, Pages = {392--396}, Pii = {35073095}, Pl = {England}, Pmid = {11331914}, Pst = {ppublish}, Pt = {Journal Article; Review}, Pubm = {Print}, Rf = {40}, Sb = {IM}, So = {Nat Rev Mol Cell Biol. 2001 May;2(5):392-6.}, Stat = {MEDLINE}, Title = {Cell control by membrane-cytoskeleton adhesion.}, Volume = {2}, Year = {2001}, Bdsk-Url-1 = {http://dx.doi.org/10.1038/35073095}} @article{Waugh:1987ty, Abstract = {The mechanical equilibrium of bilayer membrane cylinders is analyzed. The analysis is motivated by the observation that mechanically formed membrane strands (tethers) can support significant axial loads and that the tether radius varies inversely with the axial force. Previously, thin shell theory has been used to analyze the tether formation process, but this approach is inadequate for describing and predicting the equilibrium state of the tether itself. In the present work the membrane is modeled as two adjacent, thick, anisotropic liquid shells. The analysis predicts an inverse relationship between axial force and tether radius, which is consistent with experimental observation. The area expansivity modulus and bending stiffness of the tether membrane are calculated using previously measured values of tether radii. These calculated values are consistent with values of membrane properties measured previously. Application of the analysis to precise measurements of the relationship between tether radius and axial force will provide a novel method for determining the mechanical properties of biomembrane.}, Address = {Department of Biophysics, University of Rochester, School of Medicine and Dentistry, New York 14642.}, Au = {Waugh, RE and Hochmuth, RM}, Author = {Waugh, R E and Hochmuth, R M}, Da = {19871118}, Date-Added = {2008-01-30 11:33:45 -0500}, Date-Modified = {2008-05-29 17:00:04 -0700}, Dcom = {19871118}, Edat = {1987/09/01}, Gr = {HL-18208/HL/United States NHLBI; HL-23728/HL/United States NHLBI; HL-27502/HL/United States NHLBI; etc.}, Jid = {0370626}, Journal = {Biophys J}, Jt = {Biophysical journal}, Language = {eng}, Lr = {20071114}, Mh = {Kinetics; *Lipid Bilayers; Mathematics; Models, Biological; Molecular Conformation; Thermodynamics}, Mhda = {1987/09/01 00:01}, Number = {3}, Own = {NLM}, Pages = {391--400}, Pl = {UNITED STATES}, Pmid = {3651558}, Pst = {ppublish}, Pt = {Journal Article; Research Support, U.S. Gov't, P.H.S.}, Pubm = {Print}, Rn = {0 (Lipid Bilayers)}, Sb = {IM}, So = {Biophys J. 1987 Sep;52(3):391-400.}, Stat = {MEDLINE}, Title = {Mechanical equilibrium of thick, hollow, liquid membrane cylinders}, Volume = {52}, Year = {1987}} @book{Bevington:2003qy, Author = {Bevington, P R and Robinson, D K}, Date-Added = {2008-01-29 15:42:57 -0800}, Date-Modified = {2008-05-29 16:54:49 -0700}, Edition = {3rd}, Publisher = {McGraw-Hill}, Title = {Data Reduction and Error Analysis for the Physical Sciences}, Year = {2003}} @article{Neuman:2004lr, Abstract = {Since their invention just over 20 years ago, optical traps have emerged as a powerful tool with broad-reaching applications in biology and physics. Capabilities have evolved from simple manipulation to the application of calibrated forces on-and the measurement of nanometer-level displacements of-optically trapped objects. We review progress in the development of optical trapping apparatus, including instrument design considerations, position detection schemes and calibration techniques, with an emphasis on recent advances. We conclude with a brief summary of innovative optical trapping configurations and applications.}, Address = {Department of Biological Sciences, and Department of Applied Physics, Stanford University, Stanford, California 94305.}, Au = {Neuman, KC and Block, SM}, Author = {Neuman, K C and Block, S M}, Da = {20071101}, Date-Added = {2008-01-17 17:02:20 -0800}, Date-Modified = {2008-05-29 16:52:11 -0700}, Edat = {2006/08/01 09:00}, Gr = {R01 GM051453-12/GM/United States NIGMS; R01 GM051453-12/United States NIGMS}, Jid = {0405571}, Journal = {Rev Sci Instrum}, Jt = {The Review of scientific instruments}, Language = {eng}, Mhda = {2006/08/01 09:00}, Number = {9}, Own = {NLM}, Pages = {2787--2809}, Pl = {United States}, Pmid = {16878180}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print}, So = {Rev Sci Instrum. 2004 Sep;75(9):2787-809. }, Stat = {In-Data-Review}, Title = {Optical trapping}, Volume = {75}, Year = {2004}, Bdsk-Url-1 = {http://dx.doi.org/10.1063/1.1785844}} @book{Landau:1986fr, Annote = {aka LL in short notes}, Annote1 = {Includes index}, Author = {Landau, L D and Lifshitz, E M}, Date-Added = {2008-01-16 11:42:41 -0800}, Date-Modified = {2008-01-16 11:45:02 -0800}, Edition = {3rd English ed. revised and enlarged by E.M. Lifshitz, A.M. Kosevich, and L.P. Pitaevskii %@ 0080339174 : %@ 0080339166 (soft) :}, Pages = {149-169}, Publisher = {Pergamon Press}, Title = {Theory of Elasticity}, Year = {1986}} @article{Steigmann:1999yq, Author = {Steigmann, D J}, Date-Added = {2008-01-16 11:35:33 -0800}, Date-Modified = {2008-01-16 11:36:04 -0800}, Isi = {ISI:000084835000002}, Issn = {0003-9527}, Journal = {Archive for Rational Mechanics and Analysis}, Number = {2}, Pages = {127--152}, Publication-Type = {J}, Title = {Fluid films with curvature elasticity}, Volume = {150}, Year = {1999}, Bdsk-File-1 = {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}} @article{Jenkins:1977kx, Address = {PHILADELPHIA}, Annote = {aka Jenkins1 in the short notes}, Author = {Jenkins, J T}, Author-Address = {CORNELL UNIV,DEPT THEORET & APPL MECH,ITHACA,NY 14853.}, Cited-Reference-Count = {10}, Date-Added = {2008-01-16 11:29:52 -0800}, Date-Modified = {2008-01-16 11:37:01 -0800}, Document-Type = {Article}, Isi = {ISI:A1977DH83200006}, Isi-Document-Delivery-Number = {DH832}, Iso-Source-Abbreviation = {SIAM J. Appl. Math.}, Issn = {0036-1399}, Journal = {SIAM J. Appl. Math.}, Language = {English}, Number = {4}, Page-Count = {10}, Pages = {755--764}, Publication-Type = {J}, Publisher = {SIAM PUBLICATIONS}, Publisher-Address = {3600 UNIV CITY SCIENCE CENTER, PHILADELPHIA, PA 19104-2688}, Source = {SIAM J APPL MATH}, Subject-Category = {Mathematics, Applied}, Times-Cited = {22}, Title = {Equations of Mechanical Equilibrium of a Model Membrane}, Volume = {32}, Year = {1977}} @book{Nakahara:1990uq, Annote = {Includes index}, Annote1 = {Bibliography: p. [492]-496}, Author = {Nakahara, M}, Date-Added = {2008-01-16 11:17:29 -0800}, Date-Modified = {2008-05-29 16:46:22 -0700}, Publisher = {Institute of Physics Publishing}, Title = {Geometry, Topology, and Physics}, Year = {1990}} @article{Rawicz:2000lr, Abstract = {Micropipette pressurization of giant bilayer vesicles was used to measure both elastic bending k(c) and area stretch K(A) moduli of fluid-phase phosphatidylcholine (PC) membranes. Twelve diacyl PCs were chosen: eight with two 18 carbon chains and degrees of unsaturation from one double bond (C18:1/0, C18:0/1) to six double bonds per lipid (diC18:3), two with short saturated carbon chains (diC13:0, diC14:0), and two with long unsaturated carbon chains (diC20:4, diC22:1). Bending moduli were derived from measurements of apparent expansion in vesicle surface area under very low tensions (0.001-0.5 mN/m), which is dominated by smoothing of thermal bending undulations. Area stretch moduli were obtained from measurements of vesicle surface expansion under high tensions (>0.5 mN/m), which involve an increase in area per molecule and a small-but important-contribution from smoothing of residual thermal undulations. The direct stretch moduli varied little (< +/-10%) with either chain unsaturation or length about a mean of 243 mN/m. On the other hand, the bending moduli of saturated/monounsaturated chain PCs increased progressively with chain length from 0.56 x 10(-19) J for diC13:0 to 1.2 x 10(-19) J for diC22:1. However, quite unexpectedly for longer chains, the bending moduli dropped precipitously to approximately 0.4 x 10(-19) J when two or more cis double bonds were present in a chain (C18:0/2, diC18:2, diC18:3, diC20:4). Given nearly constant area stretch moduli, the variations in bending rigidity with chain length and polyunsaturation implied significant variations in thickness. To test this hypothesis, peak-to-peak headgroup thicknesses h(pp) of bilayers were obtained from x-ray diffraction of multibilayer arrays at controlled relative humidities. For saturated/monounsaturated chain bilayers, the distances h(pp) increased smoothly from diC13:0 to diC22:1 as expected. Moreover, the distances and elastic properties correlated well with a polymer brush model of the bilayer that specifies that the elastic ratio (k(c)/K(A))(1/2) = (h(pp) - h(o))/24, where h(o) approximately 1 nm accounts for separation of the headgroup peaks from the deformable hydrocarbon region. However, the elastic ratios and thicknesses for diC18:2, diC18:3, and diC20:4 fell into a distinct group below the correlation, which showed that poly-cis unsaturated chain bilayers are thinner and more flexible than saturated/monounsaturated chain bilayers.}, Address = {Department of Pathology, University of British Columbia, Vancouver, British Columbia V6T 1W5, Canada.}, Au = {Rawicz, W and Olbrich, KC and McIntosh, T and Needham, D and Evans, E}, Author = {Rawicz, W and Olbrich, K C and McIntosh, T and Needham, D and Evans, E}, Da = {20000803}, Date-Added = {2008-01-16 11:12:16 -0800}, Date-Modified = {2008-05-29 16:45:01 -0700}, Dcom = {20000803}, Edat = {2000/06/27 11:00}, Gr = {GM08555/GM/United States NIGMS; GM27278/GM/United States NIGMS; GM40162/GM/United States NIGMS}, Jid = {0370626}, Journal = {Biophys J}, Jt = {Biophysical journal}, Language = {eng}, Lr = {20071114}, Mh = {Biophysics; Elasticity; Lipid Bilayers/*chemistry; Lipids/chemistry; Liposomes/chemistry; Models, Chemical; Phosphatidylcholines/*chemistry; Pressure; Surface Tension}, Mhda = {2000/08/06 11:00}, Number = {1}, Own = {NLM}, Pages = {328--339}, Pl = {UNITED STATES}, Pmid = {10866959}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.}, Pubm = {Print}, Rn = {0 (Lipid Bilayers); 0 (Lipids); 0 (Liposomes); 0 (Phosphatidylcholines)}, Sb = {IM}, So = {Biophys J. 2000 Jul;79(1):328-39. }, Stat = {MEDLINE}, Title = {Effect of chain length and unsaturation on elasticity of lipid bilayers}, Volume = {79}, Year = {2000}, Bdsk-File-1 = 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@article{Hess:2007ve, Abstract = {Organization in biological membranes spans many orders of magnitude in length scale, but limited resolution in far-field light microscopy has impeded distinction between numerous biomembrane models. One canonical example of a heterogeneously distributed membrane protein is hemagglutinin (HA) from influenza virus, which is associated with controversial cholesterol-rich lipid rafts. Using fluorescence photoactivation localization microscopy, we are able to image distributions of tens of thousands of HA molecules with subdiffraction resolution ( approximately 40 nm) in live and fixed fibroblasts. HA molecules form irregular clusters on length scales from approximately 40 nm up to many micrometers, consistent with results from electron microscopy. In live cells, the dynamics of HA molecules within clusters is observed and quantified to determine an effective diffusion coefficient. The results are interpreted in terms of several established models of biological membranes.}, Address = {Department of Physics and Astronomy and Institute for Molecular Biophysics, University of Maine, Orono, ME 04469, USA. sam.hess@umit.maine.edu}, Au = {Hess, ST and Gould, TJ and Gudheti, MV and Maas, SA and Mills, KD and Zimmerberg, J}, Author = {Hess, Samuel T and Gould, Travis J and Gudheti, Manasa V and Maas, Sarah A and Mills, Kevin D and Zimmerberg, Joshua}, Da = {20071105}, Date-Added = {2008-01-04 14:49:56 -0800}, Date-Modified = {2008-01-04 14:51:19 -0800}, Dcom = {20071227}, Dep = {20071024}, Doi = {10.1073/pnas.0708066104}, Edat = {2007/10/26 09:00}, Gr = {K25AI65459/AI/United States NIAID}, Issn = {0027-8424 (Print)}, Jid = {7505876}, Journal = {Proc Natl Acad Sci U S A}, Jt = {Proceedings of the National Academy of Sciences of the United States of America}, Keywords = {Cell Line; Cell Survival; Hemagglutinins/*metabolism; Membrane Microdomains/*metabolism/*ultrastructure; Nanostructures/*ultrastructure}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Hess/2007.pdf}, Mhda = {2007/12/28 09:00}, Number = {44}, Own = {NLM}, Pages = {17370--17375}, Phst = {2007/10/24 {$[$}aheadofprint{$]$}}, Pii = {0708066104}, Pl = {United States}, Pmid = {17959773}, Pst = {ppublish}, Pt = {Journal Article; Research Support, N.I.H., Extramural; Research Support, N.I.H., Intramural; Research Support, Non-U.S. Gov't}, Pubm = {Print-Electronic}, Rn = {0 (Hemagglutinins)}, Sb = {IM}, So = {Proc Natl Acad Sci U S A. 2007 Oct 30;104(44):17370-5. Epub 2007 Oct 24. }, Stat = {MEDLINE}, Title = {Dynamic clustered distribution of hemagglutinin resolved at 40 nm in living cell membranes discriminates between raft theories}, Volume = {104}, Year = {2007}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://dx.doi.org/10.1073/pnas.0708066104}} @article{Bruinsma:1996zr, Author = {Bruinsma, R and Pincus, P}, Date-Added = {2008-01-04 14:46:08 -0800}, Date-Modified = {2008-05-29 16:38:29 -0700}, Isbn = {1359-0286}, Journal = {Curr Opin Solid St M}, Number = {3}, Pages = {401--406}, Title = {Protein aggregation in membranes}, Volume = {1}, Year = {1996}} @article{Feng:2006rr, Abstract = { A numerical simulation framework is presented for the study of biological membranes composed of lipid bilayers based on the finite element method. The classic model for these membranes employs a two-dimensional-fluid-like elastic constitutive law which is sensitive to curvature, and subjects vesicles to physically imposed constraints on surface area and volume. This model is implemented numerically via the use of C1-conforming triangular Loop subdivision finite elements. The validity of the framework is tested by computing equilibrium shapes from previously-determined axisymmetric shape-phase diagram of lipid bilayer vesicles with homogeneous material properties. Some of the benefits and challenges of finite element modeling of lipid bilayer systems are discussed, and it is indicated how this framework is natural for future investigation of biologically realistic bilayer structures involving nonaxisymmetric geometries, binding and adhesive interactions, heterogeneous mechanical properties, cytoskeletal interactions, and complex loading arrangements. These biologically relevant features have important consequences for the shape mechanics of nonidealized vesicles and cells, and their study requires not simply advances in theory, but also advances in numerical simulation techniques, such as those presented here.}, Author = {Feng, F and Klug, W S}, Date-Added = {2008-01-03 12:57:58 -0800}, Date-Modified = {2008-05-29 16:40:50 -0700}, Journal = {J Comput Phys}, Keywords = {Biomembranes; Lipid bilayer mechanics; Cell mechanics; Finite element; Subdivision surfaces}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Feng/2006.pdf}, Number = {1}, Pages = {394--408}, Title = {Finite element modeling of lipid bilayer membranes}, Ty = {JOUR}, Volume = {220}, Year = {2006}, Bdsk-File-1 = {YnBsaXN0MDDUAQIDBAUGCQpYJHZlcnNpb25UJHRvcFkkYXJjaGl2ZXJYJG9iamVjdHMSAAGGoNEHCFRyb290gAFfEA9OU0tleWVkQXJjaGl2ZXKoCwwXGBkdJCVVJG51bGzTDQ4PEBEUViRjbGFzc1dOUy5rZXlzWk5TLm9iamVjdHOAB6ISE4ACgAOiFRaABIAGWWFsaWFzRGF0YVxyZWxhdGl2ZVBhdGjSDRobHFdOUy5kYXRhgAVPEQGIAAAAAAGIAAIAAANoc3IAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAADBcRzJSCsAAACQfXgIMjAwNi5wZGYAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAJB9V8OijEQAAAAAAAAAAAAEAAMAAAkgAAAAAAAAAAAAAAAAAAAABEZlbmcAEAAIAADBcY1JAAAAEQAIAADDovzEAAAAAQAYAJB9eABGa88ARmrVAEZqGwBGZGgAQIlDAAIAP2hzcjpVc2VyczphdG9taWNwaXJhdGU6RG9jdW1lbnRzOkNhbHRlY2g6QXJ0aWNsZXM6RmVuZzoyMDA2LnBkZgAADgASAAgAMgAwADAANgAuAHAAZABmAA8ACAADAGgAcwByABIAO1VzZXJzL2F0b21pY3BpcmF0ZS9Eb2N1bWVudHMvQ2FsdGVjaC9BcnRpY2xlcy9GZW5nLzIwMDYucGRmAAATAAEvAAAVAAIAE///AADSHh8gIVgkY2xhc3Nlc1okY2xhc3NuYW1loyEiI11OU011dGFibGVEYXRhVk5TRGF0YVhOU09iamVjdF8QIi4uLy4uLy4uLy4uL0FydGljbGVzL0ZlbmcvMjAwNi5wZGbSHh8mJ6InI1xOU0RpY3Rpb25hcnkACAARABoAHwApADIANwA6AD8AQQBTAFwAYgBpAHAAeACDAIUAiACKAIwAjwCRAJMAnQCqAK8AtwC5AkUCSgJTAl4CYgJwAncCgAKlAqoCrQAAAAAAAAIBAAAAAAAAACgAAAAAAAAAAAAAAAAAAAK6}, Bdsk-Url-1 = {http://www.sciencedirect.com/science/article/B6WHY-4KCHDB4-3/2/c5456826ad705bdb9103008bb0ae61a5}} @article{Hoglund:1992fv, Abstract = {The core of late states of maturing human immunodeficiency virus type 1 (HIV-1) has been visualized in three dimensions at approximately 7 nm resolution by electron microscopic tomography. After budding, approximately 25 nm thick precursor material is observed densely assembled inside the viral envelope. Upon proteolysis the core material is transported and condensed in the center of the virion. The core, 100 nm in length, spans the entire diameter of the virion showing a 40-60 nm wide free end and a narrow end approximately 20 nm. A model of the core is derived consisting of two fibers packed into a bilateral, elongated structure. Two ends of the fibers are compacted together, forming one narrow end of the core, while the two other fiber ends are situated more loosely together allowing for flexibility. Structural maturation of the virus could be reflected by the degree of compactness of the core. The narrow end of the core is observed attached to the envelope with a conspicuous core-envelope link (CEL).}, Address = {Department of Biochemistry, Biomedical Center, Uppsala, Sweden.}, Au = {Hoglund, S and Ofverstedt, LG and Nilsson, A and Lundquist, P and Gelderblom, H and Ozel, M and Skoglund, U}, Author = {Hoglund, S and Ofverstedt, L G and Nilsson, A and Lundquist, P and Gelderblom, H and Ozel, M and Skoglund, U}, Da = {19920317}, Date-Added = {2008-01-03 11:59:24 -0800}, Date-Modified = {2008-01-03 11:59:45 -0800}, Dcom = {19920317}, Edat = {1992/01/01}, Issn = {0889-2229 (Print)}, Jid = {8709376}, Journal = {AIDS Res Hum Retroviruses}, Jt = {AIDS research and human retroviruses}, Keywords = {HIV-1/physiology/*ultrastructure; Humans; Image Processing, Computer-Assisted; Ribonucleoproteins/ultrastructure; Viral Core Proteins/ultrastructure; Viral Envelope Proteins/ultrastructure; Virion/*ultrastructure; *Virus Replication}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Hoglund/1992.pdf}, Lr = {20061115}, Mhda = {1992/01/01 00:01}, Number = {1}, Own = {NLM}, Pages = {1--7}, Pl = {UNITED STATES}, Pmid = {1736937}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't}, Pubm = {Print}, Rn = {0 (Ribonucleoproteins); 0 (Viral Core Proteins); 0 (Viral Envelope Proteins)}, Sb = {IM; X}, So = {AIDS Res Hum Retroviruses. 1992 Jan;8(1):1-7. }, Stat = {MEDLINE}, Title = {Spatial visualization of the maturing HIV-1 core and its linkage to the envelope}, Volume = {8}, Year = {1992}, Bdsk-File-1 = {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}} @article{Benjamin:2005qv, Abstract = {While the structures of nearly every HIV-1 protein are known in atomic detail from X-ray crystallography and NMR spectroscopy, many questions remain about how the individual proteins are arranged in the mature infectious viral particle. Here, we report the three-dimensional structures of individual HIV-1 virus-like particles (VLPs) as obtained by electron cryotomography. These reconstructions revealed that while the structures and positions of the conical cores within each VLP were unique, they exhibited several surprisingly consistent features, including similarities in the size and shape of the wide end of the capsid (the "base"), uniform positioning of the base and other regions of the capsid 11nm away from the envelope/MA layer, a cone angle that typically varied from 24 degrees to 18 degrees around the long axis of the cone, and an internal density (presumably part of the NC/RNA complex) cupped within the base. Multiple and nested capsids were observed. These results support the fullerene cone model for the viral capsid, indicate that viral maturation involves a free re-organization of the capsid shell rather than a continuous condensation, imply that capsid assembly is both concentration-driven and template-driven, suggest that specific interactions exist between the capsid and the adjacent envelope/MA and NC/RNA layers, and show that a particular capsid shape is favored strongly in-vivo.}, Address = {Division of Biology, California Institute of Technology, 1200 E. California Blvd., Pasadena, CA 91125, USA.}, Au = {Benjamin, J and Ganser-Pornillos, BK and Tivol, WF and Sundquist, WI and Jensen, GJ}, Author = {Benjamin, Jordan and Ganser-Pornillos, Barbie K and Tivol, William F and Sundquist, Wesley I and Jensen, Grant J}, Da = {20050126}, Date-Added = {2008-01-02 15:57:14 -0800}, Date-Modified = {2008-01-02 15:57:28 -0800}, Dcom = {20050318}, Dep = {20041219}, Doi = {10.1016/j.jmb.2004.11.064}, Edat = {2005/01/27 09:00}, Gr = {P01 GM66521/GM/United States NIGMS}, Issn = {0022-2836 (Print)}, Jid = {2985088R}, Journal = {J Mol Biol}, Jt = {Journal of molecular biology}, Keywords = {Capsid/chemistry; Cryoelectron Microscopy/*methods; Fullerenes/chemistry; HIV-1/*chemistry; Imaging, Three-Dimensional; Protein Conformation; Viral Envelope Proteins; Virion/*chemistry}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Benjamin/2005.pdf}, Lr = {20071114}, Mhda = {2005/03/19 09:00}, Number = {2}, Own = {NLM}, Pages = {577--588}, Phst = {2004/09/24 {$[$}received{$]$}; 2004/11/18 {$[$}revised{$]$}; 2004/11/23 {$[$}accepted{$]$}; 2004/12/19 {$[$}aheadofprint{$]$}}, Pii = {S0022-2836(04)01535-9}, Pl = {England}, Pmid = {15670606}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.}, Pubm = {Print-Electronic}, Rn = {0 (Fullerenes); 0 (Viral Envelope Proteins)}, Sb = {IM}, So = {J Mol Biol. 2005 Feb 18;346(2):577-88. Epub 2004 Dec 19.}, Stat = {MEDLINE}, Title = {Three-dimensional structure of HIV-1 virus-like particles by electron cryotomography}, Volume = {346}, Year = {2005}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://dx.doi.org/10.1016/j.jmb.2004.11.064}} @article{Cheng:2007os, Address = {Department of Biochemistry and Biophysics, University of California-San Francisco, San Francisco, California 94143, USA.}, Au = {Cheng, Y and Walz, T}, Author = {Cheng, Y and Walz, T}, Da = {20070228}, Date-Added = {2008-01-02 15:48:37 -0800}, Date-Modified = {2008-05-29 16:35:07 -0700}, Dcom = {20070419}, Edat = {2007/03/01 09:00}, Group = {Endocytosis}, Jid = {0373334}, Journal = {Methods Cell Biol}, Jt = {Methods in cell biology}, Keywords = {Animals; Clathrin/*chemistry/*ultrastructure; Clathrin-Coated Vesicles/*ultrastructure; Cryoelectron Microscopy; Crystallography, X-Ray; Endocytosis; Humans; Microscopy, Electron/*methods; Nuclear Magnetic Resonance, Biomolecular; Receptors, Transferrin/*chemistry/*ultrastructure; Transferrin/chemistry/ultrastructure}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Cheng/2007a.pdf}, Mhda = {2007/04/20 09:00}, Own = {NLM}, Pages = {463--487}, Pii = {S0091-679X(06)79018-5}, Pl = {United States}, Pmid = {17327169}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print}, Rn = {0 (Clathrin); 0 (Receptors, Transferrin); 11096-37-0 (Transferrin)}, Sb = {IM}, So = {Methods Cell Biol. 2007;79:463-87.}, Stat = {MEDLINE}, Title = {Reconstructing the endocytotic machinery}, Volume = {79}, Year = {2007}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://dx.doi.org/10.1016/S0091-679X(06)79018-5}} @article{Higgins:2002qf, Abstract = {Clathrin-mediated endocytosis is one of the major entry routes into a eukaryotic cell. It is driven by protein components that aid the selection of cargo and provide the mechanical force needed to both deform the plasma membrane and detach a vesicle. Clathrin-coated vesicles were first observed by electron microscopy in the early 1960s. In subsequent years, many of the characteristic intermediates generated during vesicle formation have been trapped and observed. A variety of electron microscopy techniques, from the analysis of sections through cells to the study of endocytic intermediates formed in vitro, have led to the proposition of a sequence of events and of roles for different proteins during vesicle formation. In this article, these techniques and the insights gained are reviewed, and their role in providing snap-shots of the stages of endocytosis in atomic detail is discussed.}, Address = {MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.}, Au = {Higgins, MK and McMahon, HT}, Author = {Higgins, Matthew K and McMahon, Harvey T}, Da = {20020621}, Date-Added = {2008-01-02 15:32:56 -0800}, Date-Modified = {2008-01-02 15:38:21 -0800}, Dcom = {20021209}, Edat = {2002/06/22 10:00}, Group = {Endocytosis}, Issn = {0968-0004 (Print)}, Jid = {7610674}, Journal = {Trends Biochem Sci}, Jt = {Trends in biochemical sciences}, Keywords = {Animals; Clathrin/*metabolism; Clathrin-Coated Vesicles/*metabolism/ultrastructure; Endocytosis/*physiology; Fluorescent Dyes/metabolism; Lipid Metabolism; Lipids/chemistry; Models, Biological}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Higgins/2002.pdf}, Lr = {20051117}, Mhda = {2002/12/10 04:00}, Number = {5}, Own = {NLM}, Pages = {257--263}, Pii = {S0968000402020893}, Pl = {England}, Pmid = {12076538}, Pst = {ppublish}, Pt = {Journal Article; Review}, Pubm = {Print}, Rf = {45}, Rn = {0 (Clathrin); 0 (Fluorescent Dyes); 0 (Lipids)}, Sb = {IM}, So = {Trends Biochem Sci. 2002 May;27(5):257-63.