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1
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0015514472
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The fluid mosaic model of the structure of cell membranes
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Thompson TE, Sankaram MB, Biltonen RL, Marsh D, Vaz WCL. Effects of domain structure on in-plane reactions and interactions. Mol Membr Biol. 12:1995;157-162.
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0029738420
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Fluorescence-quenching study of percolation and compartmentalization in two-phase lipid bilayers
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of special interest. An elegant experimental demonstration of the way changes in membrane domains can alter percolation thresholds and hence the rates of collision of mobile molecules in membranes.
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Piknova B, Marsh D, Thompson TE. Fluorescence-quenching study of percolation and compartmentalization in two-phase lipid bilayers. of special interest Biophys J. 71:1996;892-897 An elegant experimental demonstration of the way changes in membrane domains can alter percolation thresholds and hence the rates of collision of mobile molecules in membranes.
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Biophys J
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Piknova, B.1
Marsh, D.2
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Mechanisms of cell polarity: Sorting and transport in epithelial cells
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Matter K, Mellman I. Mechanisms of cell polarity: sorting and transport in epithelial cells. Curr Opin Cell Biol. 6:1994;545-554.
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Curr Opin Cell Biol
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Matter, K.1
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Edidin M. Getting there is only half the fun. Curr Top Membr. 43:1996;1-13.
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Edidin, M.1
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0029005840
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Revisiting the fluid mosaic model of membranes
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Jacobson K, Sheets ED, Simson R. Revisiting the fluid mosaic model of membranes. Science. 268:1995;1441-1442.
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Jacobson, K.1
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Lipid domains in biological membranes
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Glaser M. Lipid domains in biological membranes. Curr Opin Struct Biol. 3:1993;475-481.
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Glaser, M.1
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0028102173
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Lipid domains and lipid - protein interactions in biological membranes
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Tocanne J-F, Cezanne L, Lopez A, Piknova B, Schram V, Tournier J-F, Welby M. Lipid domains and lipid - protein interactions in biological membranes. Chem Phys Lipids. 73:1994;139-158.
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Tocanne, J.-F.1
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Schram, V.5
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Welby, M.7
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Lipid domains in model and biological membranes
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Welti R, Glaser M. Lipid domains in model and biological membranes. Chem Phys Lipids. 73:1994;121-137.
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Chem Phys Lipids
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Welti, R.1
Glaser, M.2
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13
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0029205482
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The cows or the fence?
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Parsegian VA. The cows or the fence? Mol Membr Biol. 12:1995;5-7.
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Parsegian, V.A.1
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Slow nonequilibrium dynamical rearrangement of the lateral structure of a lipid membrane
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Jørgensen K, Klinger K, Braiman M, Biltonen RL. Slow nonequilibrium dynamical rearrangement of the lateral structure of a lipid membrane. J Phys Chem. 100:1996;2766-2769.
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Jørgensen, K.1
Klinger, K.2
Braiman, M.3
Biltonen, R.L.4
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15
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0029946890
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Constrained diffusion or immobile fraction on cell surfaces: A new interpretation
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of outstanding interest. A new approach to FPR data that assumes that the actual mobile fraction of labeled molecules is 100% and that the apparent lower mobile fraction is due to anomalous, spatially restricted, D. The model for these experiments is one in which the membrane is considered as a random array of continuously changing potential energy traps. The range of binding energies of, and escape rates from, the traps is so broad that there is no average binding or residence time - the traps occur on all temporal and spatial scales.
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Feder T, Brust-Mascher I, Slattery JP, Baird B, Webb WW. Constrained diffusion or immobile fraction on cell surfaces: a new interpretation. of outstanding interest Biophys J. 70:1996;2767-2773 A new approach to FPR data that assumes that the actual mobile fraction of labeled molecules is 100% and that the apparent lower mobile fraction is due to anomalous, spatially restricted, D. The model for these experiments is one in which the membrane is considered as a random array of continuously changing potential energy traps. The range of binding energies of, and escape rates from, the traps is so broad that there is no average binding or residence time - the traps occur on all temporal and spatial scales.
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(1996)
Biophys J
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Feder, T.1
Brust-Mascher, I.2
Slattery, J.P.3
Baird, B.4
Webb, W.W.5
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16
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0001811532
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Lipid domains: The parable of the blind men and the elephant
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Wolf DE. Lipid domains: the parable of the blind men and the elephant. Comm Mol Cell Biophys. 8:1992;83-95.
