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Volumn 1838, Issue 6, 2014, Pages 1451-1466

The Fluid - Mosaic Model of Membrane Structure: Still relevant to understanding the structure, function and dynamics of biological membranes after more than 40 years

Author keywords

Membrane domains; Membrane dynamics; Membrane lipids; Membrane model; Membrane proteins; Membrane thermodynamics

Indexed keywords

MEMBRANE DOMAINS; MEMBRANE DYNAMICS; MEMBRANE LIPIDS; MEMBRANE MODEL; MEMBRANE PROTEINS; MEMBRANE THERMODYNAMICS;

EID: 84899444997     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2013.10.019     Document Type: Review
Times cited : (504)

References (248)
  • 1
    • 0015514472 scopus 로고
    • The Fluid Mosaic Model of the structure of cell membranes
    • S.J. Singer, and G.L. Nicolson The Fluid Mosaic Model of the structure of cell membranes Science 175 1972 720 731
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 2
    • 70449246410 scopus 로고
    • The ultrastructure of cell membranes and their derivatives
    • J.D. Robertson The ultrastructure of cell membranes and their derivatives Biochem. Soc. Symp. 16 1959 3 43
    • (1959) Biochem. Soc. Symp. , vol.16 , pp. 3-43
    • Robertson, J.D.1
  • 3
    • 0008394796 scopus 로고
    • The molecular structure and contact relationships of cell membranes
    • J.D. Robertson The molecular structure and contact relationships of cell membranes Prog. Biophys. Biophys. Chem. 10 1960 343 418
    • (1960) Prog. Biophys. Biophys. Chem. , vol.10 , pp. 343-418
    • Robertson, J.D.1
  • 5
    • 0000954302 scopus 로고
    • A contribution to the theory of permeability of thin films
    • J.F. Danielli, and H. Davson A contribution to the theory of permeability of thin films J. Cell. Comp. Physiol. 5 1935 495 508
    • (1935) J. Cell. Comp. Physiol. , vol.5 , pp. 495-508
    • Danielli, J.F.1    Davson, H.2
  • 6
    • 0343800636 scopus 로고
    • On bimolecular layers of lipoids on the chromocytes of the blood
    • E. Gorter, and F. Grendel On bimolecular layers of lipoids on the chromocytes of the blood J. Exp. Med. 41 1925 439 443
    • (1925) J. Exp. Med. , vol.41 , pp. 439-443
    • Gorter, E.1    Grendel, F.2
  • 7
    • 0014804933 scopus 로고
    • Membrane splitting in freeze-etching. Covalently bound ferritin as a membrane marker
    • P. Pinto da Silva, and D. Branton Membrane splitting in freeze-etching. Covalently bound ferritin as a membrane marker J. Cell Biol. 45 1970 598 605
    • (1970) J. Cell Biol. , vol.45 , pp. 598-605
    • Pinto Da Silva, P.1    Branton, D.2
  • 8
    • 0014572123 scopus 로고
    • Current models for the structure of biological membranes
    • W. Stoeckenius, and D.M. Engelman Current models for the structure of biological membranes J. Cell Biol. 42 1969 613 646
    • (1969) J. Cell Biol. , vol.42 , pp. 613-646
    • Stoeckenius, W.1    Engelman, D.M.2
  • 9
    • 0013912955 scopus 로고
    • On the orientation of lipids in chloroplast and cell membranes
    • A.A. Benson On the orientation of lipids in chloroplast and cell membranes J. Am. Oil Chem. Soc. 43 1966 265 270
    • (1966) J. Am. Oil Chem. Soc. , vol.43 , pp. 265-270
    • Benson, A.A.1
  • 11
    • 0015474668 scopus 로고
    • Lipid bilayers and biomembranes
    • A.D. Bangham Lipid bilayers and biomembranes Annu. Rev. Biochem. 41 1972 753 776
    • (1972) Annu. Rev. Biochem. , vol.41 , pp. 753-776
    • Bangham, A.D.1
  • 12
    • 0015876764 scopus 로고
    • Membrane structure: Some general principals
    • M.S. Bretscher Membrane structure: some general principals Science 181 1973 622 829
    • (1973) Science , vol.181 , pp. 622-829
    • Bretscher, M.S.1
  • 13
    • 0014674140 scopus 로고
    • Planar liquid-like arrangement of photopigment molecules in frog retinal receptor disk membranes
    • J.K. Blasie, and C.R. Worthington Planar liquid-like arrangement of photopigment molecules in frog retinal receptor disk membranes J. Mol. Biol. 39 1969 417 439
    • (1969) J. Mol. Biol. , vol.39 , pp. 417-439
    • Blasie, J.K.1    Worthington, C.R.2
  • 14
    • 0016506002 scopus 로고
    • Phase transitions and fluidity characteristics of lipids and cell membranes
    • D. Chapman Phase transitions and fluidity characteristics of lipids and cell membranes Q. Rev. Biophys. 8 1975 185 235
    • (1975) Q. Rev. Biophys. , vol.8 , pp. 185-235