}, Stat = {MEDLINE}, Title = {Snap-shots of clathrin-mediated endocytosis}, Volume = {27}, Year = {2002}, Bdsk-File-1 = {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}} @article{Cheng:2007ye, Abstract = {Clathrin-coated vesicles mediate vesicular traffic in cells. Three-dimensional image reconstructions of homogenous populations of in vitro assembled clathrin coats have yielded a molecular model for clathrin and its interactions with some of its partners. The intrinsic averaging required for those calculations has precluded detailed analysis of heterogeneous populations of clathrin-coated vesicles isolated from cells. We have therefore used cryo-electron tomography to study the lattice organization of individual clathrin-coated vesicles and the disposition of the captured vesicle with respect to the surrounding coat. We find a wide range of designs for the clathrin lattice, with different patterns of pentagonal, hexagonal, and occasionally heptagonal facets. Many coats, even smaller ones, enclose membrane vesicles, which are generally offset from the center of the clathrin shell. The electron density distribution between the coat and the underlying vesicle is not uniform, and the number of apparent contacts that anchor the clathrin lattice to the vesicle membrane is significantly less than the number of clathrin heavy chains in the assembly. We suggest that the eccentric position of the vesicle reflects the polarity of assembly, from initiation of coat formation to membrane pinching.}, Address = {Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA. ycheng@biochem.ucsf.edu}, Au = {Cheng, Y and Boll, W and Kirchhausen, T and Harrison, SC and Walz, T}, Author = {Cheng, Yifan and Boll, Werner and Kirchhausen, Tomas and Harrison, Stephen C and Walz, Thomas}, Da = {20061226}, Date-Added = {2008-01-02 15:29:39 -0800}, Date-Modified = {2008-01-02 15:41:51 -0800}, Dcom = {20070221}, Dep = {20061014}, Doi = {10.1016/j.jmb.2006.10.036}, Edat = {2006/11/11 09:00}, Gr = {GM 36548/GM/United States NIGMS; GM 62580/GM/United States NIGMS; P01 GM062580-05/GM/United States NIGMS; R01 GM036548-20/GM/United States NIGMS}, Group = {Endocytosis}, Issn = {0022-2836 (Print)}, Jid = {2985088R}, Journal = {J Mol Biol}, Jt = {Journal of molecular biology}, Keywords = {Animals; Cattle; Cell Membrane/ultrastructure; Clathrin/ultrastructure; Clathrin-Coated Vesicles/*ultrastructure; Cryoelectron Microscopy/*methods; Tomography, X-Ray Computed/*methods}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Cheng/2007.pdf}, Lr = {20071203}, Mhda = {2007/02/22 09:00}, Number = {3}, Own = {NLM}, Pages = {892--899}, Phst = {2006/08/01 {$[$}received{$]$}; 2006/09/24 {$[$}revised{$]$}; 2006/10/05 {$[$}accepted{$]$}; 2006/10/14 {$[$}aheadofprint{$]$}}, Pii = {S0022-2836(06)01414-8}, Pl = {England}, Pmid = {17095010}, Pst = {ppublish}, Pt = {Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't}, Pubm = {Print-Electronic}, Rn = {0 (Clathrin)}, Sb = {IM}, So = {J Mol Biol. 2007 Jan 19;365(3):892-9. Epub 2006 Oct 14.}, Stat = {MEDLINE}, Title = {Cryo-electron tomography of clathrin-coated vesicles: structural implications for coat assembly}, Volume = {365}, Year = {2007}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://dx.doi.org/10.1016/j.jmb.2006.10.036}} @article{Marsh:2007ph, Address = {Institute for Molecular Bioscience, Queensland Bioscience Precinct, The University of Queensland, Brisbane, Queensland, Australia.}, Au = {Marsh, BJ}, Author = {Marsh, Brad J}, Da = {20070228}, Date-Added = {2008-01-02 15:17:17 -0800}, Date-Modified = {2008-01-02 15:17:26 -0800}, Dcom = {20070419}, Doi = {10.1016/S0091-679X(06)79008-2}, Edat = {2007/03/01 09:00}, Gr = {DK-71236/DK/United States NIDDK; GM42629/GM/United States NIGMS; P01-GM61306/GM/United States NIGMS; P41-RR00592/RR/United States NCRR}, Issn = {0091-679X (Print)}, Jid = {0373334}, Journal = {Methods Cell Biol}, Jt = {Methods in cell biology}, Keywords = {Animals; Cells, Cultured; Golgi Apparatus/ultrastructure; Humans; Imaging, Three-Dimensional/*methods; Intracellular Membranes/*ultrastructure; Microscopy, Electron/*methods; Microtomy}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Marsh/2007.pdf}, Lr = {20071203}, Mhda = {2007/04/20 09:00}, Own = {NLM}, Pages = {193--220}, Pii = {S0091-679X(06)79008-2}, Pl = {United States}, Pmid = {17327158}, Pst = {ppublish}, Pt = {Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't}, Pubm = {Print}, Sb = {IM}, So = {Methods Cell Biol. 2007;79:193-220.}, Stat = {MEDLINE}, Title = {Reconstructing mammalian membrane architecture by large area cellular tomography}, Volume = {79}, Year = {2007}, Bdsk-File-1 = {YnBsaXN0MDDUAQIDBAUGCQpYJHZlcnNpb25UJHRvcFkkYXJjaGl2ZXJYJG9iamVjdHMSAAGGoNEHCFRyb290gAFfEA9OU0tleWVkQXJjaGl2ZXKoCwwXGBkdJCVVJG51bGzTDQ4PEBEUViRjbGFzc1dOUy5rZXlzWk5TLm9iamVjdHOAB6ISE4ACgAOiFRaABIAGWWFsaWFzRGF0YVxyZWxhdGl2ZVBhdGjSDRobHFdOUy5kYXRhgAVPEQGKAAAAAAGKAAIAAANoc3IAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAADBcRzJSCsAAACOzyEIMjAwNy5wZGYAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAI7N5cOhWmsAAAAAAAAAAAAEAAMAAAkgAAAAAAAAAAAAAAAAAAAABU1hcnNoAAAQAAgAAMFxjUkAAAARAAgAAMOhyusAAAABABgAjs8hAEZrzwBGatUARmobAEZkaABAiUMAAgBAaHNyOlVzZXJzOmF0b21pY3BpcmF0ZTpEb2N1bWVudHM6Q2FsdGVjaDpBcnRpY2xlczpNYXJzaDoyMDA3LnBkZgAOABIACAAyADAAMAA3AC4AcABkAGYADwAIAAMAaABzAHIAEgA8VXNlcnMvYXRvbWljcGlyYXRlL0RvY3VtZW50cy9DYWx0ZWNoL0FydGljbGVzL01hcnNoLzIwMDcucGRmABMAAS8AABUAAgAT//8AANIeHyAhWCRjbGFzc2VzWiRjbGFzc25hbWWjISIjXU5TTXV0YWJsZURhdGFWTlNEYXRhWE5TT2JqZWN0XxAjLi4vLi4vLi4vLi4vQXJ0aWNsZXMvTWFyc2gvMjAwNy5wZGbSHh8mJ6InI1xOU0RpY3Rpb25hcnkACAARABoAHwApADIANwA6AD8AQQBTAFwAYgBpAHAAeACDAIUAiACKAIwAjwCRAJMAnQCqAK8AtwC5AkcCTAJVAmACZAJyAnkCggKoAq0CsAAAAAAAAAIBAAAAAAAAACgAAAAAAAAAAAAAAAAAAAK9}, Bdsk-Url-1 = {http://dx.doi.org/10.1016/S0091-679X(06)79008-2}} @article{Ladinsky:2007gd, Address = {Boulder Laboratory for 3D Electron Microscopy of Cells, Department of MCD Biology, University of Colorado, Boulder, Colorado 80309, USA.}, Au = {Ladinsky, MS and Howell, KE}, Author = {Ladinsky, Mark S and Howell, Kathryn E}, Da = {20070228}, Date-Added = {2008-01-02 15:16:21 -0800}, Date-Modified = {2008-01-02 15:16:36 -0800}, Dcom = {20070419}, Doi = {10.1016/S0091-679X(06)79021-5}, Edat = {2007/03/01 09:00}, Issn = {0091-679X (Print)}, Jid = {0373334}, Journal = {Methods Cell Biol}, Jt = {Methods in cell biology}, Keywords = {Animals; *Cryoultramicrotomy; Humans; Immunohistochemistry/*methods; Mice; Microscopy, Immunoelectron/*methods; Organelles/*ultrastructure; Staining and Labeling}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Ladinsky/2007.pdf}, Mhda = {2007/04/20 09:00}, Own = {NLM}, Pages = {543--558}, Pii = {S0091-679X(06)79021-5}, Pl = {United States}, Pmid = {17327173}, Pst = {ppublish}, Pt = {Journal Article; Review}, Pubm = {Print}, Rf = {27}, Sb = {IM}, So = {Methods Cell Biol. 2007;79:543-58.}, Stat = {MEDLINE}, Title = {Electron tomography of immunolabeled cryosections}, Volume = {79}, Year = {2007}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://dx.doi.org/10.1016/S0091-679X(06)79021-5}} @article{Sougrat:2007it, Abstract = {The envelope glycoproteins of primate lentiviruses, including human and simian immunodeficiency viruses (HIV and SIV), are heterodimers of a transmembrane glycoprotein (usually gp41), and a surface glycoprotein (gp120), which binds CD4 on target cells to initiate viral entry. We have used electron tomography to determine the three-dimensional architectures of purified SIV virions in isolation and in contact with CD4+ target cells. The trimeric viral envelope glycoprotein surface spikes are heterogeneous in appearance and typically approximately 120 A long and approximately 120 A wide at the distal end. Docking of SIV or HIV-1 on the T cell surface occurs via a neck-shaped contact region that is approximately 400 A wide and consistently consists of a closely spaced cluster of five to seven rod-shaped features, each approximately 100 A long and approximately 100 A wide. This distinctive structure is not observed when viruses are incubated with T lymphocytes in the presence of anti-CD4 antibodies, the CCR5 antagonist TAK779, or the peptide entry inhibitor SIVmac251 C34. For virions bound to cells, few trimers were observed away from this cluster at the virion-cell interface, even in cases where virus preparations showing as many as 70 envelope glycoprotein trimers per virus particle were used. This contact zone, which we term the "entry claw", provides a spatial context to understand the molecular mechanisms of viral entry. Determination of the molecular composition and structure of the entry claw may facilitate the identification of improved drugs for the inhibition of HIV-1 entry.}, Address = {Laboratory of Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland, United States of America.}, Au = {Sougrat, R and Bartesaghi, A and Lifson, JD and Bennett, AE and Bess, JW and Zabransky, DJ and Subramaniam, S}, Author = {Sougrat, R and Bartesaghi, A and Lifson, J D and Bennett, A E and Bess, J W and Zabransky, D J and Subramaniam, S}, Da = {20070528}, Date-Added = {2008-01-02 15:09:41 -0800}, Date-Modified = {2008-05-29 16:34:09 -0700}, Dcom = {20070612}, Edat = {2007/05/08 09:00}, Gr = {N01-CO-12400/CO/United States NCI}, Jid = {101238921}, Journal = {PLoS Pathog}, Jt = {PLoS pathogens}, Keywords = {Antigens, CD4/metabolism/physiology; Binding Sites; CD4-Positive T-Lymphocytes/*virology; *Electrons; HIV Envelope Protein gp120/metabolism/physiology; HIV Envelope Protein gp41/metabolism/physiology; HIV-1/*pathogenicity; Imaging, Three-Dimensional; Simian immunodeficiency virus/*pathogenicity; Tomography/*methods; Virion}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Sougrat/2007.pdf}, Lr = {20071203}, Mhda = {2007/06/15 09:00}, Number = {5}, Own = {NLM}, Pages = {e63}, Phst = {2006/12/07 {$[$}received{$]$}; 2007/03/19 {$[$}accepted{$]$}}, Pii = {06-PLPA-RA-0530R3}, Pl = {United States}, Pmid = {17480119}, Pst = {ppublish}, Pt = {Journal Article; Research Support, N.I.H., Extramural; Research Support, N.I.H., Intramural}, Pubm = {Print}, Rn = {0 (Antigens, CD4); 0 (HIV Envelope Protein gp120); 0 (HIV Envelope Protein gp41)}, Sb = {IM}, So = {PLoS Pathog. 2007 May 4;3(5):e63.}, Stat = {MEDLINE}, Title = {Electron tomography of the contact between {T} cells and {SIV/HIV-1}: implications for viral entry}, Volume = {3}, Year = {2007}, Bdsk-File-1 = {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}, Bdsk-File-2 = {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}, Bdsk-Url-1 = {http://dx.doi.org/10.1371/journal.ppat.0030063}} @article{Briggs:2006la, Abstract = {Infectious HIV particles contain a characteristic cone-shaped core encasing the viral RNA and replication proteins. The core exhibits significant heterogeneity in size and shape, yet consistently forms a well-defined structure. The mechanism by which the core is assembled in the maturing virion remains poorly understood. Using cryo-electron tomography, we have produced three-dimensional reconstructions of authentic, unstained HIV-1. These reveal the viral morphology with unprecedented clarity and suggest the following mechanism for core formation inside the extracellular virion: core growth initiates at the narrow end of the cone and proceeds toward the distal side of the virion until limited by the viral membrane. Curvature and closure of the broad end of the core are then directed by the inner surface of the viral membrane. This mechanism accommodates significant flexibility in lattice growth while ensuring the closure of cores of variable size and shape.}, Address = {Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Headington, Oxford OX3 7BN, UK.}, Au = {Briggs, JA and Grunewald, K and Glass, B and Forster, F and Krausslich, HG and Fuller, SD}, Author = {Briggs, John A G and Grunewald, Kay and Glass, Barbel and Forster, Friedrich and Krausslich, Hans-Georg and Fuller, Stephen D}, Da = {20060112}, Date-Added = {2008-01-02 14:46:48 -0800}, Date-Modified = {2008-01-02 14:47:36 -0800}, Dcom = {20060413}, Doi = {10.1016/j.str.2005.09.010}, Edat = {2006/01/13 09:00}, Gr = {United Kingdom Wellcome Trust}, Issn = {0969-2126 (Print)}, Jid = {101087697}, Journal = {Structure}, Jt = {Structure (London, England : 1993)}, Keywords = {Cryoelectron Microscopy; Gene Products, env/physiology/ultrastructure; HIV-1/chemistry/growth \& development/*physiology/*ultrastructure; Humans; *Models, Biological; Models, Chemical; Viral Core Proteins/physiology/ultrastructure; Virion/chemistry/growth \& development/*physiology/*ultrastructure; Virus Assembly/*physiology}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Briggs/2006.pdf}, Lr = {20070813}, Mhda = {2006/04/14 09:00}, Number = {1}, Own = {NLM}, Pages = {15--20}, Phst = {2005/07/05 {$[$}received{$]$}; 2005/09/01 {$[$}revised{$]$}; 2005/09/03 {$[$}accepted{$]$}}, Pii = {S0969-2126(05)00389-8}, Pl = {United States}, Pmid = {16407061}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't}, Pubm = {Print}, Rn = {0 (Gene Products, env); 0 (Viral Core Proteins)}, Sb = {IM}, So = {Structure. 2006 Jan;14(1):15-20.}, Stat = {MEDLINE}, Title = {The mechanism of HIV-1 core assembly: insights from three-dimensional reconstructions of authentic virions}, Volume = {14}, Year = {2006}, Bdsk-File-1 = {YnBsaXN0MDDUAQIDBAUGCQpYJHZlcnNpb25UJHRvcFkkYXJjaGl2ZXJYJG9iamVjdHMSAAGGoNEHCFRyb290gAFfEA9OU0tleWVkQXJjaGl2ZXKoCwwXGBkdJCVVJG51bGzTDQ4PEBEUViRjbGFzc1dOUy5rZXlzWk5TLm9iamVjdHOAB6ISE4ACgAOiFRaABIAGWWFsaWFzRGF0YVxyZWxhdGl2ZVBhdGjSDRobHFdOUy5kYXRhgAVPEQGOAAAAAAGOAAIAAANoc3IAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAADBcRzJSCsAAACOyhkIMjAwNi5wZGYAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAI7J0MOhVDQAAAAAAAAAAAAEAAMAAAkgAAAAAAAAAAAAAAAAAAAABkJyaWdncwAQAAgAAMFxjUkAAAARAAgAAMOhxLQAAAABABgAjsoZAEZrzwBGatUARmobAEZkaABAiUMAAgBBaHNyOlVzZXJzOmF0b21pY3BpcmF0ZTpEb2N1bWVudHM6Q2FsdGVjaDpBcnRpY2xlczpCcmlnZ3M6MjAwNi5wZGYAAA4AEgAIADIAMAAwADYALgBwAGQAZgAPAAgAAwBoAHMAcgASAD1Vc2Vycy9hdG9taWNwaXJhdGUvRG9jdW1lbnRzL0NhbHRlY2gvQXJ0aWNsZXMvQnJpZ2dzLzIwMDYucGRmAAATAAEvAAAVAAIAE///AADSHh8gIVgkY2xhc3Nlc1okY2xhc3NuYW1loyEiI11OU011dGFibGVEYXRhVk5TRGF0YVhOU09iamVjdF8QJC4uLy4uLy4uLy4uL0FydGljbGVzL0JyaWdncy8yMDA2LnBkZtIeHyYnoicjXE5TRGljdGlvbmFyeQAIABEAGgAfACkAMgA3ADoAPwBBAFMAXABiAGkAcAB4AIMAhQCIAIoAjACPAJEAkwCdAKoArwC3ALkCSwJQAlkCZAJoAnYCfQKGAq0CsgK1AAAAAAAAAgEAAAAAAAAAKAAAAAAAAAAAAAAAAAAAAsI=}, Bdsk-Url-1 = {http://dx.doi.org/10.1016/j.str.2005.09.010}} @article{Martone:1993ek, Abstract = {The three-dimensional organization of the smooth endoplasmic reticulum (SER) in Purkinje cell dendrites in the chick cerebellum was investigated to assess the connectivity between its various components. Three-dimensional reconstructions of the SER within portions of Purkinje cell dendrites were performed from serial sections through the cerebellar molecular layer. In addition, semithick and thick sections (0.25-1 micron) of chick cerebellum in which the endomembrane system had been selectively stained were examined with an intermediate high-voltage electron microscope. Three-dimensional information was extracted from thick sections using stereo pairs and tomographic reconstructions from single axis tilt series. In contrast to its discontinuous appearance in thin sections, in both the three-dimensional reconstructions and selectively stained thick sections the endoplasmic reticulum formed a highly interconnected network of tubules and cisterns extending throughout the dendritic shaft and into the spines. Several distinct morphological domains of endoplasmic reticulum were noted, including the hypolemmal cisternae, the endomembranes associated with the dendritic spines, and the tubular and cisternal endoplasmic reticulum in the dendritic shaft. In older chicks (aged 2 weeks), stacks of endoplasmic reticulum were also noted within the dendritic shaft. All elements of the SER within the dendritic shaft and spine appeared to be continuous with one another. The results of this study strongly suggest that the endoplasmic reticulum forms a complicated network that may be part of a single endomembrane system within Purkinje cell dendrite.}, Address = {Department of Neurosciences, University of California at San Diego 92093-0608.}, Au = {Martone, ME and Zhang, Y and Simpliciano, VM and Carragher, BO and Ellisman, MH}, Author = {Martone, M E and Zhang, Y and Simpliciano, V M and Carragher, B O and Ellisman, M H}, Da = {19931208}, Date-Added = {2008-01-02 14:23:19 -0800}, Date-Modified = {2008-01-02 14:23:31 -0800}, Dcom = {19931208}, Edat = {1993/11/01}, Gr = {HL27470/HL/United States NHLBI; NS14718/NS/United States NINDS; NS26739/NS/United States NINDS; etc.}, Issn = {0270-6474 (Print)}, Jid = {8102140}, Journal = {J Neurosci}, Jt = {The Journal of neuroscience : the official journal of the Society for Neuroscience}, Keywords = {Aging/physiology; Animals; Calcium Channels/analysis; Cerebellum/growth \& development/*ultrastructure; Chickens; Computer Simulation; Dendrites/*ultrastructure; Endoplasmic Reticulum/*ultrastructure; Fluorescent Antibody Technique; Inositol 1,4,5-Trisphosphate Receptors; Inositol Phosphates/metabolism; Microscopy, Electron; Models, Anatomic; Muscle Proteins/analysis; Purkinje Cells/cytology/*ultrastructure; Receptors, Cytoplasmic and Nuclear/analysis; Ryanodine Receptor Calcium Release Channel}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Martone/1993.pdf}, Lr = {20071114}, Mhda = {1993/11/01 00:01}, Number = {11}, Own = {NLM}, Pages = {4636--4646}, Pl = {UNITED STATES}, Pmid = {8229189}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.}, Pubm = {Print}, Rn = {0 (Calcium Channels); 0 (Inositol 1,4,5-Trisphosphate Receptors); 0 (Inositol Phosphates); 0 (Muscle Proteins); 0 (Receptors, Cytoplasmic and Nuclear); 0 (Ryanodine Receptor Calcium Release Channel)}, Sb = {IM}, So = {J Neurosci. 1993 Nov;13(11):4636-46.}, Stat = {MEDLINE}, Title = {Three-dimensional visualization of the smooth endoplasmic reticulum in Purkinje cell dendrites}, Volume = {13}, Year = {1993}, Bdsk-File-1 = {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}} @article{Frey:2006qq, Abstract = {Electron microscope tomography produces three-dimensional reconstructions and has been used to image organelles both isolated and in situ, providing new insight into their structure and function. It is analogous to the various tomographies used in medical imaging. Compared with light microscopy, electron tomography offers an improvement in resolution of 30- to 80-fold and currently ranges from 3 to 8 nm, thus filling the gap between high-resolution structure determinations of isolated macromolecules and larger-scale studies on cells and tissues by light microscopy. Here, we provide an introduction to electron tomography and applications of the method in characterizing organelle architecture that also show its power for suggesting functional significance. Further improvements in labeling modalities, imaging tools, specimen preparation, and reconstruction algorithms promise to increase the quality and breadth of reconstructions by electron tomography and eventually to allow the mapping of the cellular proteomes onto detailed three-dimensional models of cellular structure.}, Address = {Department of Biology, San Diego State University, San Diego, California 92182-4614, USA. tfrey@sunstroke.sdsu.edu}, Au = {Frey, TG and Perkins, GA and Ellisman, MH}, Author = {Frey, Terrence G and Perkins, Guy A and Ellisman, Mark H}, Da = {20060512}, Date-Added = {2008-01-02 14:16:08 -0800}, Date-Modified = {2008-01-02 14:16:20 -0800}, Dcom = {20060727}, Doi = {10.1146/annurev.biophys.35.040405.102039}, Edat = {2006/05/13 09:00}, Gr = {P41 RR04050/RR/United States NCRR}, Issn = {1056-8700 (Print)}, Jid = {9211097}, Journal = {Annu Rev Biophys Biomol Struct}, Jt = {Annual review of biophysics and biomolecular structure}, Keywords = {Animals; Cell Membrane Structures/*ultrastructure; Humans; Image Enhancement/*methods; Image Interpretation, Computer-Assisted/*methods; Imaging, Three-Dimensional/*methods; Microscopy, Electron, Scanning/*methods; Organelles/*ultrastructure; Tomography, X-Ray Computed/*methods}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Frey/2006.pdf}, Lr = {20071114}, Mhda = {2006/07/28 09:00}, Own = {NLM}, Pages = {199--224}, Pl = {United States}, Pmid = {16689634}, Pst = {ppublish}, Pt = {Journal Article; Research Support, N.I.H., Extramural; Review}, Pubm = {Print}, Rf = {113}, Sb = {IM}, So = {Annu Rev Biophys Biomol Struct. 2006;35:199-224.}, Stat = {MEDLINE}, Title = {Electron tomography of membrane-bound cellular organelles}, Volume = {35}, Year = {2006}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://dx.doi.org/10.1146/annurev.biophys.35.040405.102039}} @article{Ladinsky:1999uo, Abstract = {Three-dimensional reconstructions of portions of the Golgi complex from cryofixed, freeze-substituted normal rat kidney cells have been made by dual-axis, high-voltage EM tomography at approximately 7-nm resolution. The reconstruction shown here ( approximately 1 x 1 x 4 microm3) contains two stacks of seven cisternae separated by a noncompact region across which bridges connect some cisternae at equivalent levels, but none at nonequivalent levels. The rest of the noncompact region is filled with both vesicles and polymorphic membranous elements. All cisternae are fenestrated and display coated buds. They all have about the same surface area, but they differ in volume by as much as 50%. The trans-most cisterna produces exclusively clathrin-coated buds, whereas the others display only nonclathrin coated buds. This finding challenges traditional views of where sorting occurs within the Golgi complex. Tubules with budding profiles extend from the margins of both cis and trans cisternae. They pass beyond neighboring cisternae, suggesting that these tubules contribute to traffic to and/or from the Golgi. Vesicle-filled "wells" open to both the cis and lateral sides of the stacks. The stacks of cisternae are positioned between two types of ER, cis and trans. The cis ER lies adjacent to the ER-Golgi intermediate compartment, which consists of discrete polymorphic membranous elements layered in front of the cis-most Golgi cisterna. The extensive trans ER forms close contacts with the two trans-most cisternae; this apposition may permit direct transfer of lipids between ER and Golgi membranes. Within 0.2 microm of the cisternae studied, there are 394 vesicles (8 clathrin coated, 190 nonclathrin coated, and 196 noncoated), indicating considerable vesicular traffic in this Golgi region. Our data place structural constraints on models of trafficking to, through, and from the Golgi complex.}, Address = {Laboratory for Three-Dimensional Fine Structure, Cellular, and Developmental Biology, University of Colorado, Boulder, Colorado 80309-0347, USA.}, Au = {Ladinsky, MS and Mastronarde, DN and McIntosh, JR and Howell, KE and Staehelin, LA}, Author = {Ladinsky, M S and Mastronarde, D N and McIntosh, J R and Howell, K E and Staehelin, L A}, Da = {19990614}, Date-Added = {2008-01-02 14:02:04 -0800}, Date-Modified = {2008-05-29 16:33:05 -0700}, Dcom = {19990614}, Edat = {1999/03/24}, Gr = {GM18639/GM/United States NIGMS; GM42629/GM/United States NIGMS; RR00592/RR/United States NCRR}, Jid = {0375356}, Journal = {J Cell Biol}, Jt = {The Journal of cell biology}, Keywords = {Animals; Biological Transport, Active; Cells, Cultured; Computer Graphics; Computer Simulation; Cryoelectron Microscopy; Endoplasmic Reticulum/metabolism/ultrastructure; Freeze Substitution; Golgi Apparatus/metabolism/*ultrastructure; Image Processing, Computer-Assisted/*methods; Kidney/metabolism/*ultrastructure; Lipid Metabolism; Models, Anatomic; Models, Biological; Rats}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Ladinsky/1999.pdf}, Lr = {20071114}, Mhda = {1999/03/24 00:01}, Number = {6}, Own = {NLM}, Pages = {1135--1149}, Pl = {UNITED STATES}, Pmid = {10087259}, Pst = {ppublish}, Pt = {Journal Article; Research Support, U.S. Gov't, P.H.S.}, Pubm = {Print}, Sb = {IM}, So = {J Cell Biol. 1999 Mar 22;144(6):1135-49.