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Comm Mol Cell Biophys
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Wolf, D.E.1
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0027567883
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Lipid phases in renal brush border membranes revealed by laurdan fluorescence
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Levi M, Wilson PV, Cooper OJ, Gratton E. Lipid phases in renal brush border membranes revealed by laurdan fluorescence. Photochem Photobiol. 57:1993;420-425.
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Levi, M.1
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Gratton, E.4
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18
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0031049676
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Evidence for phospholipid microdomain formation in liquid crystalline liposomes reconstituted with Escherichia coli lactose permease
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of outstanding interest. An example of the way in which fluid lipid domains can segregate from bulk membrane lipids due to hydrophobic mismatch of protein transmembrane regions and the average thickness of the lipid bilayer.
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Lehtonen JYA, Kinnunen PKJ. Evidence for phospholipid microdomain formation in liquid crystalline liposomes reconstituted with Escherichia coli lactose permease. of outstanding interest Biophys J. 72:1997;1247-1257 An example of the way in which fluid lipid domains can segregate from bulk membrane lipids due to hydrophobic mismatch of protein transmembrane regions and the average thickness of the lipid bilayer.
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Biophys J
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Lehtonen, J.Y.A.1
Kinnunen, P.K.J.2
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19
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0028363363
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Reorganization of lipid domain structure in membranes by a transmembrane peptide: An ESR spin label study on the effect of the Escherichia coli outer membrane protein A signal peptide on the fluid lipid domain connectivity in binary mixtures of dimyristoyl phosphatidylcholine and distearoyl phosphatidylcholine
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Sankaram MB, Marsh D, Gierasch LM, Thompson TE. Reorganization of lipid domain structure in membranes by a transmembrane peptide: an ESR spin label study on the effect of the Escherichia coli outer membrane protein A signal peptide on the fluid lipid domain connectivity in binary mixtures of dimyristoyl phosphatidylcholine and distearoyl phosphatidylcholine. Biophys J. 66:1994;1959-1968.
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Sankaram, M.B.1
Marsh, D.2
Gierasch, L.M.3
Thompson, T.E.4
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20
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0030978356
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Fluorescence quenching and ESR study of percolation in a two-phase lipid bilayer containing bacteriorhodopsin
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of special interest labeled lipids. These results are consistent with increases in the size of fluid phase domains in the presence of bacteriorhodopsin but are also consistent with changes in the shape of the domains towards uniform circular profiles. This paper concludes with some interesting speculations on the relationship between partitioning of membrane proteins into gel or fluid phases, the interphase and the size and shape of lipid microdomains
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Piknova B, Marsh D, Thompson TE. Fluorescence quenching and ESR study of percolation in a two-phase lipid bilayer containing bacteriorhodopsin. of special interest Biophys J. 1997; Although incorporation of up to 1 mol% bacteriorhodopsin in fluid/gel bilayers has little or no effect on the phase diagram of the system, it affects the topology of fluid domains, as probed by lateral diffusion of fluorescent or spin-labeled lipids. These results are consistent with increases in the size of fluid phase domains in the presence of bacteriorhodopsin but are also consistent with changes in the shape of the domains towards uniform circular profiles. This paper concludes with some interesting speculations on the relationship between partitioning of membrane proteins into gel or fluid phases, the interphase and the size and shape of lipid microdomains.
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(1997)
Biophys J
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Piknova, B.1
Marsh, D.2
Thompson, T.E.3
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21
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0030933012
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Influence of the intrinsic membrane protein bacteriorhodopsin on the gel phase domain topology in two-component phase-separated bilayers
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of special interest
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Schramm V, Thompson TE. Influence of the intrinsic membrane protein bacteriorhodopsin on the gel phase domain topology in two-component phase-separated bilayers. of special interest Biophys J. 1997; The complement to [20]. The topology of the gel domains is probed in terms of the lateral diffusion of labeled lipids and proteins measured using fluorescence photobleaching recovery.