}, Stat = {MEDLINE}, Title = {Golgi structure in three dimensions: functional insights from the normal rat kidney cell}, Volume = {144}, Year = {1999}, Bdsk-File-1 = {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}} @article{Soldati:2006rc, Annote = {10.1038/nrm2060}, Author = {Soldati, Thierry and Schliwa, Manfred}, Date-Added = {2008-01-02 10:22:18 -0800}, Date-Modified = {2008-01-02 10:22:38 -0800}, Group = {Organelle structure}, Isbn = {1471-0072}, Journal = {Nat Rev Mol Cell Biol}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Soldati/2006.pdf}, M3 = {10.1038/nrm2060}, Number = {12}, Pages = {897--908}, Title = {Powering membrane traffic in endocytosis and recycling}, Ty = {JOUR}, Url = {http://dx.doi.org/10.1038/nrm2060}, Volume = {7}, Year = {2006}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://dx.doi.org/10.1038/nrm2060}} @article{Osteryoung:2001qd, Abstract = { The cellular machineries that power chloroplast and mitochondrial division in eukaryotes carry out the topologically challenging job of constricting and severing these double-membraned organelles. Consistent with their endosymbiotic origins, mitochondria in protists and chloroplasts in photosynthetic eukaryotes have evolved organelle-targeted forms of FtsZ, the prokaryotic ancestor of tubulin, as key components of their fission complexes. In fungi, animals and plants, mitochondria no longer utilize FtsZ for division, but several mitochondrial division proteins that localize to the outer membrane and intermembrane space, including two related to the filament-forming dynamins, have been identified in yeast and animals. Although the reactions that mediate organelle division are not yet understood, recent progress in uncovering the constituents of the organelle division machineries promises rapid advancement in our understanding of the biochemical mechanisms underlying the distinct but related processes of chloroplast and mitochondrial division in eukaryotes.}, Author = {Osteryoung, Katherine W. }, Date-Added = {2008-01-02 10:18:08 -0800}, Date-Modified = {2008-01-02 10:18:17 -0800}, Group = {Organelle structure}, Journal = {Current Opinion in Microbiology}, Keywords = {chloroplast division; mitochondrial division; organelle fusion; orgenelle evolution; plastid; FtsZ; dynamin; mcv1; fzo1}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Osteryoung/2001.pdf}, Number = {6}, Pages = {639--646}, Title = {Organelle fission in eukaryotes}, Ty = {JOUR}, Url = {http://www.sciencedirect.com/science/article/B6VS2-44HYFTX-6/2/4a530e818486402c6ed9108044094e5d}, Volume = {4}, Year = {2001}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://www.sciencedirect.com/science/article/B6VS2-44HYFTX-6/2/4a530e818486402c6ed9108044094e5d}} @article{Osteryoung:2003hl, Abstract = {Mitochondria and chloroplasts are essential eukaryotic organelles of endosymbiotic origin. Dynamic cellular machineries divide these organelles. The mechanisms by which mitochondria and chloroplasts divide were thought to be fundamentally different because chloroplasts use proteins derived from the ancestral prokaryotic cell division machinery, whereas mitochondria have largely evolved a division apparatus that lacks bacterial cell division components. Recent findings indicate, however, that both types of organelles universally require dynamin-related guanosine triphosphatases to divide. This mechanistic link provides fundamental insights into the molecular events driving the division, and possibly the evolution, of organelles in eukaryotes. }, Annote = {10.1126/science.1082192}, Author = {Osteryoung, Katherine W. and Nunnari, Jodi}, Date-Added = {2008-01-02 10:16:52 -0800}, Date-Modified = {2008-01-02 10:17:11 -0800}, Group = {Organelle structure}, Journal = {Science}, Journal1 = {Science}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Osteryoung/2003.pdf}, Number = {5651}, Pages = {1698--1704}, Title = {The Division of Endosymbiotic Organelles}, Ty = {JOUR}, Url = {http://www.sciencemag.org/cgi/content/abstract/302/5651/1698}, Volume = {302}, Year = {2003}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://www.sciencemag.org/cgi/content/abstract/302/5651/1698}} @article{Estrada-de-Martin:2005zl, Abstract = {The endoplasmic reticulum (ER) is a fundamental organelle required for protein assembly, lipid biosynthesis, and vesicular traffic, as well as calcium storage and the controlled release of calcium from the ER lumen into the cytosol. Membranes functionally linked to the ER by vesicle-mediated transport, such as the Golgi complex, endosomes, vacuoles-lysosomes, secretory vesicles, and the plasma membrane, originate largely from proteins and lipids synthesized in the ER. In this review we will discuss the structural organization of the ER and its inheritance.}, Address = {Department of Cell Biology, Yale University School of Medicine, Boyer Center for Molecular Medicine, New Haven, CT 06519, USA.}, Au = {Estrada de Martin, P and Novick, P and Ferro-Novick, S}, Author = {Estrada de Martin, Paula and Novick, Peter and Ferro-Novick, Susan}, Da = {20051207}, Date-Added = {2008-01-02 09:57:31 -0800}, Date-Modified = {2008-01-02 09:59:05 -0800}, Dcom = {20060330}, Doi = {10.1139/o05-159}, Edat = {2005/12/08 09:00}, Group = {Organelle structure}, Issn = {0829-8211 (Print)}, Jid = {8606068}, Journal = {Biochem Cell Biol}, Jt = {Biochemistry and cell biology = Biochimie et biologie cellulaire}, Keywords = {Animals; Endoplasmic Reticulum/chemistry/*physiology; Eukaryotic Cells/*physiology; Golgi Apparatus; Humans; Lipid Metabolism; Organelles; Prokaryotic Cells/*physiology; Protein Folding}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Estrada%20de%20Martin/2005.pdf}, Lr = {20061115}, Mhda = {2006/03/31 09:00}, Number = {6}, Own = {NLM}, Pages = {752--761}, Pii = {o05-159}, Pl = {Canada}, Pmid = {16333327}, Pst = {ppublish}, Pt = {Journal Article; Research Support, N.I.H., Extramural; Review}, Pubm = {Print}, Rf = {128}, Sb = {IM}, So = {Biochem Cell Biol. 2005 Dec;83(6):752-61.}, Stat = {MEDLINE}, Title = {The organization, structure, and inheritance of the ER in higher and lower eukaryotes}, Volume = {83}, Year = {2005}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://dx.doi.org/10.1139/o05-159}} @article{Hell1994, Author = {Stefan W. Hell and Jan Wichmann}, Date-Added = {2007-11-12 15:34:43 -0500}, Date-Modified = {2007-11-12 15:36:13 -0500}, Journal = {Optics Letters}, Local-Url = {file://localhost/Users/wiggins/research/Papers/3590BAF4-BDB9-137E-C02A5D131286CFD3_12352.pdf}, Pages = {780--782}, Title = {Breaking the diffraction resolution limit by stimulated emission: stimulated-emission-depletion fluorescence microscopy}, Volume = {19}, Year = {1994}, Bdsk-File-1 = {YnBsaXN0MDDUAQIDBAUGCQpYJHZlcnNpb25UJHRvcFkkYXJjaGl2ZXJYJG9iamVjdHMSAAGGoNEHCFRyb290gAFfEA9OU0tleWVkQXJjaGl2ZXKoCwwXGBkdJCVVJG51bGzTDQ4PEBEUViRjbGFzc1dOUy5rZXlzWk5TLm9iamVjdHOAB6ISE4ACgAOiFRaABIAGWWFsaWFzRGF0YVxyZWxhdGl2ZVBhdGjSDRobHFdOUy5kYXRhgAVPEQHyAAAAAAHyAAIAAApzbm93ZG9tZUhEAAAAAAAAAAAAAAAAAAAAAAC/b+bvSCsAAAAHvzgfMzU5MEJBRjQtQkRCOS0xMzdFLUMjNTU4RDFBLnBkZgAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAFWNGsNeIugAAAAAAAAAAAADAAMAAAkgAAAAAAAAAAAAAAAAAAAABlBhcGVycwAQAAgAAL9wHy8AAAARAAgAAMNeaTgAAAABABAAB784AAdyzgAGt0oADwzGAAIASHNub3dkb21lSEQ6VXNlcnM6d2lnZ2luczpyZXNlYXJjaDpQYXBlcnM6MzU5MEJBRjQtQkRCOS0xMzdFLUMjNTU4RDFBLnBkZgAOAFwALQAzADUAOQAwAEIAQQBGADQALQBCAEQAQgA5AC0AMQAzADcARQAtAEMAMAAyAEEANQBEADEAMwAxADIAOAA2AEMARgBEADMAXwAxADIAMwA1ADIALgBwAGQAZgAPABYACgBzAG4AbwB3AGQAbwBtAGUASABEABIAS1VzZXJzL3dpZ2dpbnMvcmVzZWFyY2gvUGFwZXJzLzM1OTBCQUY0LUJEQjktMTM3RS1DMDJBNUQxMzEyODZDRkQzXzEyMzUyLnBkZgAAEwABLwAAFQACAA7//wAA0h4fICFYJGNsYXNzZXNaJGNsYXNzbmFtZaMhIiNdTlNNdXRhYmxlRGF0YVZOU0RhdGFYTlNPYmplY3RfEEYuLi8uLi8uLi9yZXNlYXJjaC9QYXBlcnMvMzU5MEJBRjQtQkRCOS0xMzdFLUMwMkE1RDEzMTI4NkNGRDNfMTIzNTIucGRm0h4fJieiJyNcTlNEaWN0aW9uYXJ5AAgAEQAaAB8AKQAyADcAOgA/AEEAUwBcAGIAaQBwAHgAgwCFAIgAigCMAI8AkQCTAJ0AqgCvALcAuQKvArQCvQLIAswC2gLhAuoDMwM4AzsAAAAAAAACAQAAAAAAAAAoAAAAAAAAAAAAAAAAAAADSA==}} @article{Betzig:2006lr, Abstract = {We introduce a method for optically imaging intracellular proteins at nanometer spatial resolution. Numerous sparse subsets of photoactivatable fluorescent protein molecules were activated, localized (to approximately 2 to 25 nanometers), and then bleached. The aggregate position information from all subsets was then assembled into a superresolution image. We used this method--termed photoactivated localization microscopy--to image specific target proteins in thin sections of lysosomes and mitochondria; in fixed whole cells, we imaged vinculin at focal adhesions, actin within a lamellipodium, and the distribution of the retroviral protein Gag at the plasma membrane.}, Address = {Howard Hughes Medical Institute, Janelia Farm Research Campus, Ashburn, VA 20147, USA. betzige@janelia.hhmi.org}, Au = {Betzig, E and Patterson, GH and Sougrat, R and Lindwasser, OW and Olenych, S and Bonifacino, JS and Davidson, MW and Lippincott-Schwartz, J and Hess, HF}, Author = {Betzig, Eric and Patterson, George H and Sougrat, Rachid and Lindwasser, O Wolf and Olenych, Scott and Bonifacino, Juan S and Davidson, Michael W and Lippincott-Schwartz, Jennifer and Hess, Harald F}, Da = {20060915}, Date-Added = {2007-11-12 15:28:30 -0500}, Date-Modified = {2007-12-13 10:27:57 -0800}, Dcom = {20060925}, Dep = {20060810}, Doi = {10.1126/science.1127344}, Edat = {2006/08/12 09:00}, Issn = {1095-9203 (Electronic)}, Jid = {0404511}, Journal = {Science}, Jt = {Science (New York, N.Y.)}, Keywords = {Actins/analysis; Algorithms; Animals; COS Cells; Cell Line; Cell Membrane/*chemistry; Cercopithecus aethiops; Fluorescence; Focal Adhesions/chemistry; Gene Products, gag/analysis; HIV-1; Light; Luminescent Proteins/*analysis; Lysosomes/chemistry; Microscopy/*methods; Mitochondria/chemistry; *Nanotechnology; Organelles/*chemistry; Photobleaching; Proteins/*analysis; Pseudopodia/chemistry; Recombinant Fusion Proteins/*analysis; Vinculin/analysis}, Language = {eng}, Lr = {20070319}, Mhda = {2006/09/26 09:00}, Number = {5793}, Own = {NLM}, Pages = {1642--1645}, Phst = {2006/08/10 {$[$}aheadofprint{$]$}}, Pii = {1127344}, Pl = {United States}, Pmid = {16902090}, Pst = {ppublish}, Pt = {Journal Article; Research Support, N.I.H., Extramural}, Pubm = {Print-Electronic}, Rn = {0 (Actins); 0 (Gene Products, gag); 0 (Luminescent Proteins); 0 (Proteins); 0 (Recombinant Fusion Proteins); 125361-02-6 (Vinculin)}, Sb = {IM}, So = {Science. 2006 Sep 15;313(5793):1642-5. Epub 2006 Aug 10.}, Stat = {MEDLINE}, Title = {Imaging intracellular fluorescent proteins at nanometer resolution}, Volume = {313}, Year = {2006}, Bdsk-Url-1 = {http://dx.doi.org/10.1126/science.1127344}} @article{Guven:2004sp, Author = {Guven, J.}, Date = {JUL 16}, Date-Added = {2007-10-22 23:13:23 -0400}, Date-Modified = {2007-10-22 23:13:23 -0400}, Isi = {ISI:000223017100002}, Issn = {0305-4470}, Journal = {JOURNAL OF PHYSICS A-MATHEMATICAL AND GENERAL}, Month = {Jul}, Number = {28}, Pages = {L313--L319}, Publication-Type = {J}, Title = {Membrane geometry with auxiliary variables and quadratic constraints}, Volume = {37}, Year = {2004}} @article{Capovilla:2004ij, Author = {Capovilla, R. and Guven, J.}, Date = {JUN 11}, Date-Added = {2007-10-22 23:13:23 -0400}, Date-Modified = {2007-10-22 23:17:59 -0400}, Isi = {ISI:000222543300003}, Issn = {0305-4470}, Journal = {Journal of Physics A-Mathematical and General}, Local-Url = {file://localhost/Users/wiggins/research/Papers/CApovilla2004.pdf}, Month = {Jun}, Number = {23}, Pages = {5983--6001}, Publication-Type = {J}, Title = {Second variation of the Helfrich-Canham Hamiltonian and reparametrization invariance}, Volume = {37}, Year = {2004}, Bdsk-File-1 = {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}} @article{Capovilla:2004th, Author = {Capovilla, R and Guven, J}, Date = {JUN 9}, Date-Added = {2007-10-22 23:13:23 -0400}, Date-Modified = {2008-05-29 16:49:38 -0700}, Isi = {ISI:000222194000019}, Journal = {J Phys---Condens Mat}, Local-Url = {file://localhost/Users/wiggins/research/Papers/Capovilla2004b.pdf}, Month = {Jun}, Number = {22}, Pages = {S2187--S2191}, Publication-Type = {J}, Special-Issue = {Sp. Iss. 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A.}, Date = {JUN 13}, Date-Added = {2007-10-22 23:13:23 -0400}, Date-Modified = {2007-10-22 23:18:15 -0400}, Isi = {ISI:000184057000008}, Issn = {0305-4470}, Journal = {Journal of Physics A-Mathematical and General}, Local-Url = {file://localhost/Users/wiggins/research/Papers/Caqpovilla2003.pdf}, Month = {Jun}, Number = {23}, Pages = {6281--6295}, Publication-Type = {J}, Title = {Deformations of the geometry of lipid vesicles}, Volume = {36}, Year = {2003}, Bdsk-File-1 = 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@article{Capovilla:2002fy, Author = {Capovilla, R. and Guven, J.}, Date = {OCT}, Date-Added = {2007-10-22 23:13:23 -0400}, Date-Modified = {2007-10-22 23:15:35 -0400}, Di = {ARTN 041604}, Isi = {ISI:000179176100052}, Issn = {1063-651X}, Journal = {Physical Review E}, Local-Url = {file://localhost/Users/wiggins/research/Papers/Capovilla2002.pdf}, Month = {Oct}, Number = {4}, Pages = {041604}, Part-Number = {Part 1}, Publication-Type = {J}, Title = {Geometry of lipid vesicle adhesion}, Volume = {66}, Year = {2002}, Bdsk-File-1 = 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@article{Capovilla:2005ai, Author = {Capovilla, R. and Guven, J. and Rojas, E.}, Date = {SEP 23}, Date-Added = {2007-10-22 23:13:14 -0400}, Date-Modified = {2007-10-22 23:16:19 -0400}, Isi = {ISI:000234012200004}, Issn = {0305-4470}, Journal = {Journal of Physics A-Mathematical and General}, Local-Url = {file://localhost/Users/wiggins/research/Papers/Capovilla2005.pdf}, Month = {Sep}, Number = {38}, Pages = {8201--8210}, Publication-Type = {J}, Title = {Hamilton's equations for a fluid membrane: axial symmetry}, Volume = {38}, Year = {2005}, Bdsk-File-1 = 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@article{Castro-Villarreal:2007kl, Af = {Castro-Villarreal, Pavel Guven, Jemal}, Author = {Castro-Villarreal, P. and Guven, J.}, Date = {APR 20}, Date-Added = {2007-10-22 23:13:11 -0400}, Date-Modified = {2007-10-22 23:14:13 -0400}, Isi = {ISI:000246070700005}, Issn = {1751-8113}, Journal = {JOURNAL OF PHYSICS A-MATHEMATICAL AND THEORETICAL}, Local-Url = {file://localhost/Users/wiggins/research/Papers/Castro2007b.pdf}, Month = {Apr}, Number = {16}, Pages = {4273--4283}, Publication-Type = {J}, Title = {Axially symmetric membranes with polar tethers}, Volume = {40}, Year = {2007}, Bdsk-File-1 = 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@article{Guven:2006qe, Author = {Guven, J.}, Date = {APR 7}, Date-Added = {2007-10-22 23:13:09 -0400}, Date-Modified = {2007-10-22 23:13:09 -0400}, Isi = {ISI:000237152500022}, Issn = {0305-4470}, Journal = {JOURNAL OF PHYSICS A-MATHEMATICAL AND GENERAL}, Month = {Apr}, Number = {14}, Pages = {3771--3785}, Publication-Type = {J}, Title = {Laplace pressure as a surface stress in fluid vesicles}, Volume = {39}, Year = {2006}} @article{Fournier:2007oq, Af = {Fournier, Jean-Baptiste}, Author = {Fournier, J. B.}, Date-Added = {2007-10-22 23:13:06 -0400}, Date-Modified = {2007-10-22 23:18:42 -0400}, Isi = {ISI:000247367400013}, Issn = {1744-683X}, Journal = {Soft Matter}, Local-Url = {file://localhost/Users/wiggins/research/Papers/Fournier2007.pdf}, Number = {7}, Pages = {883--888}, Publication-Type = {J}, Title = {On the stress and torque tensors in fluid membranes}, Volume = {3}, Year = {2007}, Bdsk-File-1 = {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}} @article{Capovilla:2002nx, Author = {Capovilla, R. and Chryssomalakos, C. and Guven, J.}, Date = {AUG 9}, Date-Added = {2007-10-22 23:13:03 -0400}, Date-Modified = {2007-10-22 23:13:03 -0400}, Isi = {ISI:000177801300008}, Issn = {0305-4470}, Journal = {Journal of Physics A-Mathematical and General}, Month = {Aug}, Number = {31}, Pages = {6571--6587}, Publication-Type = {J}, Title = {Hamiltonians for curves}, Volume = {35}, Year = {2002}} @article{Capovilla:2002wd, Author = {Capovilla, R. and Guven, J.}, Date = {AUG 2}, Date-Added = {2007-10-22 23:13:00 -0400}, Date-Modified = {2007-10-22 23:14:54 -0400}, Isi = {ISI:000177598700003}, Issn = {0305-4470}, Journal = {Journal of Physics A-Mathematical and General}, Local-Url = {file://localhost/Users/wiggins/research/Papers/Capovilla2002b.pdf}, Month = {Aug}, Number = {30}, Pages = {6233--6247}, Publication-Type = {J}, Title = {Stresses in lipid membranes}, Volume = {35}, Year = {2002}, Bdsk-File-1 = {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}} @article{Norouzi:2006dq, Af = {Norouzi, Davood Mueller, Martin Michael Deserno, Markus}, Author = {Norouzi, D. and Muller, M. M. and Deserno, M.}, Date = {DEC}, Date-Added = {2007-10-22 22:48:54 -0400}, Date-Modified = {2007-10-22 22:48:54 -0400}, Di = {ARTN 061914}, Isi = {ISI:000243165300076}, Issn = {1539-3755}, Journal = {PHYSICAL REVIEW E}, Month = {Dec}, Number = {6}, Pages = {061914}, Part-Number = {Part 1}, Publication-Type = {J}, Title = {How to determine local elastic properties of lipid bilayer membranes from atomic-force-microscope measurements: A theoretical analysis}, Volume = {74}, Year = {2006}} @article{Muller:2005lq, Author = {Muller, M. M. and Deserno, M. and Guven, A.}, Date = {FEB}, Date-Added = {2007-10-22 22:48:37 -0400}, Date-Modified = {2007-10-22 22:48:49 -0400}, Isi = {ISI:000227070200027}, Issn = {0295-5075}, Journal = {EUROPHYSICS LETTERS}, Local-Url = {file://localhost/Users/wiggins/research/Papers/Muller2005.pdf}, Month = {Feb}, Number = {3}, Pages = {482--488}, Publication-Type = {J}, Title = {Geometry of surface-mediated interactions}, Volume = {69}, Year = {2005}, Bdsk-File-1 = {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}} @article{Cooke:2006ve, Author = {Cooke, I. R. and Deserno, M.}, Date = {JUL 15}, Date-Added = {2007-10-22 22:39:58 -0400}, Date-Modified = {2007-10-22 22:47:33 -0400}, Isi = {ISI:000238611700013}, Issn = {0006-3495}, Journal = {BIOPHYSICAL JOURNAL}, Local-Url = {file://localhost/Users/wiggins/research/Papers/Cooke2006.pdf}, Month = {Jul}, Number = {2}, Pages = {487--495}, Publication-Type = {J}, Title = {Coupling between lipid shape and membrane curvature}, Volume = {91}, Year = {2006}, Bdsk-File-1 = {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}} @article{Muller:2005ly, Abstract = {Particles bound to an interface interact because they deform its shape. The stresses that result are fully encoded in the geometry and described by a divergence-free surface stress tensor. This stress tensor can be used to express the force on a particle as a line integral along any conveniently chosen closed contour that surrounds the particle. The resulting expression is exact (i.e., free of any "smallness" assumptions) and independent of the chosen surface parametrization. Additional surface degrees of freedom, such as vector fields describing lipid tilt, are readily included in this formalism. As an illustration, we derive the exact force for several important surface Hamiltonians in various symmetric two-particle configurations in terms of the midplane geometry; its sign is evident in certain interesting limits. Specializing to the linear regime, where the shape can be analytically determined, these general expressions yield force-distance relations, several of which have originally been derived by using an energy-based approach.}, Address = {Max-Planck-Institut fur Polymerforschung, Ackermannweg 10, 55128 Mainz, Germany.}, Au = {Muller, MM and Deserno, M and Guven, J}, Author = {Muller, Martin Michael and Deserno, Markus and Guven, Jemal}, Da = {20060220}, Date-Added = {2007-10-22 22:30:54 -0400}, Date-Modified = {2007-10-22 22:48:32 -0400}, Dcom = {20060427}, Dep = {20051229}, Edat = {2006/02/21 09:00}, Issn = {1539-3755 (Print)}, Jid = {101136452}, Journal = {Phys Rev E Stat Nonlin Soft Matter Phys}, Jt = {Physical review. E, Statistical, nonlinear, and soft matter physics}, Language = {eng}, Local-Url = {file://localhost/Users/wiggins/research/Papers/Muller2005b.pdf}, Mhda = {2006/02/21 09:01}, Number = {6 Pt 1}, Own = {NLM}, Pages = {061407}, Phst = {2005/05/23 {$[$}received{$]$}; 2005/09/14 {$[$}revised{$]$}; 2005/12/29 {$[$}aheadofprint{$]$}}, Pl = {United States}, Pmid = {16485947}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print-Electronic}, So = {Phys Rev E Stat Nonlin Soft Matter Phys. 2005 Dec;72(6 Pt 1):061407. Epub 2005 Dec 29.}, Stat = {PubMed-not-MEDLINE}, Title = {Interface-mediated interactions between particles: a geometrical approach.}, Volume = {72}, Year = {2005}, Bdsk-File-1 = {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}} @article{Puig-de-Morales-Marinkovic:2007ys, Abstract = {We report here the first measurements of the complex modulus of the isolated red blood cell (RBC). Because the RBC is often larger than capillary diameter, important determinants of microcirculatory function are RBC deformability and its changes with pathologies, such as sickle cell disease and malaria. A functionalized ferrimagnetic microbead was attached to the membrane of healthy RBC and then subjected to an oscillatory magnetic field. The resulting torque caused cell deformation. From the oscillatory forcing and resulting bead motions, which were tracked optically, we computed elastic and frictional moduli, g' and g", respectively, from 0.1 to 100 Hz. The g' was nearly frequency independent and dominated the response at all but the highest frequencies measured. Over three frequency decades, g" increased as a power law with an exponent of 0.64, a result not predicted by any simple model. These data suggest that RBC relaxation times that have been reported previously, and any models that rest upon them, are artifactual; the artifact, we suggest, arises from forcing to an exponential fit data of limited temporal duration. A linear range of response was observed, but, as forcing amplitude increased, nonlinearities became clearly apparent. A finite element model suggests that membrane bending was localized to the vicinity of the bead and dominated membrane shear. While the mechanisms accounting for these RBC dynamics remain unclear, methods described here establish new avenues for the exploration of connections among the mechanical, chemical, and biological characteristics of the RBC in health and disease.}, Address = {Program in Molecular and Integrative Physiological Sciences (MIPS Dept of Environmental Health, Harvard School of Public Health, Boston, MA 02115, USA. mpuigdem@hsph.harvard.edu}, Au = {Puig-de-Morales-Marinkovic, M and Turner, KT and Butler, JP and Fredberg, JJ and Suresh, S}, Author = {Puig-de-Morales-Marinkovic, Marina and Turner, Kevin T and Butler, James P and Fredberg, Jeffrey J and Suresh, Subra}, Da = {20070806}, Date-Added = {2007-10-22 22:30:51 -0400}, Date-Modified = {2007-10-22 22:34:45 -0400}, Dcom = {20070920}, Dep = {20070411}, Doi = {10.1152/ajpcell.00562.2006}, Edat = {2007/04/13 09:00}, Gr = {1 R01 GM076689-01/GM/NIGMS; HL33009/HL/NHLBI; HL59682/HL/NHLBI; HL65960/HL/NHLBI}, Issn = {0363-6143 (Print)}, Jid = {100901225}, Journal = {Am J Physiol Cell Physiol}, Jt = {American journal of physiology. Cell physiology}, Keywords = {Cells, Cultured; Elasticity; *Erythrocyte Deformability; Erythrocytes/*physiology; Ferric Compounds/chemistry; Finite Element Analysis; Flow Cytometry; Hemorheology/*methods; Humans; Linear Models; Magnetics; Microspheres; *Models, Cardiovascular; Nonlinear Dynamics; Optics; Oscillometry; Reproducibility of Results; Stress, Mechanical; Time Factors; Torque; Viscosity}, Language = {eng}, Local-Url = {file://localhost/Users/wiggins/research/Papers/Marinkovic2007.pdf}, Mhda = {2007/09/21 09:00}, Number = {2}, Own = {NLM}, Pages = {C597-605}, Phst = {2007/04/11 {$[$}aheadofprint{$]$}}, Pii = {00562.2006}, Pl = {United States}, Pmid = {17428838}, Pst = {ppublish}, Pt = {Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't}, Pubm = {Print-Electronic}, Rn = {0 (Ferric Compounds); 1309-37-1 (ferric oxide)}, Sb = {IM}, So = {Am J Physiol Cell Physiol. 2007 Aug;293(2):C597-605. Epub 2007 Apr 11.}, Stat = {MEDLINE}, Title = {Viscoelasticity of the human red blood cell.}, Volume = {293}, Year = {2007}, Bdsk-Url-1 = {http://dx.doi.org/10.1152/ajpcell.00562.2006}} @article{Muller:2007fr, Abstract = {Torques on interfaces can be described by a divergence-free tensor which is fully encoded in the geometry. This tensor consists of two terms, one originating in the couple of the stress, the other capturing an intrinsic contribution due to curvature. In analogy to the description of forces in terms of a stress tensor, the torque on a particle can be expressed as a line integral along a contour surrounding the particle. Interactions between particles mediated by a fluid membrane are studied within this framework. In particular, torque balance places a strong constraint on the shape of the membrane. Symmetric two-particle configurations admit simple analytical expressions which are valid in the fully nonlinear regime; in particular, the problem may be solved exactly in the case of two membrane-bound parallel cylinders. This apparently simple system provides some flavor of the remarkably subtle nonlinear behavior associated with membrane-mediated interactions.}, Address = {Max-Planck-Institut fur Polymerforschung, Ackermannweg 10, 55128 Mainz, Germany.}, Au = {Muller, MM and Deserno, M and Guven, J}, Author = {Muller, Martin Michael and Deserno, Markus and Guven, Jemal}, Da = {20070806}, Date-Added = {2007-10-22 22:30:51 -0400}, Date-Modified = {2007-10-22 22:33:37 -0400}, Dep = {20070726}, Edat = {2007/08/07 09:00}, Issn = {1539-3755 (Print)}, Jid = {101136452}, Journal = {Phys Rev E Stat Nonlin Soft Matter Phys}, Jt = {Physical review. E, Statistical, nonlinear, and soft matter physics}, Language = {eng}, Local-Url = {file://localhost/Users/wiggins/research/Papers/Muller2007.pdf}, Mhda = {2007/08/07 09:00}, Number = {1 Pt 1}, Own = {NLM}, Pages = {011921}, Phst = {2007/02/09 {$[$}received{$]$}; 2007/07/26 {$[$}aheadofprint{$]$}}, Pl = {United States}, Pmid = {17677508}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't}, Pubm = {Print-Electronic}, Sb = {IM}, So = {Phys Rev E Stat Nonlin Soft Matter Phys. 2007 Jul;76(1 Pt 1):011921. Epub 2007 Jul 26.}, Stat = {In-Process}, Title = {Balancing torques in membrane-mediated interactions: exact results and numerical illustrations.}, Volume = {76}, Year = {2007}, Bdsk-File-1 = {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}} @article{Castro-Villarreal:2007zr, Abstract = {Under inversion in any (interior) point, a catenoid transforms into a deflated compact geometry which touches at two points (its poles). The catenoid is a minimal surface and, as such, is an equilibrium shape of a symmetric fluid membrane. The conformal symmetry of the Hamiltonian implies that inverted minimal surfaces are also equilibrium shapes. However, they will exhibit curvature singularities at their poles. Such singularities are the geometrical signature of the external forces required to pull the poles together. These forces will set up stresses in the inverted shapes. Tuning the force corresponds geometrically to the translation of the point of inversion. For any fixed surface area, there will be a maximum force. The associated shape is a symmetric discocyte. Lowering the external force will induce a transition from the discocyte to a cup-shaped stomatocyte.}, Address = {Instituto de Ciencias Nucleares, Universidad Nacional Autonoma de Mexico, Apdo. Postal 70-543, 04510 Mexico, DF, Mexico.}, Au = {Castro-Villarreal, P and Guven, J}, Author = {Castro-Villarreal, Pavel and Guven, Jemal}, Da = {20070806}, Date-Added = {2007-10-22 22:30:51 -0400}, Date-Modified = {2007-10-22 23:13:51 -0400}, Dep = {20070727}, Edat = {2007/08/07 09:00}, Issn = {1539-3755 (Print)}, Jid = {101136452}, Journal = {Phys Rev E Stat Nonlin Soft Matter Phys}, Jt = {Physical review. E, Statistical, nonlinear, and soft matter physics}, Language = {eng}, Local-Url = {file://localhost/Users/wiggins/research/Papers/Castro2007.pdf}, Mhda = {2007/08/07 09:00}, Number = {1 Pt 1}, Own = {NLM}, Pages = {011922}, Phst = {2007/02/13 {$[$}received{$]$}; 2007/07/27 {$[$}aheadofprint{$]$}}, Pl = {United States}, Pmid = {17677509}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't}, Pubm = {Print-Electronic}, Sb = {IM}, So = {Phys Rev E Stat Nonlin Soft Matter Phys. 2007 Jul;76(1 Pt 1):011922. Epub 2007 Jul 27.}, Stat = {In-Process}, Title = {Inverted catenoid as a fluid membrane with two points pulled together.}, Volume = {76}, Year = {2007}, Bdsk-File-1 = {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}} @article{Deserno:2007mz, Abstract = {When a fluid surface adheres to a substrate, the location of the contact line adjusts in order to minimize the overall energy. This implies boundary conditions which depend on the characteristic surface deformation energies. We develop a general geometrical framework within which these conditions can be derived in a completely systematic way. We treat both adhesion to a rigid substrate and adhesion between two fluid surfaces, and illustrate our general results for several important Hamiltonians involving both curvature and curvature gradients. Some of these have previously been studied using very different techniques. With the exception of capillary phenomena, the Hamiltonian will not only be sensitive to boundary translations, but may also respond to changes in slope and even in curvature. The functional form of the additional contributions will follow readily from our treatment. We will show that the boundary conditions describing adhesion between two fluid surfaces express the balance of stresses and torques, as one would expect. At a rigid substrate, however, this simple identification will generally fail. This is because local rotations of the surface normal will be entirely "enslaved" to translations on the substrate. As a consequence, stresses and torques enter a single balance condition and cannot be disentangled.}, Address = {Max-Planck-Institut fur Polymerforschung, Ackermannweg 10, 55128 Mainz, Germany.}, Au = {Deserno, M and Muller, MM and Guven, J}, Author = {Deserno, Markus and Muller, Martin Michael and Guven, Jemal}, Da = {20070806}, Date-Added = {2007-10-22 22:30:51 -0400}, Date-Modified = {2007-10-22 22:35:19 -0400}, Dep = {20070726}, Edat = {2007/08/07 09:00}, Issn = {1539-3755 (Print)}, Jid = {101136452}, Journal = {Phys Rev E Stat Nonlin Soft Matter Phys}, Jt = {Physical review. E, Statistical, nonlinear, and soft matter physics}, Language = {eng}, Local-Url = {file://localhost/Users/wiggins/research/Papers/Deserno2007.pdf}, Mhda = {2007/08/07 09:00}, Number = {1 Pt 1}, Own = {NLM}, Pages = {011605}, Phst = {2007/03/01 {$[$}received{$]$}; 2007/07/26 {$[$}aheadofprint{$]$}}, Pl = {United States}, Pmid = {17677462}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't}, Pubm = {Print-Electronic}, Sb = {IM}, So = {Phys Rev E Stat Nonlin Soft Matter Phys. 2007 Jul;76(1 Pt 1):011605. Epub 2007 Jul 26.}, Stat = {In-Process}, Title = {Contact lines for fluid surface adhesion.}, Volume = {76}, Year = {2007}, Bdsk-File-1 = {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}} @article{Mills:2004yq, Abstract = {Studies of the deformation characteristics of single biological cells can offer insights into the connections among mechanical state, biochemical response and the onset and progression of diseases. Deformation imposed by optical tweezers provides a useful means for the study of single cell mechanics under a variety of well-controlled stress-states. In this paper, we first critically review recent advances in the study of single cell mechanics employing the optical tweezers method, and assess its significance and limitations in comparison to other experimental tools. We then present new experimental and computational results on shape evolution, force-extension curves, elastic properties and viscoelastic response of human red blood cells subjected to large elastic deformation using optical tweezers. Potential applications of the methods examined here to study diseased cells are also briefly addressed.}, Address = {Department of Materials Science and Engineering. National University of Singapore, Singapore 117576, Singapore.}, Au = {Mills, JP and Qie, L and Dao, M and Lim, CT and Suresh, S}, Author = {Mills, J P and Qie, L and Dao, M and Lim, C T and Suresh, S}, Da = {20060620}, Date-Added = {2007-10-22 22:05:24 -0400}, Date-Modified = {2007-10-22 22:05:24 -0400}, Dcom = {20060705}, Edat = {2006/06/21 09:00}, Issn = {1546-2048 (Print)}, Jid = {101258184}, Journal = {Mech Chem Biosyst}, Jt = {Mechanics \& chemistry of biosystems : MCB}, Keywords = {*Elasticity; *Erythrocyte Deformability; Humans; Optics/*instrumentation; *Viscosity}, Language = {eng}, Lr = {20061115}, Mhda = {2006/07/06 09:00}, Number = {3}, Own = {NLM}, Pages = {169--180}, Pl = {United States}, Pmid = {16783930}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't; Review}, Pubm = {Print}, Rf = {29}, Sb = {IM}, So = {Mech Chem Biosyst. 2004 Sep;1(3):169-80.}, Stat = {MEDLINE}, Title = {Nonlinear elastic and viscoelastic deformation of the human red blood cell with optical tweezers.}, Volume = {1}, Year = {2004}} @article{Seifert:1997kx, Author = {Seifert, U}, Date = {JAN-FEB}, Date-Added = {2007-10-22 16:07:18 -0400}, Date-Modified = {2008-05-29 16:42:47 -0700}, Isi = {ISI:A1997WE91800002}, Issn = {0001-8732}, Journal = {Adv Phys}, Month = {Jan--Feb}, Number = {1}, Pages = {13--137}, Publication-Type = {J}, Title = {Configurations of fluid membranes and vesicles}, Volume = {46}, Year = {1997}, Bdsk-File-1 = {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}} @article{Dabora:1988uq, Abstract = {The formation of a dynamic tubulovesicular membrane network that resembles the endoplasmic reticulum (ER) has been observed in extracts of cultured chick embryo fibroblasts (CEF cells) using video-enhanced differential interference contrast microscopy. Initially, membranes in the CEF extracts appeared amorphous and aggregated, but with time, membrane tubules moved out along stationary microtubules. The membrane tubules formed new branches on intersecting microtubules and fused with other branches to form a network of interconnected polygons. The tubulovesicular network was solubilized by detergent and took on a beaded morphology in a hypotonic buffer. Formation of the tubulovesicular network required ATP and microtubules. The network did not contain elements of the plasma membrane, Golgi apparatus, or mitochondria but could be labeled with ER markers. We suggest that the tubulovesicular network contains components from the ER and is formed by membrane associated motors moving upon microtubules in a process we call microtubule-dependent tethering.}, Address = {Department of Cell Biology and Physiology, Washington University Medical School, St. Louis, Missouri 63110.}, Au = {Dabora, SL and Sheetz, MP}, Author = {Dabora, S L and Sheetz, M P}, Da = {19880810}, Date-Added = {2007-10-03 14:38:41 -0400}, Date-Modified = {2007-10-03 14:38:41 -0400}, Dcom = {19880810}, Edat = {1988/07/01}, Gr = {GM-36277/GM/NIGMS; NS-23345/NS/NINDS}, Issn = {0092-8674 (Print)}, Jid = {0413066}, Journal = {Cell}, Jt = {Cell}, Keywords = {Adenosine Triphosphate/physiology; Animals; Cells, Cultured; Chick Embryo; Endoplasmic Reticulum/*ultrastructure; Fibroblasts; Fluorescent Antibody Technique; Freeze Etching; Freeze Fracturing; Microscopy, Electron; Microscopy, Interference; Microtubules/*ultrastructure; Models, Biological; Osmolar Concentration}, Language = {eng}, Lr = {20061115}, Mhda = {1988/07/01 00:01}, Number = {1}, Own = {NLM}, Pages = {27--35}, Pl = {UNITED STATES}, Pmid = {3289756}, Pst = {ppublish}, Pt = {Journal Article; Research Support, U.S. Gov't, P.H.S.}, Pubm = {Print}, Rn = {56-65-5 (Adenosine Triphosphate)}, Sb = {IM}, So = {Cell. 1988 Jul 1;54(1):27-35.}, Stat = {MEDLINE}, Title = {The microtubule-dependent formation of a tubulovesicular network with characteristics of the ER from cultured cell extracts.}, Volume = {54}, Year = {1988}} @article{Roux:2005qy, Abstract = {We have recently developed a minimal system for generating long tubular nanostructures that resemble tubes observed in vivo with biological membranes. Here, we studied membrane tube pulling in ternary mixtures of sphingomyelin, phosphatidylcholine and cholesterol. Two salient results emerged: the lipid composition is significantly different in the tubes and in the vesicles; tube fission is observed when phase separation is generated in the tubes. This shows that lipid sorting may depend critically on both membrane curvature and phase separation. Phase separation also appears to be important for membrane fission in tubes pulled out of giant liposomes or purified Golgi membranes.}, Address = {UMR 144 CNRS/Institut Curie, Paris, France.}, Au = {Roux, A and Cuvelier, D and Nassoy, P and Prost, J and Bassereau, P and Goud, B}, Author = {Roux, Aurelien and Cuvelier, Damien and Nassoy, Pierre and Prost, Jacques and Bassereau, Patricia and Goud, Bruno}, Da = {20050603}, Date-Added = {2007-10-03 14:38:39 -0400}, Date-Modified = {2007-10-03 14:39:02 -0400}, Dcom = {20050712}, Dep = {20050324}, Doi = {10.1038/sj.emboj.7600631}, Edat = {2005/03/26 09:00}, Issn = {0261-4189 (Print)}, Jid = {8208664}, Journal = {EMBO J}, Jt = {The EMBO journal}, Keywords = {Brain Chemistry; Cell Membrane/*chemistry/metabolism; Cholesterol/*chemistry/metabolism; Elasticity; Golgi Apparatus/chemistry; Lipid Bilayers/chemistry; Phosphatidylcholines/*chemistry/metabolism; Photochemistry; Sphingomyelins/*chemistry/metabolism; Stress, Mechanical}, Language = {eng}, Local-Url = {file://localhost/Users/wiggins/research/Papers/Roux2005.pdf}, Lr = {20061115}, Mhda = {2005/07/13 09:00}, Number = {8}, Own = {NLM}, Pages = {1537--1545}, Phst = {2005/01/17 {$[$}received{$]$}; 2005/02/25 {$[$}accepted{$]$}; 2005/03/24 {$[$}aheadofprint{$]$}}, Pii = {7600631}, Pl = {England}, Pmid = {15791208}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't}, Pubm = {Print-Electronic}, Rn = {0 (Lipid Bilayers); 0 (Phosphatidylcholines); 0 (Sphingomyelins); 57-88-5 (Cholesterol)}, Sb = {IM}, So = {EMBO J. 2005 Apr 20;24(8):1537-45. Epub 2005 Mar 24.}, Stat = {MEDLINE}, Title = {Role of curvature and phase transition in lipid sorting and fission of membrane tubules.}, Volume = {24}, Year = {2005}, Bdsk-Url-1 = {http://dx.doi.org/10.1038/sj.emboj.7600631}} @article{Reynwar:2007lr, Abstract = {Membrane remodelling plays an important role in cellular tasks such as endocytosis, vesiculation and protein sorting, and in the biogenesis of organelles such as the endoplasmic reticulum or the Golgi apparatus. It is well established that the remodelling process is aided by specialized proteins that can sense as well as create membrane curvature, and trigger tubulation when added to synthetic liposomes. Because the energy needed for such large-scale changes in membrane geometry significantly exceeds the binding energy between individual proteins and between protein and membrane, cooperative action is essential. It has recently been suggested that curvature-mediated attractive interactions could aid cooperation and complement the effects of specific binding events on membrane remodelling. But it is difficult to experimentally isolate curvature-mediated interactions from direct attractions between proteins. Moreover, approximate theories predict repulsion between isotropically curving proteins. Here we use coarse-grained membrane simulations to show that curvature-inducing model proteins adsorbed on lipid bilayer membranes can experience attractive interactions that arise purely as a result of membrane curvature. We find that once a minimal local bending is realized, the effect robustly drives protein cluster formation and subsequent transformation into vesicles with radii that correlate with the local curvature imprint. Owing to its universal nature, curvature-mediated attraction can operate even between proteins lacking any specific interactions, such as newly synthesized and still immature membrane proteins in the endoplasmic reticulum.}, Address = {Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany.}, Au = {Reynwar, BJ and Illya, G and Harmandaris, VA and Muller, MM and Kremer, K and Deserno, M}, Author = {Reynwar, B J and Illya, G and Harmandaris, V A and Muller, M M and Kremer, K and Deserno, M}, Cin = {Nature. 2007 May 24;447(7143):387-9. PMID: 17522663}, Da = {20070524}, Date-Added = {2007-10-03 14:27:45 -0400}, Date-Modified = {2008-05-29 16:39:20 -0700}, Dcom = {20070607}, Edat = {2007/05/25 09:00}, Jid = {0410462}, Journal = {Nature}, Jt = {Nature}, Keywords = {Capsid/chemistry/metabolism/ultrastructure; Cell Membrane/chemistry/metabolism/ultrastructure; Colloids/chemistry; Computer Simulation; Endoplasmic Reticulum/chemistry/metabolism; Lipid Bilayers/*chemistry/*metabolism; Lipids/analysis/chemistry; Membrane Proteins/*chemistry/*metabolism; Models, Molecular; Nanoparticles/chemistry; Protein Binding}, Language = {eng}, Local-Url = {file://localhost/Users/wiggins/research/Papers/Reynwar2007.pdf}, Mhda = {2007/06/08 09:00}, Number = {7143}, Own = {NLM}, Pages = {461--464}, Phst = {2006/10/23 {$[$}received{$]$}; 2007/04/11 {$[$}accepted{$]$}}, Pii = {nature05840}, Pl = {England}, Pmid = {17522680}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't}, Pubm = {Print}, Rn = {0 (Colloids); 0 (Lipid Bilayers); 0 (Lipids); 0 (Membrane Proteins)}, Sb = {IM}, So = {Nature. 2007 May 24;447(7143):461-4.}, Stat = {MEDLINE}, Title = {Aggregation and vesiculation of membrane proteins by curvature-mediated interactions}, Volume = {447}, Year = {2007}, Bdsk-Url-1 = {http://dx.doi.org/10.1038/nature05840}} @article{McMahon:2005fk, Abstract = {Membrane curvature is no longer seen as a passive consequence of cellular activity but an active means to create membrane domains and to organize centres for membrane trafficking. Curvature can be dynamically modulated by changes in lipid composition, the oligomerization of curvature scaffolding proteins and the reversible insertion of protein regions that act like wedges in membranes. There is an interplay between curvature-generating and curvature-sensing proteins during vesicle budding. This is seen during vesicle budding and in the formation of microenvironments. On a larger scale, membrane curvature is a prime player in growth, division and movement.}, Address = {MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK. hmm@mrc-lmb.cam.ca.uk}, Au = {McMahon, HT and Gallop, JL}, Author = {McMahon, H T and Gallop, J L}, Da = {20051201}, Date-Added = {2007-10-03 14:27:45 -0400}, Date-Modified = {2008-05-29 16:23:40 -0700}, Dcom = {20051228}, Edat = {2005/12/02 09:00}, Jid = {0410462}, Journal = {Nature}, Jt = {Nature}, Keywords = {Cell Membrane/*chemistry/*metabolism; Cytoskeleton/metabolism; Membrane Lipids/metabolism; Membrane Proteins/chemistry/metabolism; Microtubules/metabolism; Molecular Motor Proteins/metabolism}, Language = {eng}, Local-Url = {file://localhost/Users/wiggins/research/Papers/McMahon2005_membrane_review.pdf}, Lr = {20061115}, Mhda = {2005/12/29 09:00}, Number = {7068}, Own = {NLM}, Pages = {590--596}, Pii = {nature04396}, Pl = {England}, Pmid = {16319878}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't; Review}, Pubm = {Print}, Rf = {91}, Rn = {0 (Membrane Lipids); 0 (Membrane Proteins); 0 (Molecular Motor Proteins)}, Sb = {IM}, So = {Nature. 2005 Dec 1;438(7068):590-6.}, Stat = {MEDLINE}, Title = {Membrane curvature and mechanisms of dynamic cell membrane remodelling}, Volume = {438}, Year = {2005}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://dx.doi.org/10.1038/nature04396}} @article{Frey:2000lr, Abstract = {Electron microscopic (EM) tomography is providing important new insights into the internal organization of mitochondria. The standard baffle model for cristae structure, called into question years ago, has now clearly been shown to be inaccurate. Depending on source and conformational state, cristae can vary from simple tubular structures to more complex lamellar structures merging with the inner boundary membrane through tubular structures 28 nm in diameter. The structural information provided by EM tomography has important implications for mitochondrial bioenergetics, biogenesis and the role of mitochondria in apoptosis. The structural paradigm defined by EM tomography is helping in the design of new experimental approaches to mitochondrial function.}, Address = {Department of Biology, San Diego State University, San Diego, CA 92182-4614, USA. tfrey@sunstroke.sdsu.edu}, Au = {Frey, TG and Mannella, CA}, Author = {Frey, T G and Mannella, C A}, Da = {20000915}, Date-Added = {2007-08-17 12:52:04 -0700}, Date-Modified = {2008-05-29 16:32:43 -0700}, Dcom = {20000915}, Edat = {2000/06/29 11:00}, Gr = {RR04050/RR/NCRR}, Jid = {7610674}, Journal = {Trends Biochem Sci}, Jt = {Trends in biochemical sciences}, Keywords = {Animals; Apoptosis; Computer Simulation; Diffusion; Humans; Intracellular Membranes/metabolism/*ultrastructure; Microscopy, Electron/methods; Mitochondria/metabolism/pathology/*ultrastructure; Oxidative Phosphorylation; Tomography/methods/trends}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Frey/2000.pdf}, Lr = {20061115}, Mhda = {2000/09/23 11:01}, Number = {7}, Own = {NLM}, Pages = {319--324}, Pii = {S0968-0004(00)01609-1}, Pl = {ENGLAND}, Pmid = {10871882}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.; Review}, Pubm = {Print}, Rf = {37}, Sb = {IM}, So = {Trends Biochem Sci. 2000 Jul;25(7):319-24.}, Stat = {MEDLINE}, Title = {The internal structure of mitochondria}, Volume = {25}, Year = {2000}, Bdsk-File-1 = {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}} @article{claessens:011903, Author = {M. M. A. E. Claessens and B. F. van Oort and F. A. M. Leermakers and F. A. Hoekstra and M. A. Cohen Stuart}, Date-Added = {2007-08-03 17:07:45 -0700}, Date-Modified = {2007-08-03 17:07:49 -0700}, Doi = {10.1103/PhysRevE.76.011903}, Eid = {011903}, Journal = {Physical Review E (Statistical, Nonlinear, and Soft Matter Physics)}, Keywords = {lipid bilayers; bending; biomembranes; entropy; SCF calculations; molecular biophysics; biomechanics}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Claessens/2007.pdf}, Number = {1}, Numpages = {6}, Pages = {011903}, Publisher = {APS}, Title = {Bending rigidity of mixed phospholipid bilayers and the equilibrium radius of corresponding vesicles}, Url = {http://link.aps.org/abstract/PRE/v76/e011903}, Volume = {76}, Year = {2007}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://link.aps.org/abstract/PRE/v76/e011903}, Bdsk-Url-2 = {http://dx.doi.org/10.1103/PhysRevE.76.011903}} @article{burrell:160, Author = {Keith H. Burrell}, Date-Added = {2007-07-20 09:30:33 -0700}, Date-Modified = {2007-11-12 15:27:50 -0500}, Doi = {10.1119/1.16228}, Journal = {American Journal of Physics}, Keywords = {LEAST SQUARE FIT; ERRORS; NONLINEAR PROBLEMS; DATA ANALYSIS; SERIES EXPANSION}, Local-Url = {file://localhost/Users/wiggins/Downloads/pubmed_result.txt}, Number = {2}, Pages = {160-164}, Publisher = {AAPT}, Title = {Error analysis for parameters determined in nonlinear least-squares fits}, Url = {http://link.aip.org/link/?AJP/58/160/1}, Volume = {58}, Year = {1990}, Bdsk-Url-1 = {http://link.aip.org/link/?AJP/58/160/1}, Bdsk-Url-2 = {http://dx.doi.org/10.1119/1.16228}} @article{Saffman:1975vn, Abstract = {Brownian motion (diffusion) of particles in membranes occurs in a highly anisotropic environment. For such particles a translational mobility (independent of velocity) can be defined if the viscosity of the liquid embedding the membrane is taken into account. The results of a model calculation are presented. They suggest that for a realistic situation translational diffusion should be about four times faster in relation to rotational diffusion than in the isotropic case.}, Au = {Saffman, PG and Delbruck, M}, Author = {Saffman, P G and Delbruck, M}, Da = {19760116}, Date-Added = {2007-07-13 14:30:25 -0700}, Date-Modified = {2007-07-13 14:30:34 -0700}, Dcom = {19760116}, Edat = {1975/08/01}, Issn = {0027-8424 (Print)}, Jid = {7505876}, Journal = {Proc Natl Acad Sci U S A}, Jt = {Proceedings of the National Academy of Sciences of the United States of America}, Keywords = {Animals; Anura; Biological Transport; Cell Membrane/metabolism; *Diffusion; Mathematics; Membranes/*metabolism; Models, Biological; Photoreceptors/metabolism; Protein Conformation; Rhodopsin/metabolism; Viscosity}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Saffman/1975.pdf}, Lr = {20031114}, Mhda = {1975/08/01 00:01}, Number = {8}, Own = {NLM}, Pages = {3111--3113}, Pl = {UNITED STATES}, Pmid = {1059096}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print}, Rn = {9009-81-8 (Rhodopsin)}, Sb = {IM}, So = {Proc Natl Acad Sci U S A. 1975 Aug;72(8):3111-3.}, Stat = {MEDLINE}, Title = {Brownian motion in biological membranes}, Volume = {72}, Year = {1975}, Bdsk-File-1 = {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}} @article{pandey:061913, Author = {R. B. Pandey and Kelly L. Anderson and B. L. Farmer}, Date-Added = {2007-07-13 14:29:10 -0700}, Date-Modified = {2007-07-13 14:29:19 -0700}, Doi = {10.1103/PhysRevE.75.061913}, Eid = {061913}, Journal = {Physical Review E (Statistical, Nonlinear, and Soft Matter Physics)}, Keywords = {biomembrane transport; biodiffusion; Monte Carlo methods; stochastic processes; nonlinear dynamical systems}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Pandey/2007.pdf}, Number = {6}, Numpages = {5}, Pages = {061913}, Publisher = {APS}, Title = {Multiscale mode dynamics of a tethered membrane}, Url = {http://link.aps.org/abstract/PRE/v75/e061913}, Volume = {75}, Year = {2007}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://link.aps.org/abstract/PRE/v75/e061913}, Bdsk-Url-2 = {http://dx.doi.org/10.1103/PhysRevE.75.061913}} @article{Almeida:2007fj, Abstract = {The application of fluorescence lifetime imaging microscopy to study gel/fluid and raftlike lipid domains in giant unilamellar vesicles (GUVs) is demonstrated here. Different regions of the ternary dipalmitoylphosphatidylcholine/dioleoylphosphatidylcholine/cholesterol phase diagram were studied. The head-labeled phospholipid Rhodamine-dioleoylphosphatidylethanolamine (Rhod-DOPE) was used as a fluorescent probe. Gel/fluid and liquid-ordered (l(o))/liquid-disordered (l(d)) phase separation were clearly visualized upon two-photon excitation. Fluorescence intensity decays in different regions of a GUV were also obtained with the microscope in fixed laser-beam configuration. The ensemble behavior of the system was studied by obtaining fluorescence intensity decays of Rhod-DOPE in nongiant vesicle suspensions. The fingerprints for gel/fluid coexistence and for the presence of l(o) raftlike phase, based on fluorescence lifetime imaging microscopy histograms and images, and on the fluorescence intensity decay parameters of Rhod-DOPE, are presented. The presence of three lipid phases in one single GUV is detected unequivocally. From the comparison of lifetime parameters, it can be concluded that the l(o) phase is formed in the binary dipalmitoylphosphatidylcholine/cholesterol but not in the dioleoylphosphatidylcholine/cholesterol mixture. The domains apparent in fluorescence intensity images have a more complex substructure revealed by analysis of the lifetime data. The potential applications of this combined imaging/microscopic/macroscopic methodology are discussed.