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(1997)
Biophys J
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Schramm, V.1
Thompson, T.E.2
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22
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0029987046
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The spatial distribution of phospholipids and glycolipids in the membrane of the bacterium Micrococcus luteus varies during the cell cycle
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Welby M, Poquet Y, Tocanne J-F. The spatial distribution of phospholipids and glycolipids in the membrane of the bacterium Micrococcus luteus varies during the cell cycle. FEBS Lett. 384:1996;107-111.
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FEBS Lett
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Welby, M.1
Poquet, Y.2
Tocanne, J.-F.3
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23
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0029792683
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Lipid lateral heterogeneity in phosphatidylcholine/phosphatidylserine/diacylglycerol vesicles and its influence on protein kinase C activation
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of special interest. PKC activation requires coexisting DAG-rich and DAG-poor domains. The authors suggest that DAG-rich domains can form locally (and transiently) as a consequence of phosphatidylinositol-specific phospholipase C activity.
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Dibbie ARG, Hinderliter AK, Sando JJ, Biltonen RL. Lipid lateral heterogeneity in phosphatidylcholine/phosphatidylserine/diacylglycerol vesicles and its influence on protein kinase C activation. of special interest Biophys J. 71:1996;1877-1890 PKC activation requires coexisting DAG-rich and DAG-poor domains. The authors suggest that DAG-rich domains can form locally (and transiently) as a consequence of phosphatidylinositol-specific phospholipase C activity.
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(1996)
Biophys J
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, pp. 1877-1890
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Dibbie, A.R.G.1
Hinderliter, A.K.2
Sando, J.J.3
Biltonen, R.L.4
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24
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0029194217
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Are acidic lipid domains induced by extrinsic protein binding to membranes?
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Lentz BR. Are acidic lipid domains induced by extrinsic protein binding to membranes? Mol Membr Biol. 12:1995;65-67.
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Mol Membr Biol
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Lentz, B.R.1
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25
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0029182774
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Does the binding of clusters of basic residues to acidic lipids induce domain formation in membranes?
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Buser CA, Kim J, McLaughlin S, Peitzsch RM. Does the binding of clusters of basic residues to acidic lipids induce domain formation in membranes? Mol Membr Biol. 12:1995;69-75.
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Mol Membr Biol
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Buser, C.A.1
Kim, J.2
McLaughlin, S.3
Peitzsch, R.M.4
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26
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10244224044
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Myristoylated alanine-rich C kinase substrate (MARCKS) produces reversible inhibition of phospholipase C by sequestering phosphatidylinositol 4,5-bisphosphate in lateral domains
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Glaser M, Wanaski S, Buser CA, Boguslavsky V, Rashidzada W, Morris A, Rebecchi M, Scarlata SF, Runnels LW, Prestwich GD, et al. Myristoylated alanine-rich C kinase substrate (MARCKS) produces reversible inhibition of phospholipase C by sequestering phosphatidylinositol 4,5-bisphosphate in lateral domains. J Biol Chem. 272:1996;26187-26193.
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Glaser, M.1
Wanaski, S.2
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Boguslavsky, V.4
Rashidzada, W.5
Morris, A.6
Rebecchi, M.7
Scarlata, S.F.8
Runnels, L.W.9
Prestwich, G.D.10
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27
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0029080687
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Formation of membrane domains created during the budding of vesicular stomatitis virus. A model for selective lipid and protein sorting in biological membranes
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Luan P, Yang L, Glaser M. Formation of membrane domains created during the budding of vesicular stomatitis virus. A model for selective lipid and protein sorting in biological membranes. Biochemistry. 34:1995;9874-9883.
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Biochemistry
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Luan, P.1
Yang, L.2
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28
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0031041581
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Compartmentalized activation of the high affinity IgE receptor within membrane domains
-
of special interest. Within minutes of cross-linking, the bulk of the IgE receptor shifts from dense sucrose gradient fractions to floating fractions usually associated with GPI-proteins and detergent-insoluble lipids; the fractions are enriched in tyrosine kinases. The shift appears to be required for signaling from the receptor. The biochemical changes described expand on earlier work from this group showing that cross-linking the IgE receptor results in association of a fluorescent phospholipid analog with the receptor aggregates [44].
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Field KA, Holowka D, Baird B. Compartmentalized activation of the high affinity IgE receptor within membrane domains. of special interest J Biol Chem. 272:1997;4276-4280 Within minutes of cross-linking, the bulk of the IgE receptor shifts from dense sucrose gradient fractions to floating fractions usually associated with GPI-proteins and detergent-insoluble lipids; the fractions are enriched in tyrosine kinases. The shift appears to be required for signaling from the receptor. The biochemical changes described expand on earlier work from this group showing that cross-linking the IgE receptor results in association of a fluorescent phospholipid analog with the receptor aggregates [44].
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(1997)
J Biol Chem
, vol.272
, pp. 4276-4280
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Field, K.A.1
Holowka, D.2
Baird, B.3
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29
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0031031052
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Cellular and molecular mechanics by atomic force microscopy: Capturing the exocytotic fusion pore in vivo
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Fernandez JM. Cellular and molecular mechanics by atomic force microscopy: capturing the exocytotic fusion pore in vivo. Proc Natl Acad Sci USA. 94:1997;9-10.
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Proc Natl Acad Sci USA
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Fernandez, J.M.1
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30
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0031036751
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Changes in the spectral properties of a plasma membrane lipid analog during the first seconds of endocytosis in living cells
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of special interest. A remarkable paper using changes in the spectral properties of a fluorescent lipid analog to detect the first seven seconds in the life of a newly formed membrane domain - an endocytic vesicle budding from the plasma membrane.
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Chen C-S, Martin OC, Pagano RE. Changes in the spectral properties of a plasma membrane lipid analog during the first seconds of endocytosis in living cells. of special interest Biophys J. 72:1997;37-50 A remarkable paper using changes in the spectral properties of a fluorescent lipid analog to detect the first seven seconds in the life of a newly formed membrane domain - an endocytic vesicle budding from the plasma membrane.
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(1997)
Biophys J
, vol.72
, pp. 37-50
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Chen, C.-S.1
Martin, O.C.2
Pagano, R.E.3
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31
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0030222108
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Caveolae and caveolins
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of special interest. A recent review on all aspects of caveloae, including a good section speculating on the biogenesis of caveolae and a review of caveolin isoforms.
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Parton RG. Caveolae and caveolins. of special interest Curr Opin Cell Biol. 8:1996;542-548 A recent review on all aspects of caveloae, including a good section speculating on the biogenesis of caveolae and a review of caveolin isoforms.
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(1996)
Curr Opin Cell Biol
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Parton, R.G.1
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32
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0026512314
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Corting of GPI-anchored proteins to glycolipid enriched membrane subdomains during transport to the apical cell surface
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Brown DA, Rose JKS. Corting of GPI-anchored proteins to glycolipid enriched membrane subdomains during transport to the apical cell surface. Cell. 68:1992;533-544.
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Cell
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Brown, D.A.1
Rose, J.K.S.2
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0029082412
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Separation of caveolae from associated microdomains of GPI-anchored proteins
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Schnitzer JE, McIntosh DP, Dvorak AM, Liu J, Oh P. Separation of caveolae from associated microdomains of GPI-anchored proteins. Science. 269:1995;1435-1439.
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Science
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Schnitzer, J.E.1
McIntosh, D.P.2
Dvorak, A.M.3
Liu, J.4
Oh, P.5
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34
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0029757511
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GPI-anchored proteins, glycosphingolipids and sphingomyelin are sequestered to caveolae only after crosslinking
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Fujimoto T. GPI-anchored proteins, glycosphingolipids and sphingomyelin are sequestered to caveolae only after crosslinking. J Histochem Cytochem. 44:1996;929-941.
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J Histochem Cytochem
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Fujimoto, T.1
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35
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Insolubility and redistribution of GPI-anchored proteins at the cell surface after detergent treatment
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Mayor S, Maxfield FR. Insolubility and redistribution of GPI-anchored proteins at the cell surface after detergent treatment. Mol Biol Cell. 6:1995;929-944.
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Mol Biol Cell
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Mayor, S.1
Maxfield, F.R.2
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36
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0028151351
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Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior
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Schroeder R, London E, Brown D. Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior. Proc Natl Acad Sci USA. 91:1994;12130-12134.
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Schroeder, R.1
London, E.2
Brown, D.3
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37
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0030071622
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Membrane organization at low cholesterol concentrations: A study using 7-nitrobenz-2-oxa-1,3-diazol-4-yl-labeled cholesterol
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Mukherjee S, Chattopadhyay A. Membrane organization at low cholesterol concentrations: a study using 7-nitrobenz-2-oxa-1,3-diazol-4-yl-labeled cholesterol. Biochemistry. 35:1996;1311-1322.