}, Address = {MicroSpectroscopy Centre, Laboratory of Biochemistry, Wageningen University, Wageningen, The Netherlands.}, Au = {de Almeida, RF and Borst, J and Fedorov, A and Prieto, M and Visser, AJ}, Author = {de Almeida, Rodrigo F M and Borst, Janwillem and Fedorov, Alexander and Prieto, Manuel and Visser, Antonie J W G}, Da = {20070625}, Date-Added = {2007-07-13 14:21:45 -0700}, Date-Modified = {2007-07-13 14:21:57 -0700}, Dep = {20070420}, Doi = {10.1529/biophysj.106.098822}, Edat = {2007/04/24 09:00}, Issn = {0006-3495 (Print)}, Jid = {0370626}, Journal = {Biophys J}, Jt = {Biophysical journal}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Almeida/2007.pdf}, Mhda = {2007/04/24 09:00}, Number = {2}, Own = {NLM}, Pages = {539--553}, Phst = {2007/04/20 {$[$}aheadofprint{$]$}}, Pii = {biophysj.106.098822}, Pl = {United States}, Pmid = {17449668}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print-Electronic}, Sb = {IM}, So = {Biophys J. 2007 Jul 15;93(2):539-53. Epub 2007 Apr 20.}, Stat = {In-Data-Review}, Title = {Complexity of lipid domains and rafts in giant unilamellar vesicles revealed by combining imaging and microscopic and macroscopic time-resolved fluorescence}, Volume = {93}, Year = {2007}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://dx.doi.org/10.1529/biophysj.106.098822}} @article{Wessels:2007uq, Abstract = {Many enveloped viruses employ low-pH-triggered membrane fusion during cell penetration. Solution-based in vitro assays in which viruses fuse with liposomes have provided much of our current biochemical understanding of low-pH-triggered viral membrane fusion. Here, we extend this in vitro approach by introducing a fluorescence assay using single particle tracking to observe lipid mixing between individual virus particles (influenza or Sindbis) and supported lipid bilayers. Our single-particle experiments reproduce many of the observations of the solution assays. The single-particle approach naturally separates the processes of membrane binding and membrane fusion and therefore allows measurement of details that are not available in the bulk assays. We find that the dynamics of lipid mixing during individual Sindbis fusion events is faster than 30 ms. Although neither virus binds membranes at neutral pH, under acidic conditions, the delay between membrane binding and lipid mixing is less than half a second for nearly all virus-membrane combinations. The delay between binding and lipid mixing lengthened only for Sindbis virus at the lowest pH in a cholesterol-dependent manner, highlighting the complex interaction between lipids, virus proteins, and buffer conditions in membrane fusion.}, Address = {Department of Physics, North Carolina State University, Raleigh, North Carolina.}, Au = {Wessels, L and Elting, MW and Scimeca, D and Weninger, K}, Author = {Wessels, Laura and Elting, Mary Williard and Scimeca, Dominic and Weninger, Keith}, Da = {20070625}, Date-Added = {2007-07-13 14:21:09 -0700}, Date-Modified = {2007-07-13 14:21:29 -0700}, Dep = {20070420}, Doi = {10.1529/biophysj.106.097485}, Edat = {2007/04/24 09:00}, Issn = {0006-3495 (Print)}, Jid = {0370626}, Journal = {Biophys J}, Jt = {Biophysical journal}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Wessels/2007.pdf}, Mhda = {2007/04/24 09:00}, Number = {2}, Own = {NLM}, Pages = {526--538}, Phst = {2007/04/20 {$[$}aheadofprint{$]$}}, Pii = {biophysj.106.097485}, Pl = {United States}, Pmid = {17449662}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print-Electronic}, Sb = {IM}, So = {Biophys J. 2007 Jul 15;93(2):526-38. Epub 2007 Apr 20.}, Stat = {In-Data-Review}, Title = {Rapid membrane fusion of individual virus particles with supported lipid bilayers}, Volume = {93}, Year = {2007}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://dx.doi.org/10.1529/biophysj.106.097485}} @article{Otter:2007qy, Abstract = {The flow behavior of lipid bilayer membranes is characterized by a surface viscosity for in-plane shear deformations, and an intermonolayer friction coefficient for slip between the two leaflets of the bilayer. Both properties have been studied for a variety of coarse-grained double-tailed model lipids, using equilibrium and nonequilibrium molecular dynamics simulations. For lipids with two identical tails, the surface shear viscosity rises rapidly with tail length, while the intermonolayer friction coefficient is less sensitive to the tail length. Interdigitation of lipid tails across the bilayer midsurface, as observed for lipids with two distinct tails, strongly enhances the intermonolayer friction coefficient, but hardly affects the surface shear viscosity. The simulation results are compared against the available experimental data.}, Address = {Computational Biophysics, Faculty of Science and Technology, University of Twente, Enschede, The Netherlands.}, Au = {den Otter, WK and Shkulipa, SA}, Author = {den Otter, W K and Shkulipa, S A}, Da = {20070625}, Date-Added = {2007-07-13 14:20:46 -0700}, Date-Modified = {2007-07-13 14:20:55 -0700}, Dep = {20070427}, Doi = {10.1529/biophysj.107.105395}, Edat = {2007/05/01 09:00}, Issn = {0006-3495 (Print)}, Jid = {0370626}, Journal = {Biophys J}, Jt = {Biophysical journal}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Otter/2007.pdf}, Mhda = {2007/05/01 09:00}, Number = {2}, Own = {NLM}, Pages = {423--433}, Phst = {2007/04/27 {$[$}aheadofprint{$]$}}, Pii = {biophysj.107.105395}, Pl = {United States}, Pmid = {17468168}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print-Electronic}, Sb = {IM}, So = {Biophys J. 2007 Jul 15;93(2):423-33. Epub 2007 Apr 27.}, Stat = {In-Data-Review}, Title = {Intermonolayer friction and surface shear viscosity of lipid bilayer membranes}, Volume = {93}, Year = {2007}, Bdsk-File-1 = {YnBsaXN0MDDUAQIDBAUGCQpYJHZlcnNpb25UJHRvcFkkYXJjaGl2ZXJYJG9iamVjdHMSAAGGoNEHCFRyb290gAFfEA9OU0tleWVkQXJjaGl2ZXKoCwwXGBkdJCVVJG51bGzTDQ4PEBEUViRjbGFzc1dOUy5rZXlzWk5TLm9iamVjdHOAB6ISE4ACgAOiFRaABIAGWWFsaWFzRGF0YVxyZWxhdGl2ZVBhdGjSDRobHFdOUy5kYXRhgAVPEQGKAAAAAAGKAAIAAANoc3IAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAADBcRzJSCsAAABGbNEIMjAwNy5wZGYAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAACHWdMKzy8JQREYgcHJ2dwAEAAMAAAkgAAAAAAAAAAAAAAAAAAAABU90dGVyAAAQAAgAAMFxjUkAAAARAAgAAMK0LjIAAAABABgARmzRAEZrzwBGatUARmobAEZkaABAiUMAAgBAaHNyOlVzZXJzOmF0b21pY3BpcmF0ZTpEb2N1bWVudHM6Q2FsdGVjaDpBcnRpY2xlczpPdHRlcjoyMDA3LnBkZgAOABIACAAyADAAMAA3AC4AcABkAGYADwAIAAMAaABzAHIAEgA8VXNlcnMvYXRvbWljcGlyYXRlL0RvY3VtZW50cy9DYWx0ZWNoL0FydGljbGVzL090dGVyLzIwMDcucGRmABMAAS8AABUAAgAT//8AANIeHyAhWCRjbGFzc2VzWiRjbGFzc25hbWWjISIjXU5TTXV0YWJsZURhdGFWTlNEYXRhWE5TT2JqZWN0XxAjLi4vLi4vLi4vLi4vQXJ0aWNsZXMvT3R0ZXIvMjAwNy5wZGbSHh8mJ6InI1xOU0RpY3Rpb25hcnkACAARABoAHwApADIANwA6AD8AQQBTAFwAYgBpAHAAeACDAIUAiACKAIwAjwCRAJMAnQCqAK8AtwC5AkcCTAJVAmACZAJyAnkCggKoAq0CsAAAAAAAAAIBAAAAAAAAACgAAAAAAAAAAAAAAAAAAAK9}, Bdsk-Url-1 = {http://dx.doi.org/10.1529/biophysj.107.105395}} @article{Zhu:2007fk, Abstract = {To investigate the nanomechanics of the erythrocyte membrane we developed a hybrid model that couples the actin-spectrin network to the lipid bilayer. This model features a Fourier space Brownian dynamics model of the bilayer, a Brownian dynamics model of the actin protofilament, and a modified wormlike-chain model of the spectrin (including a cable-dynamics model to predict the oscillation in tension). This model enables us to predict the nanomechanics of single or multiple units of the protein network, the lipid bilayer, and the effect of their interactions. The present work is focused on the attitude of the actin protofilament at the equilibrium states coupled with the elevations of the lipid bilayer through their primary linkage at the suspension complex in deformations. Two different actin-spectrin junctions are considered at the junctional complex. With a point-attachment junction, large pitch angles and bifurcation of yaw angles are predicted. Thermal fluctuations at bifurcation may lead to mode-switching, which may affect the network and the physiological performance of the membrane. In contrast, with a wrap-around junction, pitch angles remain small, and the occurrence of bifurcation is greatly reduced. These simulations suggest the importance of three-dimensional molecular junctions and the lipid bilayer/protein network coupling on cell membrane mechanics.}, Address = {Department of Structural Engineering and Department of Bioengineering, University of California, San Diego, La Jolla, California.}, Au = {Zhu, Q and Vera, C and Asaro, RJ and Sche, P and Sung, LA}, Author = {Zhu, Qiang and Vera, Carlos and Asaro, Robert J and Sche, Paul and Sung, L Amy}, Da = {20070625}, Date-Added = {2007-07-13 14:20:09 -0700}, Date-Modified = {2007-07-13 14:20:27 -0700}, Dep = {20070420}, Doi = {10.1529/biophysj.106.094383}, Edat = {2007/04/24 09:00}, Issn = {0006-3495 (Print)}, Jid = {0370626}, Journal = {Biophys J}, Jt = {Biophysical journal}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Zhu/2007.pdf}, Mhda = {2007/04/24 09:00}, Number = {2}, Own = {NLM}, Pages = {386--400}, Phst = {2007/04/20 {$[$}aheadofprint{$]$}}, Pii = {biophysj.106.094383}, Pl = {United States}, Pmid = {17449663}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print-Electronic}, Sb = {IM}, So = {Biophys J. 2007 Jul 15;93(2):386-400. Epub 2007 Apr 20.}, Stat = {In-Data-Review}, Title = {A hybrid model for erythrocyte membrane: a single unit of protein network coupled with lipid bilayer}, Volume = {93}, Year = {2007}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://dx.doi.org/10.1529/biophysj.106.094383}} @article{Heinrich:2007lr, Abstract = {The axial deformation of a pipette-pressurized fluid membrane bag produces minuscule yet well-defined, reproducible forces. The stiffness of this ultrasensitive force transducer is tunable and largely independent of the constitutive membrane behavior. Based on a rigorous variational treatment, we present both numerical as well as approximate analytical solutions for the force-deflection relation of this unique biophysical force probe. Our numerical results predict a measurably nonlinear force-deflection behavior at moderate-to-large deformations, which we confirm experimentally using red blood cells. Furthermore, considering nearly spherical membrane shapes and enforcing proper boundary conditions, we derive an analytical solution valid at small deformations. In this linear regime the pressurized membrane bag behaves like a Hookean spring, with a spring constant that is significantly larger than previously published for the biomembrane force probe.}, Address = {Department of Biomedical Engineering and Biomedical Engineering Graduate Group, University of California, Davis, California.}, Au = {Heinrich, V and Ounkomol, C}, Author = {Heinrich, Volkmar and Ounkomol, Chawin}, Da = {20070625}, Date-Added = {2007-07-13 14:19:36 -0700}, Date-Modified = {2007-07-13 14:19:47 -0700}, Dep = {20070427}, Doi = {10.1529/biophysj.107.104091}, Edat = {2007/05/01 09:00}, Issn = {0006-3495 (Print)}, Jid = {0370626}, Journal = {Biophys J}, Jt = {Biophysical journal}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Heinrich/2007.pdf}, Mhda = {2007/05/01 09:00}, Number = {2}, Own = {NLM}, Pages = {363--372}, Phst = {2007/04/27 {$[$}aheadofprint{$]$}}, Pii = {biophysj.107.104091}, Pl = {United States}, Pmid = {17468170}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print-Electronic}, Sb = {IM}, So = {Biophys J. 2007 Jul 15;93(2):363-72. Epub 2007 Apr 27.}, Stat = {In-Data-Review}, Title = {Force versus Axial Deflection of Pipette-Aspirated Closed Membranes}, Volume = {93}, Year = {2007}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://dx.doi.org/10.1529/biophysj.107.104091}} @article{Bozic:1992lr, Abstract = {A theoretical analysis is presented of the formation of membrane tethers from micropipette-aspirated phospholipid vesicles. In particular, it is taken into account that the phospholipid membrane is composed of two layers which are in contact but unconnected. The elastic energy of the bilayer is taken to be the sum of contributions from area expansivity, relative expansivity of the two monolayers, and bending. The vesicle is aspirated into a pipette and a constant point force is applied at the opposite side in the direction away from the pipette. The shape of the vesicle in approximated as a cylindrical projection into the pipette with a hemispherical cap, a spherical section, and a cylindrical tether with a hemispherical cap. The dimensions of the different regions of the vesicle are obtained by minimizing its elastic energy subject to the condition that the volume of the vesicle is fixed. The range of values for the parameters of the system is determined at which the existence of a tether is possible. Stability analysis is performed showing which of these configurations are stable. The importance of the relative expansion and compression of the constituent monolayers is established by recognizing that local bending energy by itself does not stabilize the vesicle geometry, and that in the limit as the relative expansivity modulus becomes infinitely large, a tether cannot be formed. Predictions are made for the functional relationships among experimentally observable quantities. In a companion report, the results of this analysis are applied to experimental measurements of tether formation, and used to calculate values for the membrane material coefficients.}, Address = {Institute of Biophysics, Medical Faculty, University of Ljubljana, Slovenia.}, Au = {Bozic, B and Svetina, S and Zeks, B and Waugh, RE}, Author = {Bozic, B and Svetina, S and Zeks, B and Waugh, R E}, Da = {19920618}, Date-Added = {2007-07-13 08:03:53 -0700}, Date-Modified = {2007-07-13 08:04:01 -0700}, Dcom = {19920618}, Edat = {1992/04/01}, Issn = {0006-3495 (Print)}, Jid = {0370626}, Journal = {Biophys J}, Jt = {Biophysical journal}, Keywords = {Biophysics; Elasticity; Lipid Bilayers/*chemistry; Membranes, Artificial; Models, Theoretical; Phospholipids/chemistry; Thermodynamics}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Bozic/1992.pdf}, Lr = {20061115}, Mhda = {1992/04/01 00:01}, Number = {4}, Own = {NLM}, Pages = {963--973}, Pl = {UNITED STATES}, Pmid = {1581505}, Pst = {ppublish}, Pt = {Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.}, Pubm = {Print}, Rn = {0 (Lipid Bilayers); 0 (Membranes, Artificial); 0 (Phospholipids)}, Sb = {IM}, So = {Biophys J. 1992 Apr;61(4):963-73.}, Stat = {MEDLINE}, Title = {Role of lamellar membrane structure in tether formation from bilayer vesicles}, Volume = {61}, Year = {1992}, Bdsk-File-1 = {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}} @article{Heinrich:1996lr, Abstract = {The bending stiffness of a phospholipid bilayer (Kc) was measured by forming thin bilayer cylinders (tethers) from giant phospholipid vesicles. Based on the balance of forces, the tether force was expected to be proportional to the square root of the membrane tension, with a constant of proportionality containing Kc. The membrane tension was controlled via the aspiration pressure in a micropipette used to hold the vesicle. The force on the tether was generated by an electromagnet acting on a paramagnetic bead attached to the vesicle surface. The magnitude of the force was determined from measurements of the magnet current, which was adjusted to maintain the position of the bead. Measurements were performed on vesicles composed of stearoyl-oleoyl-phosphatidylcholine plus 5% (by mole) biotinylated phosphatidylethanolamine to mediate adhesion to streptavidin-coated beads. From each vesicle, tethers were formed repeatedly at different values of the membrane tension. The expected relationship between membrane tension and tether force was observed. The mean value of Kc for 10 different vesicles was 1.17 x 10(-19) J (SD = 0.08 x 10(-19) J). The precision of these data demonstrates the reliability of this approach, which avoids uncertainties of interpretation and measurement that may be associated with other methods for determining Kc.}, Address = {Department of Biophysics, University of Rochester School of Medicine and Dentistry, NY 14642, USA.}, Au = {Heinrich, V and Waugh, RE}, Author = {Heinrich, V and Waugh, R E}, Da = {19970116}, Date-Added = {2007-02-20 15:30:49 -0800}, Date-Modified = {2007-02-20 15:31:00 -0800}, Dcom = {19970116}, Edat = {1996/09/01}, Gr = {HL 18208/HL/NHLBI; HL 31524/HL/NHLBI}, Issn = {0090-6964 (Print)}, Jid = {0361512}, Journal = {Ann Biomed Eng}, Jt = {Annals of biomedical engineering}, Keywords = {Calibration; Cell Membrane/*physiology; Computer Graphics; Elasticity; Electromagnetic Fields; Image Processing, Computer-Assisted; Membranes, Artificial; Micromanipulation; Microscopy, Video; *Models, Biological; Phospholipids/*physiology; *Transducers}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Heinrich/1996.pdf}, Lr = {20061115}, Mhda = {1996/09/01 00:01}, Number = {5}, Own = {NLM}, Pages = {595--605}, Pl = {UNITED STATES}, Pmid = {8886240}, Pst = {ppublish}, Pt = {Journal Article; Research Support, U.S. Gov't, P.H.S.}, Pubm = {Print}, Rn = {0 (Membranes, Artificial); 0 (Phospholipids)}, Sb = {IM}, So = {Ann Biomed Eng. 1996 Sep-Oct;24(5):595-605.}, Stat = {MEDLINE}, Title = {A piconewton force transducer and its application to measurement of the bending stiffness of phospholipid membranes}, Volume = {24}, Year = {1996}, Bdsk-File-1 = {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}} @article{Kraft:2006uq, Abstract = {Lateral variations in membrane composition are postulated to play a central role in many cellular events, but it has been difficult to probe membrane composition and organization on length scales of tens to hundreds of nanometers. We present a high-resolution imaging secondary ion mass spectrometry technique to reveal the lipid distribution within a phase-separated membrane with a lateral resolution of [~]100 nanometers. Quantitative information about the chemical composition within small lipid domains was obtained with the use of isotopic labels to identify each molecular species. Composition variations were detected within some domains. }, Author = {Kraft, Mary L. and Weber, Peter K. and Longo, Marjorie L. and Hutcheon, Ian D. and Boxer, Steven G.}, Date-Added = {2006-09-29 10:35:59 -0700}, Date-Modified = {2006-09-29 10:35:59 -0700}, Doi = {10.1126/science.1130279}, Eprint = {http://www.sciencemag.org/cgi/reprint/313/5795/1948.pdf}, Journal = {Science}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Kraft/2006.pdf}, Number = {5795}, Pages = {1948-1951}, Title = {Phase Separation of Lipid Membranes Analyzed with High-Resolution Secondary Ion Mass Spectrometry}, Url = {http://www.sciencemag.org/cgi/content/abstract/313/5795/1948}, Volume = {313}, Year = {2006}, Bdsk-File-1 = {YnBsaXN0MDDUAQIDBAUGCQpYJHZlcnNpb25UJHRvcFkkYXJjaGl2ZXJYJG9iamVjdHMSAAGGoNEHCFRyb290gAFfEA9OU0tleWVkQXJjaGl2ZXKoCwwXGBkdJCVVJG51bGzTDQ4PEBEUViRjbGFzc1dOUy5rZXlzWk5TLm9iamVjdHOAB6ISE4ACgAOiFRaABIAGWWFsaWFzRGF0YVxyZWxhdGl2ZVBhdGjSDRobHFdOUy5kYXRhgAVPEQGKAAAAAAGKAAIAAANoc3IAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAADBcRzJSCsAAABGbI0IMjAwNi5wZGYAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAnKBMFCljIAAAAAAAAAAAAEAAMAAAkgAAAAAAAAAAAAAAAAAAAABUtyYWZ0AAAQAAgAAMFxjUkAAAARAAgAAMFC+KIAAAABABgARmyNAEZrzwBGatUARmobAEZkaABAiUMAAgBAaHNyOlVzZXJzOmF0b21pY3BpcmF0ZTpEb2N1bWVudHM6Q2FsdGVjaDpBcnRpY2xlczpLcmFmdDoyMDA2LnBkZgAOABIACAAyADAAMAA2AC4AcABkAGYADwAIAAMAaABzAHIAEgA8VXNlcnMvYXRvbWljcGlyYXRlL0RvY3VtZW50cy9DYWx0ZWNoL0FydGljbGVzL0tyYWZ0LzIwMDYucGRmABMAAS8AABUAAgAT//8AANIeHyAhWCRjbGFzc2VzWiRjbGFzc25hbWWjISIjXU5TTXV0YWJsZURhdGFWTlNEYXRhWE5TT2JqZWN0XxAjLi4vLi4vLi4vLi4vQXJ0aWNsZXMvS3JhZnQvMjAwNi5wZGbSHh8mJ6InI1xOU0RpY3Rpb25hcnkACAARABoAHwApADIANwA6AD8AQQBTAFwAYgBpAHAAeACDAIUAiACKAIwAjwCRAJMAnQCqAK8AtwC5AkcCTAJVAmACZAJyAnkCggKoAq0CsAAAAAAAAAIBAAAAAAAAACgAAAAAAAAAAAAAAAAAAAK9}, Bdsk-Url-1 = {http://www.sciencemag.org/cgi/content/abstract/313/5795/1948}, Bdsk-Url-2 = {http://dx.doi.org/10.1126/science.1130279}} @article{Shibata:2006lr, Author = {Shibata, Yoko and Voeltz, Gia K. and Rapoport, Tom A.}, Date-Added = {2006-08-15 10:15:59 -0700}, Date-Modified = {2006-08-15 10:16:18 -0700}, Journal = {Cell}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Shibata/2006.pdf}, Number = {3}, Pages = {435--439}, Title = {Rough Sheets and Smooth Tubules}, Ty = {JOUR}, Url = {http://www.sciencedirect.com/science/article/B6WSN-4KM3YMP-3/2/030a1a576a9304815c5b5a1b9cd113cd}, Volume = {126}, Year = {2006}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://www.sciencedirect.com/science/article/B6WSN-4KM3YMP-3/2/030a1a576a9304815c5b5a1b9cd113cd}} @article{Liu:2006kx, Abstract = {Endocytosis in budding yeast is thought to occur in several phases. First, the membrane invaginates and then elongates into a tube. A vesicle forms at the end of the tube, eventually pinching off to form a "free" vesicle. Experiments show that actin polymerization is an active participant in the endocytic process, along with a number of membrane-associated proteins. Here we investigate the possible roles of these components in driving vesiculation by constructing a quantitative model of the process beginning at the stage where the membrane invagination has elongated into a tube encased in a sheath of membrane-associated protein. This protein sheath brings about the scission step where the vesicle separates from the tube. When the protein sheath is dynamin, it is commonly assumed that scission is brought about by the constriction of the sheath. Here, we show that an alternative scenario can work as well: The protein sheath acts as a "filter" to effect a phase separation of lipid species. The resulting line tension tends to minimize the interface between the tube region and the vesicle region. Interestingly, large vesicle size can further facilitate the reduction of the interfacial diameter down to a few nanometers, small enough so that thermal fluctuations can fuse the membrane and pinch off the vesicle. To deform the membrane into the tubular vesicle shape, the membrane elastic resistance forces must be balanced by some additional forces that we show can be generated by actin polymerization and/or myosin I. These active forces are shown to be important in successful scission processes as well.}, Affiliation = {Departments of *Chemistry and Molecular and Cellular Biology, University of California, Berkeley, CA 94720.}, Aid = {10.1073/pnas.0601045103 {$[$}doi{$]$}}, Au = {Liu J and Kaksonen M and Drubin DG and Oster G}, Author = {Liu, Jian and Kaksonen, Marko and Drubin, David G and Oster, George}, Da = {20060706}, Date-Added = {2006-08-02 11:37:35 -0400}, Date-Modified = {2006-08-02 11:37:42 -0400}, Dep = {20060626}, Edat = {2006/06/28 09:00}, Issn = {0027-8424 (Print)}, Jid = {7505876}, Journal = {Proc Natl Acad Sci U S A}, Jt = {Proceedings of the National Academy of Sciences of the United States of America.}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Liu/2006.pdf}, Mhda = {2006/06/28 09:00}, Number = {27}, Own = {NLM}, Pages = {10277-82}, Phst = {2006/06/26 {$[$}aheadofprint{$]$}}, Pl = {United States}, Pmid = {16801551}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print-Electronic}, Sb = {IM}, So = {Proc Natl Acad Sci U S A. 2006 Jul 5;103(27):10277-82. Epub 2006 Jun 26.}, Stat = {In-Data-Review}, Title = {Endocytic vesicle scission by lipid phase boundary forces}, Volume = {103}, Year = {2006}, Bdsk-File-1 = {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}} @article{Borgese:2006fj, Author = {Borgese, Nica and Francolini, Maura and Snapp, Erik}, Date-Added = {2006-08-02 11:37:01 -0400}, Date-Modified = {2007-10-22 22:30:57 -0400}, Journal = {Current Opinion in Cell Biology}, Local-Url = {file://localhost/Users/wiggins/research/Papers/pubmed_result-6.txt}, Number = {4}, Pages = {358--364}, T2 = {Membranes and organelles}, Title = {Endoplasmic reticulum architecture: structures in flux}, Ty = {JOUR}, Url = {http://www.sciencedirect.com/science/article/B6VRW-4K8S5P6-1/2/24fb5038a262ca43e1562287748dc9e0}, Volume = {18}, Year = {2006}, Bdsk-Url-1 = {http://www.sciencedirect.com/science/article/B6VRW-4K8S5P6-1/2/24fb5038a262ca43e1562287748dc9e0}} @article{Antonny:2006qy, Author = {Antonny, Bruno}, Date-Added = {2006-08-02 11:34:03 -0400}, Date-Modified = {2006-08-02 11:34:18 -0400}, Journal = {Current Opinion in Cell Biology}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Antonny/2006.pdf}, Number = {4}, Pages = {386--394}, T2 = {Membranes and organelles}, Title = {Membrane deformation by protein coats}, Ty = {JOUR}, Url = {http://www.sciencedirect.com/science/article/B6VRW-4K7165P-1/2/0fb974107d7ed32e34b3c5fff32e5862}, Volume = {18}, Year = {2006}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://www.sciencedirect.com/science/article/B6VRW-4K7165P-1/2/0fb974107d7ed32e34b3c5fff32e5862}} @article{PhysRevLett.70.1335, Author = {Seifert, Udo}, Date-Added = {2006-08-02 10:10:46 -0400}, Date-Modified = {2006-08-02 10:11:03 -0400}, Doi = {10.1103/PhysRevLett.70.1335}, Journal = {Phys. Rev. Lett.