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Biochemistry
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Mukherjee, S.1
Chattopadhyay, A.2
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38
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0029799891
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A role for caveolin in transport of cholesterol from endoplasmic reticulum to plasma membrane
-
of special interest. These experiments depend upon the isolation of a caveolar fraction, defined as a fraction that floats on a density gradient. Surprisingly, the same fraction can be isolated from L-1210 lymphoblasts which lack caveolin and morphological caveolae. Indeed, the same amount of protein is found in the 'caveolar fraction' of L-1210 as in the same fraction from L-1210 cells transfected with the caveolin I gene.
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Smart EJ, Ying Y-S, Donzell WC, Anderson RWG. A role for caveolin in transport of cholesterol from endoplasmic reticulum to plasma membrane. of special interest J Biol Chem. 271:1996;29427-29435 These experiments depend upon the isolation of a caveolar fraction, defined as a fraction that floats on a density gradient. Surprisingly, the same fraction can be isolated from L-1210 lymphoblasts which lack caveolin and morphological caveolae. Indeed, the same amount of protein is found in the 'caveolar fraction' of L-1210 as in the same fraction from L-1210 cells transfected with the caveolin I gene.
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J Biol Chem
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Smart, E.J.1
Ying, Y.-S.2
Donzell, W.C.3
Anderson, R.W.G.4
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39
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0030956033
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Single-particle tracking: Applications to membrane dynamics
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in press
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Saxton MJ, Jacobson K. Single-particle tracking: applications to membrane dynamics. in press Annu Rev Biophys Biomol Struct. 26:1997.
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Annu Rev Biophys Biomol Struct
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Saxton, M.J.1
Jacobson, K.2
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Detection of temporary lateral confinement of membrane proteins using single-particle tracking analysis
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Simson R, Sheets ED, Jacobson K. Detection of temporary lateral confinement of membrane proteins using single-particle tracking analysis. Biophys J. 69:1995;989-993.
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Simson, R.1
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Jacobson, K.3
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41
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0029981248
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Imaging of single molecule diffusion
-
of special interest. A methodology is presented for visualizing the motion of single fluorescent molecules. It is used to image the lateral diffusion of labeled phospholipids in a single membrane. Although the positional accuracy claimed is only 30 nm, the method has great potential for detecting microdomains in cell membranes in terms of the transient confinement of labeled molecules.
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Schmidt T, Schutz GJ, Baumgartner W, Gruber HJ, Schindler H. Imaging of single molecule diffusion. of special interest Proc Natl Acad Sci USA. 93:1996;2926-2929 A methodology is presented for visualizing the motion of single fluorescent molecules. It is used to image the lateral diffusion of labeled phospholipids in a single membrane. Although the positional accuracy claimed is only 30 nm, the method has great potential for detecting microdomains in cell membranes in terms of the transient confinement of labeled molecules.
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Proc Natl Acad Sci USA
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Schmidt, T.1
Schutz, G.J.2
Baumgartner, W.3
Gruber, H.J.4
Schindler, H.5
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Florescence correlation spectroscopy with high count rate and low background: Analysis of translational diffusion
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Rigler R, Mets Ü, Widengre J, Kask P. Florescence correlation spectroscopy with high count rate and low background: analysis of translational diffusion. Eur Biophys J. 22:1993;169-175.
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Rigler, R.1
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Widengre, J.3
Kask, P.4
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43
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0028806195
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Nanoscale complexity of phospholipid monolayers investigated by near-field scanning optical microscopy
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Hwang J, Tamm LK, Bohm C, Ramalingam TS, Betzig E, Edidin M. Nanoscale complexity of phospholipid monolayers investigated by near-field scanning optical microscopy. Science. 270:1995;610-614.
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Ramalingam, T.S.4
Betzig, E.5
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44
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Large-scale coaggregation of fluorescent lipid probes with cell surface proteins
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Thomas JL, Holowka D, Baird B, Webb WW. Large-scale coaggregation of fluorescent lipid probes with cell surface proteins. J Cell Biol. 125:1994;795-802.
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