}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Seifert/1993.pdf}, Month = {Mar}, Number = {9}, Numpages = {3}, Pages = {1335--1338}, Publisher = {American Physical Society}, Title = {Curvature-induced lateral phase segregation in two-component vesicles}, Volume = {70}, Year = {1993}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://dx.doi.org/10.1103/PhysRevLett.70.1335}} @article{Upadhyaya:2004fk, Abstract = {The endoplasmic reticulum (ER) and Golgi have robust bidirectional traffic between them and yet form distinct membrane compartments. Membrane tubules are pulled from large aggregates of ER or Golgi by microtubule motors to form ER tubulovesicular networks or Golgi tubules both in vivo and in vitro. The physical properties of membranes are critical for membrane traffic and organelle morphology. For example, tension applied to membranes can create tethers, drive membrane flow, and set the diameter of the tubules. Here, we formed ER and Golgi membrane networks in vitro and used optical tweezers to measure directly, for the first time, the membrane tensions of these organelles to clarify the possible role of tension in membrane flow. We report that higher forces are needed to form tethers from ER (18.6 +/- 2.8 pN) than from Golgi (11.4 +/- 1.4 pN) membrane tubules in vitro. Since ER tubules are smaller in diameter than Golgi tubules, it follows that Golgi networks have a lower tension than ER. The lower tension of the ER could be an explanation of how Golgi tubules can be rapidly drawn into the ER by tension-driven flow after fusion, as is observed in vivo.}, Affiliation = {Department of Physics, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.}, Au = {Upadhyaya A and Sheetz MP}, Author = {Upadhyaya, A and Sheetz, M P}, Da = {20040427}, Date-Added = {2006-05-18 15:25:26 -0700}, Date-Modified = {2008-05-29 16:55:38 -0700}, Dcom = {20041119}, Edat = {2004/04/28 05:00}, Jid = {0370626}, Journal = {Biophys J}, Jt = {Biophysical journal.}, Keywords = {Animals, Biophysics/methods, Cell Membrane/metabolism, Chick Embryo, Cytosol/metabolism, Endoplasmic Reticulum/*metabolism, Fibroblasts/metabolism, Golgi Apparatus/*metabolism, Intracellular Membranes/metabolism, Lipid Bilayers/chemistry, Microscopy, Phase-Contrast, Microscopy, Video, Models, Statistical}, Language = {eng}, Local-Url = {file://localhost/Users/wiggins/research/Papers/Upadhyaya2004.pdf}, Mhda = {2004/12/16 09:00}, Number = {5}, Own = {NLM}, Pages = {2923--2928}, Pl = {United States}, Pmid = {15111408}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print}, Rn = {0 (Lipid Bilayers)}, Sb = {IM}, So = {Biophys J. 2004 May;86(5):2923-8.}, Stat = {MEDLINE}, Title = {Tension in tubulovesicular networks of {Golgi} and endoplasmic reticulum membranes}, Volume = {86}, Year = {2004}, Bdsk-File-1 = {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}} @article{Julicher:1994uq, Author = {Julicher, F and Seifert, U}, Da = {19990210}, Date-Added = {2006-05-18 15:23:05 -0700}, Date-Modified = {2006-05-18 15:25:00 -0700}, Edat = {1994/05/01 00:00}, Issn = {1063-651X (Print)}, Journal = {PHYSICAL REVIEW. E. STATISTICAL PHYSICS, PLASMAS, FLUIDS, AND RELATED INTERDISCIPLINARY TOPICS}, Language = {ENG}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Julicher/1994.pdf}, Mhda = {1999/02/19 00:00}, Number = {5}, Own = {NLM}, Pages = {4728-4731}, Pmid = {9961774}, Pst = {ppublish}, Pt = {JOURNAL ARTICLE}, Pubm = {Print}, So = {PHYSICAL REVIEW. E. STATISTICAL PHYSICS, PLASMAS, FLUIDS, AND RELATED INTERDISCIPLINARY TOPICS. 1994 May;49(5):4728-4731.}, Stat = {Publisher}, Title = {Shape equations for axisymmetric vesicles: A clarification}, Volume = {49}, Year = {1994}, Bdsk-File-1 = {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}} @article{Jin:2006we, Abstract = {Using a new scheme based on atomic force microscopy (AFM), we investigate mechanical properties of clathrin-coated vesicles (CCVs). CCVs are multicomponent protein and lipid complexes of approximately 100 nm diameter that are implicated in many essential cell-trafficking processes. Our AFM imaging resolves clathrin lattice polygons and provides height deformation in quantitative response to AFM-substrate compression force. We model CCVs as multilayered elastic spherical shells and, from AFM measurements, estimate their bending rigidity to be 285 +/- 30 k(B)T, i.e., approximately 20 times that of either the outer clathrin cage or inner vesicle membrane. Further analysis reveals a flexible coupling between the clathrin coat and the membrane, a structural property whose modulation may affect vesicle biogenesis and cellular function.}, Affiliation = {Division of Bioengineering and Physical Science, Office of Research Services, Office of the Director, National Institutes of Health, Bethesda, Maryland.}, Aid = {10.1529/biophysj.105.068742 {$[$}doi{$]$}}, Au = {Jin AJ and Prasad K and Smith PD and Lafer EM and Nossal R}, Author = {Jin, Albert J and Prasad, Kondury and Smith, Paul D and Lafer, Eileen M and Nossal, Ralph}, Da = {20060410}, Date-Added = {2006-04-12 10:13:07 -0700}, Date-Modified = {2006-04-12 10:13:07 -0700}, Dep = {20060210}, Edat = {2006/02/14 09:00}, Ip = {9}, Jid = {0370626}, Journal = {Biophys J}, Jt = {Biophysical journal.}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Jin/2006.pdf}, Mhda = {2006/02/14 09:00}, Number = {0006-3495 (Print)}, Own = {NLM}, Pages = {3333-44}, Phst = {2006/02/10 {$[$}aheadofprint{$]$}}, Pl = {United States}, Pmid = {16473913}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print-Electronic}, Sb = {IM}, So = {Biophys J. 2006 May;90(9):3333-44. Epub 2006 Feb 10.}, Stat = {In-Data-Review}, Title = {Measuring the Elasticity of Clathrin-Coated Vesicles via Atomic Force Microscopy}, Volume = {90}, Year = {2006}, Bdsk-File-1 = {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}} @article{Lipowsky:1991eb, Abstract = {Membranes composed of amphiphilic molecules are highly flexible surfaces that determine the architecture of biological systems and provide a basic structural element for complex fluids such as microemulsions. Physical theories have been developed to describe many aspects of their conformational behaviour, such as the preferred shapes and shape transformations of closed vesicles, and the shape fluctuations, random-surface configurations, and adhesion and unbinding of interacting membranes. Understanding of these phenomena has been much improved through fruitful interactions between theory and experiment.}, Affiliation = {Institut fur Festkorperforschung, Forschungszentrum Julich, Germany.}, Aid = {10.1038/349475a0 {$[$}doi{$]$}}, Au = {Lipowsky R}, Author = {Lipowsky, R}, Da = {19910311}, Date-Added = {2006-04-07 12:37:33 -0400}, Date-Modified = {2006-04-07 12:37:56 -0400}, Dcom = {19910311}, Edat = {1991/02/07}, Ip = {6309}, Jid = {0410462}, Journal = {Nature}, Jt = {Nature.}, Keywords = {Animals, Cell Adhesion, Chemistry, Physical, Elasticity, Erythrocyte Membrane/chemistry/physiology/ultrastructure, Humans, Lipid Bilayers, Liposomes, Membrane Fluidity, Membrane Fusion, Membranes/chemistry/physiology/*ultrastructure, Polymers, Research Support, Non-U.S. Gov't}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Lipowsky/1991.pdf}, Lr = {20041117}, Mhda = {1991/02/07 00:01}, Number = {0028-0836 (Print)}, Own = {NLM}, Pages = {475-81}, Pl = {ENGLAND}, Pmid = {1992351}, Pst = {ppublish}, Pt = {Review}, Pubm = {Print}, Rf = {96}, Rn = {0 (Polymers)}, Sb = {IM}, So = {Nature. 1991 Feb 7;349(6309):475-81.}, Stat = {MEDLINE}, Title = {The conformation of membranes}, Volume = {349}, Year = {1991}, Bdsk-File-1 = {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}, Bdsk-File-2 = {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}, Bdsk-File-3 = {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}} @article{TG:2006bh, Abstract = {Electron microscope tomography produces three-dimensional reconstructions and has been used to image organelles both isolated and in situ, providing new insight into their structure and function. It is analogous to the various tomographies used in medical imaging. Compared with light microscopy, electron tomography offers an improvement in resolution of 30- to 80-fold and currently ranges from 3 to 8 nm, thus filling the gap between high-resolution structure determinations of isolated macromolecules and larger-scale studies on cells and tissues by light microscopy. Here, we provide an introduction to electron tomography and applications of the method in characterizing organelle architecture that also show its power for suggesting functional significance. Further improvements in labeling modalities, imaging tools, specimen preparation, and reconstruction algorithms promise to increase the quality and breadth of reconstructions by electron tomography and eventually to allow the mapping of the cellular proteomes onto detailed three-dimensional models of cellular structure. Expected online publication date for the Annual Review of Biophysics and Biomolecular Structure Volume 35 is May 5, 2006. Please see http://www.annualreviews.org/catalog/pub_dates.asp for revised estimates.}, Affiliation = {Department of Biology, San Diego State University, San Diego, CA 92182-4614 tfrey@sunstroke.sdsu.edu.}, Aid = {10.1146/annurev.biophys.35.040405.102039 {$[$}doi{$]$}}, Author = {Frey TG and Perkins GA and Ellisman MH}, Da = {20060117}, Date-Modified = {2006-03-22 15:59:26 -0800}, Dep = {20060113}, Edat = {2006/01/18 09:00}, Jid = {9211097}, Journal = {Annu Rev Biophys Biomol Struct}, Language = {ENG}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/TG/2006.pdf}, Mhda = {2006/01/18 09:00}, Number = {1056-8700 (Print)}, Own = {NLM}, Pmid = {16411839}, Pst = {aheadofprint}, Pt = {JOURNAL ARTICLE}, Pubm = {Print-Electronic}, Stat = {Publisher}, Title = {Electron Tomography of Membrane-Bound Cellular Organelles}, Year = {2006}, Bdsk-File-1 = {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}} @article{Raphael:1996vb, Abstract = {Biological membranes are lamellar structures composed of two leaflets capable of supporting different mechanical stresses. Stress differences between leaflets were generated during micromechanical experiments in which long thin tubes of lipid (tethers) were formed from the surfaces of giant phospholipid vesicles. A recent dynamic analysis of this experiment predicts the relaxation of local differences in leaflet stress by lateral slip between the leaflets. Differential stress may also relax by interleaflet transport of lipid molecules ("flip-flop"). In this report, we extend the former analysis to include interleaflet lipid transport. We show that transmembrane lipid flux will evidence itself as a linear increase in tether length with time after a step reduction in membrane tension. Multiple measurements were performed on 24 different vesicles composed of stearoyl-oleoyl-phosphatidylcholine plus 3% dinitrophenol-linked di-oleoyl-phosphatidylethanolamine. These tethers all exhibited a linear phase of growth with a mean value of the rate of interlayer permeation, cp = 0.009 s-1. This corresponds to a half-time of approximately 8 min for mechanically driven interleaflet transport. This value is found to be consistent with longer times obtained for chemically driven transport if the lipids cross the membrane via transient, localized defects in the bilayer.}, Affiliation = {Department of Biophysics, School of Medicine and Dentistry, University of Rochester, New York 14642, USA.}, Au = {Waugh RE}, Author = {Raphael, R M and Waugh, R E}, Da = {19970311}, Date-Modified = {2006-03-29 08:56:16 -0500}, Dcom = {19970311}, Edat = {1996/09/01}, Gr = {HL31524/HL/NHLBI}, Jid = {0370626}, Journal = {Biophys J}, Keywords = {Biological Transport and Biophysics and Lipid Bilayers/*chemistry and Models, Chemical and Phosphatidylcholines/*chemistry and Research Support, U.S. Gov't, P.H.S. and Stress, Mechanical and Thermodynamics}, Language = {eng}, Lr = {20041117}, Mhda = {1996/09/01 00:01}, Number = {3}, Own = {NLM}, Pages = {1374-88}, Pl = {UNITED STATES}, Pmid = {8874013}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print}, Rn = {0 (Phosphatidylcholines)}, Sb = {IM}, Stat = {MEDLINE}, Title = {Accelerated interleaflet transport of phosphatidylcholine molecules in membranes under deformation}, Volume = {71}, Year = {1996}} @article{Waugh:1992rj, Abstract = {Bilayer membranes exhibit an elastic resistance to changes in curvature. This resistance depends both on the intrinsic stiffness of the constituent monolayers and on the curvature-induced expansion or compression of the monolayers relative to each other. The monolayers are constrained by hydrophobic forces to remain in contact, but they are capable of independent lateral redistribution to minimize the relative expansion or compression of each leaflet. Therefore, the magnitude of the expansion and compression of the monolayers relative to each other depends on the integral of the curvature over the entire membrane capsule. The coefficient characterizing the membrane stiffness resulting from relative expansion is the nonlocal bending modulus kr. Both the intrinsic (local) bending modulus (kc) and the nonlocal bending modulus (kr) can be measured by the formation of thin cylindrical membrane strands (tethers) from giant phospholipid vesicles. Previously, we reported measurements of kc based on measurements of tether radius as a function of force (Song and Waugh, 1991, J. Biomech. Engr. 112:233). Further analysis has revealed that the contribution from the nonlocal bending stiffness can be detected by measuring the change in the aspiration pressure required to establish equilibrium with increasing tether length. Using this approach, we obtain a mean value for the nonlocal bending modulus kr of approximately 4.1 x 10(-19)J. The range of values is broad (1.1-10.1 x 10(-19)J) and could reflect contributions other than simple mechanical equilibrium. Inclusion of the nonlocal bending stiffness in the calculation of kc results in a value for that modulus of approximately 1.20 +/- 0.17 x 10(-19)J, in close agreement with values obtained by other methods.}, Affiliation = {Department of Biophysics, University of Rochester School of Medicine and Dentistry, New York 14642.}, Au = {Zeks B}, Author = {Waugh, R E and Song, J and Svetina, S and \v{Z}ek\v{s}, B}, Da = {19920618}, Date-Modified = {2008-05-30 02:56:07 -0700}, Dcom = {19920618}, Edat = {1992/04/01}, Gr = {HL-31524/HL/NHLBI}, Jid = {0370626}, Journal = {Biophys J}, Keywords = {Biophysics and Elasticity and Lipid Bilayers/*chemistry and Membrane Fluidity and Phosphatidylcholines/chemistry and Research Support, Non-U.S. Gov't and Research Support, U.S. Gov't, Non-P.H.S. and Research Support, U.S. Gov't, P.H.S. and Thermodynamics}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Waugh/1992.pdf}, Lr = {20041117}, Mhda = {1992/04/01 00:01}, Number = {4}, Own = {NLM}, Pages = {974--982}, Pl = {UNITED STATES}, Pmid = {1581506}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print}, Rn = {0 (Phosphatidylcholines)}, Sb = {IM}, Stat = {MEDLINE}, Title = {Local and nonlocal curvature elasticity in bilayer membranes by tether formation from lecithin vesicles}, Volume = {61}, Year = {1992}, Bdsk-File-1 = {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}} @article{Cherney:2004pn, Abstract = {Optical trapping of liposomes is a useful tool for manipulating these lipid vesicles for sampling, mechanical testing, spectroscopic observation, and chemical analysis. Through the use of confocal Raman microscopy, this study addresses the effects of optical forces on the structure of unilamellar, dipalmitoylphosphatidylcholine (DPPC) vesicles, both optically trapped in solution and adhered to a coverslip. The energy and forces involved in optical trapping of lipid vesicles were derived in terms of the dielectric contrast between the phospholipid membrane and the surrounding solution; reflection forces at the membrane/water interface were found to be negligible. At optical powers of 9 mW and greater, unilamellar liposomes trapped in bulk solution experience a gradient force sufficiently strong to bend the vesicle membrane, so that a second bilayer from the same vesicle is drawn into the optical trap, with an energy of approximately 6 x 10(-13) erg. For vesicles adhered to a coverslip, the confocal probe can be scanned through the attached vesicle. Optical forces are insufficient to detach the bilayer that is adhered to the glass; however, the upper DPPC bilayer can be manipulated by the optical trap and the shape of the vesicle distorted from a spherical geometry. The effect of calcium ion on the flexibility of membrane bilayers was also tested; with 5 mM calcium ion in solution, the lipid bilayer of a surface-attached liposome is sufficiently rigid so that it cannot be distorted at moderate laser powers.}, Affiliation = {Department of Chemistry, University of Utah, 315 South 1400 East, Salt Lake City, Utah 84112-0850, USA.}, Aid = {10.1021/ac0492620 {$[$}doi{$]$}}, Au = {Harris JM}, Author = {Cherney, Daniel P and Bridges, Travis E and Harris, Joel M}, Ci = {Copyright 2004 American Chemical Society}, Da = {20040917}, Date-Modified = {2005-08-25 09:24:02 -0700}, Edat = {2004/09/18 05:00}, Jid = {0370536}, Journal = {Anal Chem}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Cherney/2004a.pdf}, Mhda = {2004/09/18 05:00}, Number = {17}, Own = {NLM}, Pages = {4920-8}, Pl = {United States}, Pmid = {15373424}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print}, Sb = {IM}, Stat = {In-Process}, Title = {Optical trapping of unilamellar phospholipid vesicles: investigation of the effect of optical forces on the lipid membrane shape by confocal-Raman microscopy.}, Volume = {76}, Year = {2004}, Bdsk-File-1 = {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}} @article{frischknecht:041924, Author = {Amalie L. Frischknecht and Laura J. Douglas Frink}, Date-Modified = {2005-10-31 10:55:45 -0800}, Eid = {041924}, Journal = {Physical Review E (Statistical, Nonlinear, and Soft Matter Physics)}, Keywords = {lipid bilayers; density functional theory; molecular dynamics method; biomechanics; compressibility; biomembranes; liquid structure}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Frischknecht/2005.pdf}, Number = {4}, Numpages = {12}, Pages = {041924}, Publisher = {APS}, Title = {Comparison of density functional theory and simulation of fluid bilayers}, Url = {http://link.aps.org/abstract/PRE/v72/e041924}, Volume = {72}, Year = {2005}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://link.aps.org/abstract/PRE/v72/e041924}} @article{glassinger:041926, Author = {E. Glassinger and A. C. Lee and R. M. Raphael}, Date-Modified = {2005-10-31 10:56:00 -0800}, Eid = {041926}, Journal = {Physical Review E (Statistical, Nonlinear, and Soft Matter Physics)}, Keywords = {biomembranes; biothermics; bioelectric phenomena; piezoelectricity}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Glassinger/2005.pdf}, Number = {4}, Numpages = {9}, Pages = {041926}, Publisher = {APS}, Title = {Electromechanical effects on tether formation from lipid membranes: A theoretical analysis}, Url = {http://link.aps.org/abstract/PRE/v72/e041926}, Volume = {72}, Year = {2005}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://link.aps.org/abstract/PRE/v72/e041926}} @article{frink:041923, Author = {Laura J. Douglas Frink and Amalie L. Frischknecht}, Date-Modified = {2005-10-31 10:56:16 -0800}, Eid = {041923}, Journal = {Physical Review E (Statistical, Nonlinear, and Soft Matter Physics)}, Keywords = {density functional theory; lipid bilayers; molecular biophysics; phase diagrams; phase transformations; biomembranes; biochemistry; cellular biophysics}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Frink/2005.pdf}, Number = {4}, Numpages = {13}, Pages = {041923}, Publisher = {APS}, Title = {Density functional theory approach for coarse-grained lipid bilayers}, Url = {http://link.aps.org/abstract/PRE/v72/e041923}, Volume = {72}, Year = {2005}, Bdsk-File-1 = {YnBsaXN0MDDUAQIDBAUGCQpYJHZlcnNpb25UJHRvcFkkYXJjaGl2ZXJYJG9iamVjdHMSAAGGoNEHCFRyb290gAFfEA9OU0tleWVkQXJjaGl2ZXKoCwwXGBkdJCVVJG51bGzTDQ4PEBEUViRjbGFzc1dOUy5rZXlzWk5TLm9iamVjdHOAB6ISE4ACgAOiFRaABIAGWWFsaWFzRGF0YVxyZWxhdGl2ZVBhdGjSDRobHFdOUy5kYXRhgAVPEQGKAAAAAAGKAAIAAANoc3IAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAADBcRzJSCsAAABGbEEIMjAwNS5wZGYAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAnJx7+LpBcAAAAAAAAAAAAEAAMAAAkgAAAAAAAAAAAAAAAAAAAABUZyaW5rAAAQAAgAAMFxjUkAAAARAAgAAL+MFJcAAAABABgARmxBAEZrzwBGatUARmobAEZkaABAiUMAAgBAaHNyOlVzZXJzOmF0b21pY3BpcmF0ZTpEb2N1bWVudHM6Q2FsdGVjaDpBcnRpY2xlczpGcmluazoyMDA1LnBkZgAOABIACAAyADAAMAA1AC4AcABkAGYADwAIAAMAaABzAHIAEgA8VXNlcnMvYXRvbWljcGlyYXRlL0RvY3VtZW50cy9DYWx0ZWNoL0FydGljbGVzL0ZyaW5rLzIwMDUucGRmABMAAS8AABUAAgAT//8AANIeHyAhWCRjbGFzc2VzWiRjbGFzc25hbWWjISIjXU5TTXV0YWJsZURhdGFWTlNEYXRhWE5TT2JqZWN0XxAjLi4vLi4vLi4vLi4vQXJ0aWNsZXMvRnJpbmsvMjAwNS5wZGbSHh8mJ6InI1xOU0RpY3Rpb25hcnkACAARABoAHwApADIANwA6AD8AQQBTAFwAYgBpAHAAeACDAIUAiACKAIwAjwCRAJMAnQCqAK8AtwC5AkcCTAJVAmACZAJyAnkCggKoAq0CsAAAAAAAAAIBAAAAAAAAACgAAAAAAAAAAAAAAAAAAAK9}, Bdsk-Url-1 = {http://link.aps.org/abstract/PRE/v72/e041923}} @article{limozin:178101, Author = {Laurent Limozin and Alexander Roth and Erich Sackmann}, Date-Modified = {2005-10-24 13:16:17 -0700}, Eid = {178101}, Journal = {Physical Review Letters}, Keywords = {viscoelasticity; cellular biophysics; physiological models; biomechanics; deformation}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Limozin/2005.pdf}, Number = {17}, Numpages = {4}, Pages = {178101}, Publisher = {APS}, Title = {Microviscoelastic Moduli of Biomimetic Cell Envelopes}, Url = {http://link.aps.org/abstract/PRL/v95/e178101}, Volume = {95}, Year = {2005}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://link.aps.org/abstract/PRL/v95/e178101}} @article{Sheetz:1974el, Au = {Singer SJ}, Author = {Sheetz, M P and Singer, S J}, Da = {19750310}, Date-Modified = {2005-09-26 22:59:40 -0400}, Dcom = {19750310}, Edat = {1974/11/01}, Jid = {7505876}, Journal = {Proc Natl Acad Sci U S A}, Keywords = {Ammonium Compounds/metabolism and Binding Sites and *Cell Membrane/metabolism/ultrastructure and Cell Membrane Permeability and Chlorpromazine/analogs \& derivatives/metabolism and Erythrocytes/*ultrastructure and Hemolysis and Humans and Lidocaine/metabolism and *Lipids/metabolism and Microscopy, Electron, Scanning and Molecular Conformation and Nitrobenzenes/metabolism and Phospholipids/metabolism and Proteins/metabolism and Structure-Activity Relationship}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Sheetz/1974.pdf}, Lr = {20041117}, Mhda = {1974/11/01 00:01}, Number = {11}, Own = {NLM}, Pages = {4457-61}, Pl = {UNITED STATES}, Pmid = {4530994}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print}, Rn = {50-53-3 (Chlorpromazine)}, Sb = {IM}, Stat = {MEDLINE}, Title = {Biological membranes as bilayer couples. A molecular mechanism of drug-erythrocyte interactions}, Volume = {71}, Year = {1974}, Bdsk-File-1 = {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}} @article{Kim:1999fv, Abstract = {The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved. In contrast to many mammalian receptors which signal by oligomerizing upon ligand binding, the chemotaxis receptors are dimeric even in the absence of their ligands, and their signalling does not depend on a monomer-dimer equilibrium. Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors. Here we report the crystal structure of the cytoplasmic domain of a serine chemotaxis receptor of Escherichia coli, which reveals a 200 A-long coiled-coil of two antiparallel helices connected by a 'U-turn'. Two of these domains form a long, supercoiled, four-helical bundle in the cytoplasmic portion of the receptor.}, Affiliation = {Department of Chemistry, University of California, Berkeley 94720-5230, USA.}, Aid = {10.1038/23512 {$[$}doi{$]$}}, Au = {Kim SH}, Author = {Kim, K K and Yokota, H and Kim, S H}, Da = {19990908}, Date-Modified = {2005-08-25 09:26:45 -0700}, Dcom = {19990908}, Edat = {1999/08/31 09:00}, Jid = {0410462}, Journal = {Nature}, Keywords = {*Chemotaxis and Cloning, Molecular and Crystallography, X-Ray and Cytoplasm/chemistry and Escherichia coli/*chemistry and Methylation and Models, Molecular and Mutagenesis and Protein Conformation and Receptors, Amino Acid/*chemistry/genetics and Research Support, U.S. Gov't, Non-P.H.S. and Research Support, U.S. Gov't, P.H.S.}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Kim/1999.pdf}, Lr = {20041117}, Mhda = {2001/03/23 10:01}, Number = {6746}, Own = {NLM}, Pages = {787-92}, Pl = {ENGLAND}, Pmid = {10466731}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print}, Rn = {0 (serine receptor)}, Sb = {IM}, Si = {PDB/1QU7}, Stat = {MEDLINE}, Title = {Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor}, Volume = {400}, Year = {1999}, Bdsk-File-1 = {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}} @article{Lefman, Abstract = {Electron tomography is a powerful method for determining the three-dimensional structures of large macromolecular assemblies, such as cells, organelles, and multiprotein complexes, when crystallographic averaging methods are not applicable. Here we used electron tomographic imaging to determine the molecular architecture of Escherichia coli cells engineered to overproduce the bacterial chemotaxis receptor Tsr. Tomograms constructed from fixed, cryosectioned cells revealed that overproduction of Tsr led to formation of an extended internal membrane network composed of stacks and extended tubular structures. We present an interpretation of the tomogram in terms of the packing arrangement of Tsr using constraints derived from previous X-ray and electron-crystallographic studies of receptor clusters. Our results imply that the interaction between the cytoplasmic ends of Tsr is likely to stabilize the presence of the membrane networks in cells overproducing Tsr. We propose that membrane invaginations that are potentially capable of supporting axial interactions between receptor clusters in apposing membranes could also be present in wild-type E. coli and that such receptor aggregates could play an important role in signal transduction during bacterial chemotaxis. }, Author = {Lefman, Jonathan and Zhang, Peijun and Hirai, Teruhisa and Weis, Robert M. and Juliani, Jemma and Bliss, Donald and Kessel, Martin and Bos, Erik and Peters, Peter J. and Subramaniam, Sriram}, Date-Modified = {2005-05-24 12:59:43 -0700}, Eprint = {http://jb.asm.org/cgi/reprint/186/15/5052.pdf}, Journal = {J. Bacteriol.}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Lefman/2004.pdf}, Number = {15}, Pages = {5052-5061}, Title = {Three-Dimensional Electron Microscopic Imaging of Membrane Invaginations in Escherichia coli Overproducing the Chemotaxis Receptor Tsr}, Url = {http://jb.asm.org/cgi/content/abstract/186/15/5052}, Volume = {186}, Year = {2004}, Bdsk-File-1 = {YnBsaXN0MDDUAQIDBAUGCQpYJHZlcnNpb25UJHRvcFkkYXJjaGl2ZXJYJG9iamVjdHMSAAGGoNEHCFRyb290gAFfEA9OU0tleWVkQXJjaGl2ZXKoCwwXGBkdJCVVJG51bGzTDQ4PEBEUViRjbGFzc1dOUy5rZXlzWk5TLm9iamVjdHOAB6ISE4ACgAOiFRaABIAGWWFsaWFzRGF0YVxyZWxhdGl2ZVBhdGjSDRobHFdOUy5kYXRhgAVPEQGOAAAAAAGOAAIAAANoc3IAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAADBcRzJSCsAAABGbJkIMjAwNC5wZGYAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAnKYb64v7cAAAAAAAAAAAAEAAMAAAkgAAAAAAAAAAAAAAAAAAAABkxlZm1hbgAQAAgAAMFxjUkAAAARAAgAAL65IicAAAABABgARmyZAEZrzwBGatUARmobAEZkaABAiUMAAgBBaHNyOlVzZXJzOmF0b21pY3BpcmF0ZTpEb2N1bWVudHM6Q2FsdGVjaDpBcnRpY2xlczpMZWZtYW46MjAwNC5wZGYAAA4AEgAIADIAMAAwADQALgBwAGQAZgAPAAgAAwBoAHMAcgASAD1Vc2Vycy9hdG9taWNwaXJhdGUvRG9jdW1lbnRzL0NhbHRlY2gvQXJ0aWNsZXMvTGVmbWFuLzIwMDQucGRmAAATAAEvAAAVAAIAE///AADSHh8gIVgkY2xhc3Nlc1okY2xhc3NuYW1loyEiI11OU011dGFibGVEYXRhVk5TRGF0YVhOU09iamVjdF8QJC4uLy4uLy4uLy4uL0FydGljbGVzL0xlZm1hbi8yMDA0LnBkZtIeHyYnoicjXE5TRGljdGlvbmFyeQAIABEAGgAfACkAMgA3ADoAPwBBAFMAXABiAGkAcAB4AIMAhQCIAIoAjACPAJEAkwCdAKoArwC3ALkCSwJQAlkCZAJoAnYCfQKGAq0CsgK1AAAAAAAAAgEAAAAAAAAAKAAAAAAAAAAAAAAAAAAAAsI=}, Bdsk-Url-1 = {http://jb.asm.org/cgi/content/abstract/186/15/5052}} @article{Cuvelier:2005ht, Abstract = {Tethers are nanocylinders of lipid bilayer membrane, arising in situations ranging from micromanipulation experiments on synthetic vesicles to the formation of dynamic tubular networks in the Golgi apparatus. Relying on the extensive theoretical and experimental works aimed to understand the physics of individual tethers formation, we addressed the problem of the interaction between two nanotubes. By using a combination of micropipette manipulation and optical tweezers, we quantitatively studied the process of coalescence that occurred when the separation distance between both vesicle-tether junctions became smaller than a threshold length. Our experiments, which were supported by an original theoretical analysis, demonstrated that the measurements of the tether force and angle between tethers at coalescence directly yield the bending rigidity, kappa, and the membrane tension, sigma, of the vesicles. Contrary to other methods used to probe the bending rigidity of vesicles, the proposed approach permits a direct measurement of kappa without requiring any control of the membrane tension. Finally, after validation of the method and proposal of possible applications, we experimentally investigated the dynamics of the coalescence process.}, Affiliation = {Laboratoire de Physico-Chimie Curie, Institut Curie, F-75005 Paris, France.}, Aid = {10.1529/biophysj.104.056473 {$[$}doi{$]$}}, Au = {Nassoy P}, Author = {Cuvelier, D and Derenyi, I and Bassereau, P and Nassoy, P}, Da = {20050328}, Date-Modified = {2008-05-29 16:57:45 -0700}, Dcom = {20050817}, Dep = {20050204}, Edat = {2005/02/08 09:00}, Jid = {0370626}, Journal = {Biophys J}, Keywords = {Animals and Biophysics/*methods and Calibration and Cell Membrane/*chemistry and Chickens and Cytoskeleton/metabolism and Electrochemistry and Lipid Bilayers/*chemistry/metabolism and Lipids/chemistry and Membrane Fluidity and Membranes/*chemistry and Membranes, Artificial and Microscopy, Video and Models, Biological and Models, Statistical and Models, Theoretical and Phosphatidylcholines/chemistry and Research Support, Non-U.S. Gov't and Surface Properties and Time Factors}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Cuvelier/2005a.pdf}, Mhda = {2005/08/18 09:00}, Number = {4}, Own = {NLM}, Pages = {2714--2726}, Phst = {2005/02/04 {$[$}aheadofprint{$]$}}, Pl = {United States}, Pmid = {15695629}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print-Electronic}, Rn = {0 (Phosphatidylcholines)}, Sb = {IM}, Stat = {MEDLINE}, Title = {Coalescence of membrane tethers: experiments, theory, and applications}, Volume = {88}, Year = {2005}, Bdsk-File-1 = {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}} @article{Sackmann:1994pc, Abstract = {The main objective of this lecture is to discuss the role of lipid-bilayer elasticity (1) for the self-organization of lipid/protein-bilayers (2) for the stabilization of domain structures and shapes of cell membranes and (3) for the control of shape transitions (e.g. bud- and pit-formation) and shape instabilities (vesicle fission). It is demonstrated that many complex shape transitions of cell membranes can be mimicked by single lipid bilayer vesicles by simply varying the area-to-volume ratio or by chemically induced bending moments suggesting that these processes are governed by the universal minimum bending energy concept of closed shells composed of stratified membranes. The essential role of the coupling between curvature and phase separation in mixed membranes for the formation and stabilization of local pits and buds or the fission of budded vesicles is demonstrated. Finally, we discuss the consequences of the pronounced thermally excited bending undulations of the hyperelastic membranes for the membrane tension, the material exchange at membrane surfaces and the control of the adhesion of vesicles (or cells) on solid substrates.}, Affiliation = {Physics Department (Biophysics Group E22), Technische Universitat Munchen, Garching, Germany.}, Au = {Sackmann E}, Author = {Sackmann, E}, Da = {19940708}, Date-Modified = {2005-08-25 09:21:47 -0700}, Dcom = {19940708}, Edat = {1994/06/06}, Jid = {0155157}, Journal = {FEBS Lett}, Keywords = {Biophysics and Cell Membrane/*physiology and Cells/*cytology and Cytoskeleton/physiology and Elasticity and Lipid Bilayers and *Liposomes and Membrane Lipids/physiology and Membrane Proteins/physiology and Thermodynamics}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Sackmann/1994.pdf}, Lr = {20001218}, Mhda = {1994/06/06 00:01}, Number = {1}, Own = {NLM}, Pages = {3-16}, Pl = {NETHERLANDS}, Pmid = {8206154}, Pst = {ppublish}, Pt = {Review, Tutorial}, Pubm = {Print}, Rf = {32}, Rn = {0 (Membrane Proteins)}, Sb = {IM}, Stat = {MEDLINE}, Title = {The seventh Datta Lecture. Membrane bending energy concept of vesicle- and cell-shapes and shape-transitions.}, Volume = {346}, Year = {1994}, Bdsk-File-1 = {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}} @article{Umeda:2005oe, Abstract = {Cuplike lipid vesicles with a single hole and tubelike vesicles with two holes were theoretically analyzed by taking into account the line tension of membrane holes and the bending energy of membranes, using the area difference elasticity model. We numerically solved the Euler-Lagrange equation and the boundary conditions holding on the membrane edge to obtain axisymmetric vesicle shapes that minimize the total energy. The numerical results showed that when the line tension is very low, and for appropriate values of the relaxed area difference between the two monolayers of bilayer membranes, the model yields cup-, tube-, and funnel-shaped vesicles that closely resemble previously observed shapes of opening-up vesicles with additive guest molecules such as the protein talin and some detergents. This strongly suggests that these additive molecules greatly reduce the line tension of lipid membranes. The effect of the Gaussian bending modulus on the shape of the opening-up vesicles was also evaluated and the effect is greatest when the size of hole is small.}, Affiliation = {Faculty of Maritime Sciences, Kobe University, Fukae-minami-machi, Higashinada-ku, Kobe 658-0022, Japan.}, Au = {Hotani H}, Author = {Umeda, Tamiki and Suezaki, Yukio and Takiguchi, Kingo and Hotani, Hirokazu}, Da = {20050208}, Date-Modified = {2005-08-25 09:10:58 -0700}, Dcom = {20050519}, Dep = {20050131}, Edat = {2005/02/09 09:00}, Jid = {101136452}, Journal = {Phys Rev E Stat Nonlin Soft Matter Phys}, Keywords = {Comparative Study and Computer Simulation and Lipid Bilayers/*chemistry and Liposomes/*chemistry and *Membrane Fluidity and Membranes, Artificial and Microfluidics/*methods and *Models, Chemical and Permeability and Research Support, Non-U.S. Gov't}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Umeda/2005.pdf}, Mhda = {2005/05/20 09:00}, Number = {1 Pt 1}, Own = {NLM}, Pages = {011913}, Phst = {2005/01/31 {$[$}aheadofprint{$]$}}, Pl = {United States}, Pmid = {15697636}, Pst = {ppublish}, Pt = {Validation Studies}, Pubm = {Print-Electronic}, Rn = {0 (Liposomes)}, Sb = {IM}, Stat = {MEDLINE}, Title = {Theoretical analysis of opening-up vesicles with single and two holes}, Volume = {71}, Year = {2005}, Bdsk-File-1 = {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}} @article{Sung-HouKim09032002, Abstract = {Bacterial chemotaxis receptors can detect a small concentration gradient of attractants and repellents in the environment over a wide range of background concentration. The clustering of these receptors to form patches observed in vivo and in vitro has been suspected as a reason for the high sensitivity, and such wide dynamic range is thought to be due to the resetting of the receptor sensitivity threshold by methylation/demethylation of the receptors. However, the mechanisms by which such high sensitivity is achieved and how the methylation/demethylation resets the sensitivity are not well understood. A molecular modeling of an intact bacterial chemotaxis receptor based on the crystal structures of a cytoplasmic domain and a periplasmic domain suggests an interesting clustering of three dimeric receptors and a two-dimensional, close-packed lattice formation of the clusters, where each receptor dimer contacts two other receptor dimers at the cytoplasmic domain and two yet different receptor dimers at the periplasmic domain. This interconnection of the receptors to form a patch of receptor clusters suggests a structural basis for the high sensitivity of the bacterial chemotaxis receptors. Furthermore, we present crystallographic data suggesting that, in contrast to most molecular signaling by conformational changes and/or oligomerization of the signaling molecules, the changes in dynamic property of the receptors on ligand binding or methylation may be the language of the signaling by the chemotaxis receptors. Taken together, the changes of the dynamic property of one receptor propagating mechanically to many others in the receptor patch provides a plausible, simple mechanism for the high sensitivity and the dynamic range of the receptors. }, Author = {Kim, Sung-Hou and Wang, Weiru and Kim, Kyeong Kyu}, Date-Modified = {2005-08-25 09:14:15 -0700}, Eprint = {http://www.pnas.org/cgi/reprint/99/18/11611.pdf}, Journal = {PNAS}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Kim/2002.pdf}, Number = {18}, Pages = {11611-11615}, Title = {Dynamic and clustering model of bacterial chemotaxis receptors: Structural basis for signaling and high sensitivity}, Url = {http://www.pnas.org/cgi/content/abstract/99/18/11611}, Volume = {99}, Year = {2002}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://www.pnas.org/cgi/content/abstract/99/18/11611}} @article{Baumgart:2003us, Abstract = {Lipid bilayer membranes--ubiquitous in biological systems and closely associated with cell function--exhibit rich shape-transition behaviour, including bud formation and vesicle fission. Membranes formed from multiple lipid components can laterally separate into coexisting liquid phases, or domains, with distinct compositions. This process, which may resemble raft formation in cell membranes, has been directly observed in giant unilamellar vesicles. Detailed theoretical frameworks link the elasticity of domains and their boundary properties to the shape adopted by membranes and the formation of particular domain patterns, but it has been difficult to experimentally probe and validate these theories. Here we show that high-resolution fluorescence imaging using two dyes preferentially labelling different fluid phases directly provides a correlation between domain composition and local membrane curvature. Using freely suspended membranes of giant unilamellar vesicles, we are able to optically resolve curvature and line tension interactions of circular, stripe and ring domains. We observe long-range domain ordering in the form of locally parallel stripes and hexagonal arrays of circular domains, curvature-dependent domain sorting, and membrane fission into separate vesicles at domain boundaries. By analysing our observations using available membrane theory, we are able to provide experimental estimates of boundary tension between fluid bilayer domains.}, Affiliation = {Applied and Engineering Physics, Cornell University, Ithaca, New York 14853, USA.}, Aid = {nature02013 {$[$}pii{$]$}}, Au = {Webb WW}, Author = {Baumgart, T and Hess, S T and Webb, W W}, Da = {20031023}, Date-Modified = {2008-05-29 16:41:31 -0700}, Dcom = {20031117}, Edat = {2003/10/24 05:00}, Jid = {0410462}, Journal = {Nature}, Keywords = {Cell Membrane/chemistry/metabolism and Fluorescent Dyes and Lipid Bilayers/*chemistry/*metabolism and Liposomes/*chemistry/*metabolism and Microscopy, Fluorescence and Models, Biological and Models, Chemical and Phosphatidylcholines/metabolism and Phosphatidylethanolamines/metabolism and Photons and Research Support, Non-U.S. Gov't and Research Support, U.S. Gov't, P.H.S. and Temperature}, Language = {eng}, Local-Url = {file://localhost/Users/wiggins/research/Papers/Baumgart2003.pdf}, Lr = {20041117}, Mhda = {2003/12/03 05:00}, Number = {6960}, Own = {NLM}, Pages = {821--824}, Phst = {2003/08/19 {$[$}accepted{$]$}}, Pl = {England}, Pmid = {14574408}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print}, Rn = {3026-45-7 (1,2-dipalmitoyl-3-phosphatidylethanolamine)}, Sb = {IM}, Stat = {MEDLINE}, Title = {Imaging coexisting fluid domains in biomembrane models coupling curvature and line tension}, Volume = {425}, Year = {2003}, Bdsk-File-1 = {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}} @article{laradji:198105, Author = {Mohamed Laradji and P. B. Sunil Kumar}, Date-Modified = {2005-04-01 17:26:52 -0800}, Eid = {198105}, Journal = {Physical Review Letters}, Keywords = {phase separation; biomembranes; lipid bilayers}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Laradji/2004.pdf}, Number = {19}, Numpages = {4}, Pages = {198105}, Publisher = {APS}, Title = {Dynamics of Domain Growth in Self-Assembled Fluid Vesicles}, Url = {http://link.aps.org/abstract/PRL/v93/e198105}, Volume = {93}, Year = {2004}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://link.aps.org/abstract/PRL/v93/e198105}} @article{Claessens:2004mu, Abstract = {The swelling behavior of charged phospholipids in pure water is completely different from that of neutral or isoelectric phospholipids. It was therefore suggested in the past that, instead of multilamellar phases, vesicles represent the stable structures of charged lipids in excess water. In this article, we show that this might indeed be the case for dioleoylphosphatidylglycerol and even for dioleoylphosphatidylcholine in certain salts. The size of the vesicles formed by these lipids depends on the phospholipid concentration in a way that has been predicted in the literature for vesicles of which the curvature energy is compensated for by translational entropy and a renormalization of the bending moduli (entropic stabilization). Self-consistent field calculations on charged bilayers show that the mean bending modulus kc and the Gaussian bending modulus k have opposite sign and /k/>kc, especially at low ionic strength. This has the implication that the energy needed to curve the bilayer into a closed vesicle Eves=4pi(2kc+k) is much less than one would expect based on the value of kc alone. As a result, Eves can relatively easily be entropically compensated. The radii of vesicles that are stabilized by entropy are expected to depend on the membrane persistence length and thus on kc. Experiments in which the vesicle size is studied as a function of the salt and the salt concentration correlate well with self-consistent field predictions of kc as a function of ionic strength.}, Affiliation = {Laboratory of Physical Chemistry and Colloid Science, and Laboratory of Plant Physiology, Wageningen University, Wageningen, The Netherlands. mireille.claessens@wur.nl}, Aid = {biophysj.103.036772 {$[$}pii{$]$}}, Au = {Cohen Stuart MA}, Author = {Claessens, M M A E and van Oort, B F and Leermakers, F A M and Hoekstra, F A and Cohen Stuart, M A}, Da = {20041201}, Date-Modified = {2005-05-05 17:07:05 -0700}, Dcom = {20050426}, Dep = {20040917}, Edat = {2004/09/21 05:00}, Jid = {0370626}, Journal = {Biophys J}, Keywords = {Computer Simulation and Elasticity and Electrostatics and Lipid Bilayers/*chemistry and Liposomes/*chemistry and *Membrane Fluidity and *Models, Chemical and *Models, Molecular and Molecular Conformation and Particle Size and Phosphatidylglycerols/*chemistry and Sodium Chloride/*chemistry and Stress, Mechanical and Surface Properties and Temperature}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Claessens/2004.pdf}, Mhda = {2005/04/27 09:00}, Number = {6}, Own = {NLM}, Pages = {3882-93}, Phst = {2004/09/17 {$[$}aheadofprint{$]$}}, Pl = {United States}, Pmid = {15377511}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print-Electronic}, Rn = {7647-14-5 (Sodium Chloride)}, Sb = {IM}, Stat = {MEDLINE}, Title = {Charged lipid vesicles: effects of salts on bending rigidity, stability, and size}, Volume = {87}, Year = {2004}, Bdsk-File-1 = {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}} @article{Giardini:2003qs, Abstract = {Polymerizing networks of actin filaments generate force for a variety of movements in living cells, including protrusion of filopodia and lamellipodia, intra- and intercellular motility of certain bacterial and viral pathogens, and motility of endocytic vesicles and other membrane-bound organelles. During actin-based motility, coexisting populations of actin filaments exert both pushing and retarding forces on the moving cargo. To examine the distribution and magnitude of forces generated by actin, we have developed a model system where large artificial lipid vesicles coated with the protein ActA from the bacterial pathogen Listeria monocytogenes are propelled by actin polymerization in cytoplasmic extract. We find that motile vesicles associated with actin comet tails are significantly deformed due to an inward compression force exerted by actin polymerization orthogonal to the direction of motion, which is >10-fold greater in magnitude than the component of the force exerted in the direction of motion. Furthermore, there is a spatial segregation of the pushing and retarding forces, such that pushing predominates along the sides of the vesicle, although retarding forces predominate at the rear. We estimate that the total net (pushing minus retarding) force generated by the actin comet tail is approximately 0.4-4 nN. In addition, actin comet tail formation is associated with polarization of the ActA protein on the fluid vesicle surface, which may reinforce the persistence of unidirectional motion by helping to maintain a persistent asymmetry of actin filament density.}, Affiliation = {Department of Biochemistry, Stanford University School of Medicine, CA 94305-5307, USA.}, Aid = {1031670100 {$[$}pii{$]$}}, Au = {Theriot JA}, Author = {Giardini, Paula A and Fletcher, Daniel A and Theriot, Julie A}, Da = {20030528}, Date-Modified = {2005-04-13 10:30:21 -0700}, Dcom = {20030716}, Dep = {20030508}, Edat = {2003/05/10 05:00}, Jid = {7505876}, Journal = {Proc Natl Acad Sci U S A}, Keywords = {Actins/*metabolism and Biopolymers and Lipids/*metabolism and Models, Biological and Research Support, Non-U.S. Gov't}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Giardini/2003.pdf}, Lr = {20041117}, Mhda = {2003/07/17 05:00}, Number = {11}, Own = {NLM}, Pages = {6493-8}, Phst = {2003/05/08 {$[$}aheadofprint{$]$}}, Pl = {United States}, Pmid = {12738883}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print-Electronic}, Rn = {0 (Lipids)}, Sb = {IM}, Stat = {MEDLINE}, Title = {Compression forces generated by actin comet tails on lipid vesicles}, Volume = {100}, Year = {2003}, Bdsk-File-1 = {YnBsaXN0MDDUAQIDBAUGCQpYJHZlcnNpb25UJHRvcFkkYXJjaGl2ZXJYJG9iamVjdHMSAAGGoNEHCFRyb290gAFfEA9OU0tleWVkQXJjaGl2ZXKoCwwXGBkdJCVVJG51bGzTDQ4PEBEUViRjbGFzc1dOUy5rZXlzWk5TLm9iamVjdHOAB6ISE4ACgAOiFRaABIAGWWFsaWFzRGF0YVxyZWxhdGl2ZVBhdGjSDRobHFdOUy5kYXRhgAVPEQGUAAAAAAGUAAIAAANoc3IAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAADBcRzJSCsAAABGbEYIMjAwMy5wZGYAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAnKAL6BgexQREYgAAAAAAAEAAMAAAkgAAAAAAAAAAAAAAAAAAAACEdpYXJkaW5pABAACAAAwXGNSQAAABEACAAAvoHkXAAAAAEAGABGbEYARmvPAEZq1QBGahsARmRoAECJQwACAENoc3I6VXNlcnM6YXRvbWljcGlyYXRlOkRvY3VtZW50czpDYWx0ZWNoOkFydGljbGVzOkdpYXJkaW5pOjIwMDMucGRmAAAOABIACAAyADAAMAAzAC4AcABkAGYADwAIAAMAaABzAHIAEgA/VXNlcnMvYXRvbWljcGlyYXRlL0RvY3VtZW50cy9DYWx0ZWNoL0FydGljbGVzL0dpYXJkaW5pLzIwMDMucGRmAAATAAEvAAAVAAIAE///AADSHh8gIVgkY2xhc3Nlc1okY2xhc3NuYW1loyEiI11OU011dGFibGVEYXRhVk5TRGF0YVhOU09iamVjdF8QJi4uLy4uLy4uLy4uL0FydGljbGVzL0dpYXJkaW5pLzIwMDMucGRm0h4fJieiJyNcTlNEaWN0aW9uYXJ5AAgAEQAaAB8AKQAyADcAOgA/AEEAUwBcAGIAaQBwAHgAgwCFAIgAigCMAI8AkQCTAJ0AqgCvALcAuQJRAlYCXwJqAm4CfAKDAowCtQK6Ar0AAAAAAAACAQAAAAAAAAAoAAAAAAAAAAAAAAAAAAACyg==}} @article{Jenkins:1977nx, Abstract = {The membrane of the red blood cell is modeled as a fluid shell which resists bending and changes in area. The differential equations governing the mechanical equilibrium of such a membrane are derived and axisymmetric solutions are obtained numerically.}, Annote = {aka Jenkins2 in the short notes}, Au = {Jenkins JT}, Author = {Jenkins, J T}, Da = {19770929}, Date-Modified = {2008-01-16 11:37:19 -0800}, Dcom = {19770929}, Edat = {1977/05/23}, Jid = {7502105}, Journal = {J Math Biol}, Keywords = {*Biomechanics and Cell Membrane and *Erythrocytes and Mathematics and *Models, Biological}, Language = {eng}, Lr = {20001218}, Mhda = {1977/05/23 00:01}, Number = {2}, Own = {NLM}, Pages = {149-69}, Pl = {GERMANY, WEST}, Pmid = {886227}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print}, Sb = {IM}, Stat = {MEDLINE}, Title = {Static equilibrium configurations of a model red blood cell}, Volume = {4}, Year = {1977}} @article{Powers:2002wd, Abstract = {Thin cylindrical tethers are common lipid bilayer membrane structures, arising in situations ranging from micromanipulation experiments on artificial vesicles to the dynamic structure of the Golgi apparatus. We study the shape and formation of a tether in terms of the classical soap-film problem, which is applied to the case of a membrane disk under tension subject to a point force. A tether forms from the elastic boundary layer near the point of application of the force, for sufficiently large displacement. Analytic results for various aspects of the membrane shape are given.}, Affiliation = {Division of Engineering, Brown University, Providence, Rhode Island 02912, USA. Thomas_Powers@brown.edu}, Au = {Goldstein RE}, Author = {Powers, T R and Huber, G and Goldstein, R E}, Da = {20020513}, Date-Modified = {2008-05-29 17:00:59 -0700}, Dcom = {20021108}, Dep = {20020313}, Edat = {2002/05/15 10:00}, Jid = {101136452}, Journal = {Phys Rev E}, Keywords = {Cytoplasmic Vesicles/chemistry and Elasticity and Golgi Apparatus/chemistry and Lipid Bilayers/*chemistry and Membrane Fluidity and *Membranes, Artificial and Models, Biological and Research Support, U.S. Gov't, Non-P.H.S. and Surface Properties and Tubulin/chemistry}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Powers/2002.pdf}, Lr = {20041117}, Mhda = {2002/11/26 04:00}, Number = {4 Pt 1}, Own = {NLM}, Pages = {041901}, Phst = {2002/03/13 {$[$}aheadofprint{$]$}}, Pl = {United States}, Pmid = {12005867}, Pst = {ppublish}, Pt = {Review, Tutorial}, Pubm = {Print-Electronic}, Rf = {40}, Rn = {0 (Tubulin)}, Sb = {IM}, Stat = {MEDLINE}, Title = {Fluid-membrane tethers: minimal surfaces and elastic boundary layers}, Volume = {65}, Year = {2002}, Bdsk-File-1 = {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}} @article{Kamien, Author = {Kamien, Randall D}, Date-Added = {2005-03-03 09:15:08 -0800}, Date-Modified = {2005-03-16 21:12:05 -0800}, Journal = {Rev Mod Phys}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Kamien/2002.pdf}, Month = {September}, Pages = {953}, Title = {The geometry of soft materials: a primer}, Volume = {74}, Year = {2002}, Bdsk-File-1 = {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}} @article{Calladine:2002vp, Abstract = {It is well-known that a {\tt{}"{}} tether{\tt{}"{}} may be drawn out from a pressurized liposome by means of a suitably applied radial-outward force applied locally to the lipid bilayer. The tether is a narrow, uniform cylindrical tube, which joins the main vesicle in a short "transition region." A first-order energy analysis establishes the broad relationship between the force F needed to draw the tether, the radius R0 of the tether, the bending-stiffness constant B for the lipid bilayer and the membrane tension T in the pressurized liposome. The aim of the present paper is to study in detail the "transition region" between the tether and the main vesicle, by means of a careful application of the engineering theory of axisymmetric shell structures. It turns out that the well-known textbook "thin-shell" theory is inadequate for this purpose, because the tether is evidently an example of a thick-walled shell; and a novel ingredient of the present study is the introduction of elastic constitutive relations that are appropriate to the thick-shell situation. The governing equations are set up in dimensionless form, and are solved by means of a "shooting" technique, starting with a single disposable parameter at a point on the meridian in the tether, which can be adjusted until the boundary conditions at the far "equator" of the main vessel are satisfied. It turns out that the "transition region" between the tether and the main vessel is well characterized by only a few parameters, while the tether and main vessel themselves are described by very simple equations. Introduction of the thick-shell constitutive relation makes little difference to the conformation of and stress-resultants in, the main vessel; but it makes a great deal of difference in the tether itself Indeed, a kind of phase-change appears to take place in the "transition region" between these two zones of the liposome.}, Affiliation = {Department of Engineering, University of Cambridge, UK.}, Au = {Greenwood JA}, Author = {Calladine, C R and Greenwood, J A}, Da = {20021030}, Date-Modified = {2005-03-16 21:24:06 -0800}, Dcom = {20030424}, Edat = {2002/10/31 04:00}, Jid = {7909584}, Journal = {J Biomech Eng}, Keywords = {*Computer Simulation and Elasticity and Lipid Bilayers/*chemistry and Liposomes/*chemistry and Membrane Fluidity and *Models, Chemical and *Models, Molecular and Molecular Conformation and Pressure and *Sensitivity and Specificity and Stress, Mechanical and Surface Properties and Torque and Viscosity}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Calladine/2002.pdf}, Mhda = {2003/04/25 05:00}, Number = {5}, Own = {NLM}, Pages = {576-85}, Pl = {United States}, Pmid = {12405601}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print}, Rn = {0 (Liposomes)}, Sb = {IM}, Stat = {MEDLINE}, Title = {Mechanics of tether formation in liposomes}, Volume = {124}, Year = {2002}, Bdsk-File-1 = {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}} @book{Wald, Address = {Chicago}, Author = {Wald, R M}, Date-Modified = {2008-05-30 00:35:54 -0700}, Pages = {453}, Publisher = {The University of Chicago Press}, Title = {General Relativity}, Year = {1984}} @article{Canham:1970rc, Au = {Canham PB}, Author = {Canham, P B}, Da = {19700302}, Date-Modified = {2008-05-29 16:43:50 -0700}, Dcom = {19700302}, Edat = {1970/01/01}, Jid = {0376342}, Journal = {J Theor Biol}, Keywords = {Cell Membrane/*physiology and Elasticity and Erythrocytes/*physiology and Humans and Hypotonic Solutions and Isotonic Solutions and Models, Theoretical and Osmotic Pressure and Photomicrography}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Canham/1970.pdf}, Lr = {20041117}, Mhda = {1970/01/01 00:01}, Number = {1}, Own = {NLM}, Pages = {61--81}, Pl = {ENGLAND}, Pmid = {5411112}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print}, Rn = {0 (Isotonic Solutions)}, Sb = {IM}, Stat = {MEDLINE}, Title = {The minimum energy of bending as a possible explanation of the biconcave shape of the human red blood cell}, Volume = {26}, Year = {1970}, Bdsk-File-1 = {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}} @article{yamamoto:7937, Author = {Satoru Yamamoto and Shi-aki Hyodo}, Date-Modified = {2005-04-01 17:26:16 -0800}, Journal = {The Journal of Chemical Physics}, Keywords = {membranes; biomembranes; phase separation}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Yamamoto/2003.pdf}, Number = {17}, Pages = {7937-7943}, Publisher = {AIP}, Title = {Budding and fission dynamics of two-component vesicles}, Url = {http://link.aip.org/link/?JCP/118/7937/1}, Volume = {118}, Year = {2003}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://link.aip.org/link/?JCP/118/7937/1}} @article{koster:068101, Author = {Gerbrand Koster and Angelo Cacciuto and Imre Derenyi and Daan Frenkel and Marileen Dogterom}, Date-Modified = {2005-03-16 21:23:03 -0800}, Eid = {068101}, Journal = {Physical Review Letters}, Keywords = {membranes; Monte Carlo methods; radiation pressure; lipid bilayers}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Koster/2005.pdf}, Number = {6}, Numpages = {4}, Pages = {068101}, Publisher = {APS}, Title = {Force Barriers for Membrane Tube Formation}, Url = {http://link.aps.org/abstract/PRL/v94/e068101}, Volume = {94}, Year = {2005}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://link.aps.org/abstract/PRL/v94/e068101}} @article{Kuwert, Author = {Kuwert, Ernst and Sch{\"a}tzle, Reiner}, Date-Added = {2005-03-03 09:23:18 -0800}, Date-Modified = {2005-03-16 21:10:30 -0800}, Journal = {J Differential Geometry}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Kuwert/2001.pdf}, Pages = {409-441}, Title = {The Willmore Flow With Small Initial Energy}, Volume = {57}, Year = {2001}, Bdsk-File-1 = {YnBsaXN0MDDUAQIDBAUGCQpYJHZlcnNpb25UJHRvcFkkYXJjaGl2ZXJYJG9iamVjdHMSAAGGoNEHCFRyb290gAFfEA9OU0tleWVkQXJjaGl2ZXKoCwwXGBkdJCVVJG51bGzTDQ4PEBEUViRjbGFzc1dOUy5rZXlzWk5TLm9iamVjdHOAB6ISE4ACgAOiFRaABIAGWWFsaWFzRGF0YVxyZWxhdGl2ZVBhdGjSDRobHFdOUy5kYXRhgAVPEQGOAAAAAAGOAAIAAANoc3IAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAADBcRzJSCsAAABGbJAIMjAwMS5wZGYAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAnLAbhZ1YYAAAAAAAAAAAAEAAMAAAkgAAAAAAAAAAAAAAAAAAAABkt1d2VydAAQAAgAAMFxjUkAAAARAAgAALhaRgYAAAABABgARmyQAEZrzwBGatUARmobAEZkaABAiUMAAgBBaHNyOlVzZXJzOmF0b21pY3BpcmF0ZTpEb2N1bWVudHM6Q2FsdGVjaDpBcnRpY2xlczpLdXdlcnQ6MjAwMS5wZGYAAA4AEgAIADIAMAAwADEALgBwAGQAZgAPAAgAAwBoAHMAcgASAD1Vc2Vycy9hdG9taWNwaXJhdGUvRG9jdW1lbnRzL0NhbHRlY2gvQXJ0aWNsZXMvS3V3ZXJ0LzIwMDEucGRmAAATAAEvAAAVAAIAE///AADSHh8gIVgkY2xhc3Nlc1okY2xhc3NuYW1loyEiI11OU011dGFibGVEYXRhVk5TRGF0YVhOU09iamVjdF8QJC4uLy4uLy4uLy4uL0FydGljbGVzL0t1d2VydC8yMDAxLnBkZtIeHyYnoicjXE5TRGljdGlvbmFyeQAIABEAGgAfACkAMgA3ADoAPwBBAFMAXABiAGkAcAB4AIMAhQCIAIoAjACPAJEAkwCdAKoArwC3ALkCSwJQAlkCZAJoAnYCfQKGAq0CsgK1AAAAAAAAAgEAAAAAAAAAKAAAAAAAAAAAAAAAAAAAAsI=}} @unpublished{Chou, Author = {Chou, Tom}, Date-Added = {2005-03-02 17:59:39 -0800}, Date-Modified = {2005-03-16 21:18:54 -0800}, Keywords = {membrane canham helfrich energy area difference bilayer couple}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Chou/2002.pdf}, Month = {December}, Title = {Physics of Cellular Materials: Biomembranes}, Year = {2002}, Bdsk-File-1 = {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}} @article{cirak01, Author = {Cirak, F and Ortiz, M}, Date-Added = {2005-03-03 09:51:46 -0800}, Date-Modified = {2005-03-16 21:08:18 -0800}, Journal = {Int J Numer Meth Eng}, Keywords = {finite elements; non-linear shell elements; subdivision surfaces}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Cirak/2001.pdf}, Month = {July}, Number = {7}, Pages = {813-833}, Title = {Fully C-1-conforming subdivision elements for finite deformation thin-shell analysis}, Volume = {51}, Year = {2001}, Bdsk-File-1 = {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}} @article{Larabell:2004yd, Abstract = {We examined the yeast, Saccharomyces cerevisiae, using X-ray tomography and demonstrate unique views of the internal structural organization of these cells at 60-nm resolution. Cryo X-ray tomography is a new imaging technique that generates three-dimensional (3-D) information of whole cells. In the energy range of X-rays used to examine cells, organic material absorbs approximately an order of magnitude more strongly than water. This produces a quantifiable natural contrast in fully hydrated cells and eliminates the need for chemical fixatives or contrast enhancement reagents to visualize cellular structures. Because proteins can be localized in the X-ray microscope using immunogold labeling protocols (Meyer-Ilse et al., 2001. J. Microsc. 201, 395-403), tomography enables 3-D molecular localization. The time required to collect the data for each cell shown here was <15 min and has recently been reduced to 3 min, making it possible to examine numerous yeast and to collect statistically significant high-resolution data. In this video essay, we show examples of 3-D tomographic reconstructions of whole yeast and demonstrate the power of this technology to obtain quantifiable information from whole, hydrated cells.}, Affiliation = {Department of Anatomy, University of California, San Francisco California 94143, USA. larabel@itsa.ucsf.edu}, Aid = {E03-07-0522 {$[$}pii{$]$}}, Au = {Le Gros MA}, Author = {Larabell, Carolyn A and Le Gros, Mark A}, Da = {20040304}, Date-Modified = {2005-03-30 11:42:23 -0800}, Dcom = {20041102}, Dep = {20031229}, Edat = {2003/12/31 05:00}, Gr = {GM 63948/GM/NIGMS}, Jid = {9201390}, Journal = {Mol Biol Cell}, Keywords = {*Cryopreservation and Image Processing, Computer-Assisted and Organelles/*ultrastructure and Research Support, U.S. Gov't, Non-P.H.S. and Research Support, U.S. Gov't, P.H.S. and Saccharomyces cerevisiae/*ultrastructure and Tomography, X-Ray Computed/*methods}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Larabell/2004.pdf}, Lr = {20041117}, Mhda = {2004/11/04 09:00}, Number = {3}, Own = {NLM}, Pages = {957-62}, Phst = {2003/12/29 {$[$}aheadofprint{$]$}}, Pl = {United States}, Pmid = {14699066}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print-Electronic}, Sb = {IM}, Stat = {MEDLINE}, Title = {X-ray tomography generates 3-D reconstructions of the yeast, saccharomyces cerevisiae, at 60-nm resolution.}, Volume = {15}, Year = {2004}, Bdsk-File-1 = {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}} @article{cirak00, Author = {Cirak, F and Ortiz, M and Schroder, P}, Date-Added = {2005-03-03 09:54:07 -0800}, Date-Modified = {2005-03-16 21:08:03 -0800}, Journal = {Int J Numer Meth Eng}, Keywords = {shells; finite elements; subdivision surfaces}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Cirak/2000.pdf}, Month = {April}, Number = {12}, Pages = {2039-2072}, Title = {Subdivision surfaces: a new paradigm for thin-shell finite-element analysis}, Volume = {47}, Year = {2000}, Bdsk-File-1 = {YnBsaXN0MDDUAQIDBAUGCQpYJHZlcnNpb25UJHRvcFkkYXJjaGl2ZXJYJG9iamVjdHMSAAGGoNEHCFRyb290gAFfEA9OU0tleWVkQXJjaGl2ZXKoCwwXGBkdJCVVJG51bGzTDQ4PEBEUViRjbGFzc1dOUy5rZXlzWk5TLm9iamVjdHOAB6ISE4ACgAOiFRaABIAGWWFsaWFzRGF0YVxyZWxhdGl2ZVBhdGjSDRobHFdOUy5kYXRhgAVPEQGKAAAAAAGKAAIAAANoc3IAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAADBcRzJSCsAAABGbBYIMjAwMC5wZGYAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAnLQr5MjVEAAAAAAAAAAAAEAAMAAAkgAAAAAAAAAAAAAAAAAAAABUNpcmFrAAAQAAgAAMFxjUkAAAARAAgAAL5M/dEAAAABABgARmwWAEZrzwBGatUARmobAEZkaABAiUMAAgBAaHNyOlVzZXJzOmF0b21pY3BpcmF0ZTpEb2N1bWVudHM6Q2FsdGVjaDpBcnRpY2xlczpDaXJhazoyMDAwLnBkZgAOABIACAAyADAAMAAwAC4AcABkAGYADwAIAAMAaABzAHIAEgA8VXNlcnMvYXRvbWljcGlyYXRlL0RvY3VtZW50cy9DYWx0ZWNoL0FydGljbGVzL0NpcmFrLzIwMDAucGRmABMAAS8AABUAAgAT//8AANIeHyAhWCRjbGFzc2VzWiRjbGFzc25hbWWjISIjXU5TTXV0YWJsZURhdGFWTlNEYXRhWE5TT2JqZWN0XxAjLi4vLi4vLi4vLi4vQXJ0aWNsZXMvQ2lyYWsvMjAwMC5wZGbSHh8mJ6InI1xOU0RpY3Rpb25hcnkACAARABoAHwApADIANwA6AD8AQQBTAFwAYgBpAHAAeACDAIUAiACKAIwAjwCRAJMAnQCqAK8AtwC5AkcCTAJVAmACZAJyAnkCggKoAq0CsAAAAAAAAAIBAAAAAAAAACgAAAAAAAAAAAAAAAAAAAK9}} @article{Lin:2004dp, Abstract = {We present a theoretical treatment and simulation algorithm for the dynamics of Helfrich elastic membrane surfaces in the presence of general harmonic perturbations and hydrodynamic coupling to the surrounding solvent. In the limit of localized and strong interactions, this harmonic model can be used to pin the membrane to intracellular/intercellular structures. We consider the case of pinning to the cytoskeleton and use such a model to estimate the macroscopic diffusion constant for band 3 protein on the surface of human erythrocytes. Comparison to experimental results suggests that thermal undulations of the membrane surface should play a significant role in protein mobility on the red blood cell.}, Affiliation = {Department of Physics, University of California, Santa Barbara, California 93106-9510, USA.}, Au = {Brown FL}, Author = {Lin, Lawrence C-L and Brown, Frank L H}, Da = {20040128}, Date-Modified = {2005-03-30 11:36:08 -0800}, Dcom = {20040920}, Edat = {2004/01/30 05:00}, Jid = {0370626}, Journal = {Biophys J}, Keywords = {Adsorption and *Algorithms and Anion Exchange Protein 1, Erythrocyte/*chemistry and Computer Simulation and Cytoskeleton/*chemistry and Diffusion and Erythrocyte Membrane/*chemistry and Lipid Bilayers/*chemistry and *Membrane Fluidity and *Models, Biological and Models, Chemical and Motion and Research Support, U.S. Gov't, Non-P.H.S.}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Lin/2004.pdf}, Lr = {20041117}, Mhda = {2004/09/21 05:00}, Number = {2}, Own = {NLM}, Pages = {764-80}, Pl = {United States}, Pmid = {14747313}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print}, Rn = {0 (Lipid Bilayers)}, Sb = {IM}, Stat = {MEDLINE}, Title = {Dynamics of pinned membranes with application to protein diffusion on the surface of red blood cells.}, Volume = {86}, Year = {2004}, Bdsk-File-1 = 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@inbook{Deckelnick, Author = {Deckelnick, K and Dziuk, G}, Chapter = {Mean curvature flow and related topics}, Date-Added = {2005-03-02 18:24:30 -0800}, Date-Modified = {2005-03-16 21:18:41 -0800}, Editor = {Blowey, F and Craig, A W and Shardlow, T}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Deckelnick/2003.pdf}, Pages = {63-108}, Publisher = {Springer}, Series = {Universitext}, Title = {Frontiers in Numerical Analysis}, Volume = {XIII}, Year = {2003}, Bdsk-File-1 = 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@inproceedings{Desbrun:1999aa, Author = {Desbrun, Mathieu and Meyer, Mark and Schr{\"o}der, Peter and Barr, Alan H.}, Booktitle = {International Conference on Computer Graphics and Interactive Techniques: Proceedings of the 26th annual conference on Computer graphics and interactive techniques}, Date-Added = {2005-03-10 14:40:23 -0800}, Date-Modified = {2005-03-18 14:12:23 -0800}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Desbrun/1999.pdf}, Pages = {317--324}, Title = {Implicit fairing of irregular meshes using diffusion and curvature flow}, Year = {1999}, Bdsk-File-1 = 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@incollection{Meyer02Vismath, Address = {Heidelberg}, Author = {Mark Meyer and Mathieu Desbrun and Peter Schr{\"o}der and Alan H. Barr}, Booktitle = {Visualization and Mathematics III}, Date-Modified = {2005-03-16 21:25:22 -0800}, Editor = {Hans-Christian Hege and Konrad Polthier}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Meyer/2003.pdf}, Pages = {35--57}, Publisher = {Springer-Verlag}, Title = {Discrete Differential-Geometry Operators for Triangulated 2-Manifolds}, Year = {2003}, Bdsk-File-1 = {YnBsaXN0MDDUAQIDBAUGCQpYJHZlcnNpb25UJHRvcFkkYXJjaGl2ZXJYJG9iamVjdHMSAAGGoNEHCFRyb290gAFfEA9OU0tleWVkQXJjaGl2ZXKoCwwXGBkdJCVVJG51bGzTDQ4PEBEUViRjbGFzc1dOUy5rZXlzWk5TLm9iamVjdHOAB6ISE4ACgAOiFRaABIAGWWFsaWFzRGF0YVxyZWxhdGl2ZVBhdGjSDRobHFdOUy5kYXRhgAVPEQGKAAAAAAGKAAIAAANoc3IAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAADBcRzJSCsAAABGbLgIMjAwMy5wZGYAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAnKy75dy1hQREYgQ0FSTwAEAAMAAAkgAAAAAAAAAAAAAAAAAAAABU1leWVyAAAQAAgAAMFxjUkAAAARAAgAAL5eO9gAAAABABgARmy4AEZrzwBGatUARmobAEZkaABAiUMAAgBAaHNyOlVzZXJzOmF0b21pY3BpcmF0ZTpEb2N1bWVudHM6Q2FsdGVjaDpBcnRpY2xlczpNZXllcjoyMDAzLnBkZgAOABIACAAyADAAMAAzAC4AcABkAGYADwAIAAMAaABzAHIAEgA8VXNlcnMvYXRvbWljcGlyYXRlL0RvY3VtZW50cy9DYWx0ZWNoL0FydGljbGVzL01leWVyLzIwMDMucGRmABMAAS8AABUAAgAT//8AANIeHyAhWCRjbGFzc2VzWiRjbGFzc25hbWWjISIjXU5TTXV0YWJsZURhdGFWTlNEYXRhWE5TT2JqZWN0XxAjLi4vLi4vLi4vLi4vQXJ0aWNsZXMvTWV5ZXIvMjAwMy5wZGbSHh8mJ6InI1xOU0RpY3Rpb25hcnkACAARABoAHwApADIANwA6AD8AQQBTAFwAYgBpAHAAeACDAIUAiACKAIwAjwCRAJMAnQCqAK8AtwC5AkcCTAJVAmACZAJyAnkCggKoAq0CsAAAAAAAAAIBAAAAAAAAACgAAAAAAAAAAAAAAAAAAAK9}} @article{elbaum:4078, Author = {Michael Elbaum and Deborah Kuchnir Fygenson and Albert Libchaber}, Date-Modified = {2005-03-17 08:06:41 -0800}, Journal = {Physical Review Letters}, Keywords = {VESICLES; BUCKLING; MICROTUBULES; TENSION; MEMBRANES; SHAPE}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Elbaum/1996.pdf}, Number = {21}, Pages = {4078-4081}, Publisher = {APS}, Title = {Buckling microtubules in vesicles}, Url = {http://link.aps.org/abstract/PRL/v76/p4078}, Volume = {76}, Year = {1996}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://link.aps.org/abstract/PRL/v76/p4078}} @article{Miao:1994ch, Author = {Miao, L and Seifert, U and Wortis, M and Dobereiner, H G}, Da = {19990210}, Date-Modified = {2008-05-29 16:58:47 -0700}, Edat = {1999/02/19}, Journal = {Phys Rev E}, Language = {ENG}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Miao/1994.pdf}, Mhda = {1999/02/19}, Number = {6}, Own = {NLM}, Pages = {5389-5407}, Pmid = {9961866}, Pst = {ppublish}, Pt = {JOURNAL ARTICLE}, Pubm = {Print}, Stat = {Publisher}, Title = {Budding transitions of fluid-bilayer vesicles: The effect of area-difference elasticity}, Volume = {49}, Year = {1994}, Bdsk-File-1 = {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}} @article{Evans, Author = {Evans, E A}, Date-Modified = {2008-05-30 00:34:59 -0700}, Journal = {Biophys J}, Pages = {923--931}, Title = {Bending Resistance and Chemically Induced Moments In Membrane Bilayers}, Volume = {14}, Year = {1974}} @article{fygenson:4497, Author = {Fygenson, D K and Marko, J F and Libchaber, A}, Date-Modified = {2008-05-29 16:57:05 -0700}, Journal = {Phys Rev Lett}, Keywords = {membranes; lipid bilayers; deformation; polymerisation; buckling; fluctuations}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Fygenson/1997.pdf}, Number = {22}, Pages = {4497--4500}, Publisher = {APS}, Title = {Mechanics of Microtubule-Based Membrane Extension}, Volume = {79}, Year = {1997}, Bdsk-File-1 = {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}, Bdsk-Url-1 = {http://link.aps.org/abstract/PRL/v79/p4497}} @article{Heinrich:1999rm, Abstract = {A sufficiently large force acting on a single point of the fluid membrane of a flaccid phospholipid vesicle is known to cause the formation of a narrow bilayer tube (tether). We analyze this phenomenon by means of general mathematical methods allowing us to determine the shapes of strongly deformed vesicles including their stability. Starting from a free vesicle with an axisymmetric, prolate equilibrium shape, we consider an axial load that pulls (or pushes) the poles of the vesicle apart. Arranging the resulting shapes of strained vesicles in dependence of the axial deformation and of the area difference of monolayers, phase diagrams of stable shapes are presented comprising prolate shapes with or without equatorial mirror symmetry. For realistic values of membrane parameters, we study the force-extension relation of strained vesicles, and we demonstrate in detail how the initially elongated shape of an axially stretched vesicle transforms into a shape involving a membrane tether. This tethering transition may be continuous or discontinuous. If the free vesicle is mirror symmetric, the mirror symmetry is broken as the tether forms. The stability analysis of tethered shapes reveals that, for the considered vesicles, the stable shape is always asymmetric (polar), i.e., it involves only a single tether on one side of the main vesicle body. Although a bilayer tube formed from a closed vesicle is not an ideal cylinder, we show that, for most practical purposes, it is safe to assume a cylindrical geometry of tethers. This analysis is supplemented by the documentation of a prototype experiment supporting our theoretical predictions. It shows that the currently accepted model for the description of lipid-bilayer elasticity (generalized bilayer couple model) properly accounts for the tethering phenomenon.}, Affiliation = {Institute of Biophysics, Medical Faculty, Lipiceva 2, University of Ljubljana, Slovenia.}, Au = {Zeks B}, Author = {Heinrich, V and Bo\v{z}i\v{c}, B and Svetina, S and \v{Z}ek\v{s}, B}, Da = {19990507}, Date-Modified = {2008-05-29 17:28:53 -0700}, Dcom = {19990507}, Edat = {1999/03/30}, Jid = {0370626}, Journal = {Biophys J}, Keywords = {Biophysics and Elasticity and Lipid Bilayers/chemistry and Liposomes/*chemistry and Membrane Fluidity and Microscopy, Video and Models, Chemical and Phospholipids/chemistry and Research Support, Non-U.S. Gov't and Thermodynamics}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Heinrich/1999.pdf}, Lr = {20041117}, Mhda = {1999/03/30 00:01}, Number = {4}, Own = {NLM}, Pages = {2056--2071}, Pl = {UNITED STATES}, Pmid = {10096901}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print}, Rn = {0 (Phospholipids)}, Sb = {IM}, Stat = {MEDLINE}, Title = {Vesicle deformation by an axial load: from elongated shapes to tethered vesicles}, Volume = {76}, Year = {1999}, Bdsk-File-1 = {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}} @article{Helfrich:1973lr, Au = {Helfrich W}, Author = {Helfrich, W}, Da = {19740502}, Date-Modified = {2008-05-29 16:43:21 -0700}, Dcom = {19740502}, Edat = {1973/11/01}, Jid = {7801145}, Journal = {Z Naturforsch}, Keywords = {*Elasticity and *Lipids and Magnetics and Mathematics and *Membranes, Artificial}, Language = {eng}, Local-Url = {file://localhost/Users/atomicpirate/Documents/Caltech/Articles/Helfrich/1973.pdf}, Lr = {20001218}, Mhda = {1973/11/01 00:01}, Number = {11}, Own = {NLM}, Pages = {693--703}, Pl = {GERMANY, WEST}, Pmid = {4273690}, Pst = {ppublish}, Pt = {Journal Article}, Pubm = {Print}, Rn = {0 (Lipids)}, Sb = {IM}, Stat = {MEDLINE}, Title = {Elastic properties of lipid bilayers: theory and possible experiments}, Volume = {28}, Year = {1973}, Bdsk-File-1 = {YnBsaXN0MDDUAQIDBAUGCQpYJHZlcnNpb25UJHRvcFkkYXJjaGl2ZXJYJG9iamVjdHMSAAGGoNEHCFRyb290gAFfEA9OU0tleWVkQXJjaGl2ZXKoCwwXGBkdJCVVJG51bGzTDQ4PEBEUViRjbGFzc1dOUy5rZXlzWk5TLm9iamVjdHOAB6ISE4ACgAOiFRaABIAGWWFsaWFzRGF0YVxyZWxhdGl2ZVBhdGjSDRobHFdOUy5kYXRhgAVPEQGUAAAAAAGUAAIAAANoc3IAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAADBcRzJSCsAAABGbGIIMTk3My5wZGYAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAnLRbyFA0IAAAAAAAAAAAAEAAMAAAkgAAAAAAAAAAAAAAAAAAAACEhlbGZyaWNoABAACAAAwXGNSQAAABEACAAAvIVzwgAAAAEAGABGbGIARmvPAEZq1QBGahsARmRoAECJQwACAENoc3I6VXNlcnM6YXRvbWljcGlyYXRlOkRvY3VtZW50czpDYWx0ZWNoOkFydGljbGVzOkhlbGZyaWNoOjE5NzMucGRmAAAOABIACAAxADkANwAzAC4AcABkAGYADwAIAAMAaABzAHIAEgA/VXNlcnMvYXRvbWljcGlyYXRlL0RvY3VtZW50cy9DYWx0ZWNoL0FydGljbGVzL0hlbGZyaWNoLzE5NzMucGRmAAATAAEvAAAVAAIAE///AADSHh8gIVgkY2xhc3Nlc1okY2xhc3NuYW1loyEiI11OU011dGFibGVEYXRhVk5TRGF0YVhOU09iamVjdF8QJi4uLy4uLy4uLy4uL0FydGljbGVzL0hlbGZyaWNoLzE5NzMucGRm0h4fJieiJyNcTlNEaWN0aW9uYXJ5AAgAEQAaAB8AKQAyADcAOgA/AEEAUwBcAGIAaQBwAHgAgwCFAIgAigCMAI8AkQCTAJ0AqgCvALcAuQJRAlYCXwJqAm4CfAKDAowCtQK6Ar0AAAAAAAACAQAAAAAAAAAoAAAAAAAAAAAAAAAAAAACyg==}}