    • Chapman, D.1
  • 15
    • 0018225465 scopus 로고
    • Fluidity parameters of lipid regions determined by fluorescence polarization
    • M. Shinitzky, and Y. Barenholz Fluidity parameters of lipid regions determined by fluorescence polarization Biochim. Biophys. Acta 515 1978 367 394 (Pubitemid 9099585)
    • (1978) Biochimica et Biophysica Acta , vol.515 , Issue.4 , pp. 367-394
    • Shinitzky, M.1    Barenholz, Y.2
  • 17
    • 0038557037 scopus 로고    scopus 로고
    • Lipids on the frontier: A century of cell-membrane bilayers
    • DOI 10.1038/nrm1102
    • M. Edidin Lipids on the frontier: a quarter century of cell-membrane bilayers Nat. Rev. Mol. Cell Biol. 4 2003 414 418 (Pubitemid 36565573)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.5 , pp. 414-418
    • Edidin, M.1
  • 20
    • 84864705022 scopus 로고    scopus 로고
    • Resolving the kinetics of lipid, protein and peptide diffusion in membranes
    • J.M. Sanderson Resolving the kinetics of lipid, protein and peptide diffusion in membranes Mol. Membr. Biol. 29 2012 118 143
    • (2012) Mol. Membr. Biol. , vol.29 , pp. 118-143
    • Sanderson, J.M.1
  • 21
    • 77954763297 scopus 로고    scopus 로고
    • Lipid diffusion in planar membranes investigated by fluorescence correlation spectroscopy
    • R. Machán, and M. Hof Lipid diffusion in planar membranes investigated by fluorescence correlation spectroscopy Biochim. Biophys. Acta 1798 2010 1377 1391
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1377-1391
    • Machán, R.1    Hof, M.2
  • 22
    • 58149185333 scopus 로고    scopus 로고
    • Lipid lateral diffusion and membrane heterogeneity
    • G. Lindblom, and G. Orädd Lipid lateral diffusion and membrane heterogeneity Biochim. Biophys. Acta 1788 2009 234 244
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 234-244
    • Lindblom, G.1    Orädd, G.2
  • 24
    • 0004938386 scopus 로고
    • Protein conformation in cell membrane preparations as studied by optical rotatory dispersion and circular dichroism
    • J. Lenard, and S.J. Singer Protein conformation in cell membrane preparations as studied by optical rotatory dispersion and circular dichroism Proc. Natl. Acad. Sci. U. S. A. 56 1966 1828 1835
    • (1966) Proc. Natl. Acad. Sci. U. S. A. , vol.56 , pp. 1828-1835
    • Lenard, J.1    Singer, S.J.2
  • 25
    • 0018118306 scopus 로고
    • Structures of membrane proteins
    • S.J. Kennedy Structures of membrane proteins J. Membr. Biol. 42 1978 265 279 (Pubitemid 9044382)
    • (1978) Journal of Membrane Biology , vol.42 , Issue.3 , pp. 265-279
    • Kennedy, S.J.1
  • 26
    • 0023943214 scopus 로고
    • Lipid fluidity directly modulates the overall protein rotational motility of the Ca-ATPase in sarcoplasmic reticulum
    • T.C. Squier, D.J. Bigelow, and D.D. Thomas Lipid fluidity directly modulates the overall protein rotational motility of the Ca-ATPase in sarcoplasmic reticulum J. Biol. Chem. 263 1988 9178 9186
    • (1988) J. Biol. Chem. , vol.263 , pp. 9178-9186
    • Squier, T.C.1    Bigelow, D.J.2    Thomas, D.D.3
  • 27
    • 0016001009 scopus 로고
    • The molecular organization of membranes
    • S.J. Singer The molecular organization of membranes Annu. Rev. Biochem. 43 1974 805 833
    • (1974) Annu. Rev. Biochem. , vol.43 , pp. 805-833
    • Singer, S.J.1
  • 29
    • 0014840359 scopus 로고
    • The rapid intermixing of cell surface antigens after formation of mouse-human heterokaryons
    • L.D. Frye, and M. Edidin The rapid intermixing of cell surface antigens after formation of mouse-human heterokaryons J. Cell Sci. 7 1970 319 335
    • (1970) J. Cell Sci. , vol.7 , pp. 319-335
    • Frye, L.D.1    Edidin, M.2
  • 30
    • 0017287098 scopus 로고
    • Transmembrane control of the receptors on normal and tumor cells. I. Cytoplasmic influence over cell surface components
    • G.L. Nicolson Transmembrane control of the receptors on normal and tumor cells. I. Cytoplasmic influence over cell surface components Biochim. Biophys. Acta 457 1976 57 108
    • (1976) Biochim. Biophys. Acta , vol.457 , pp. 57-108
    • Nicolson, G.L.1
  • 31
  • 32
    • 0020686156 scopus 로고
    • Lateral motion of membrane proteins and biological function
    • D. Axelrod Lateral motion of membrane proteins and biological function J. Membr. Biol. 75 1983 1 10
    • (1983) J. Membr. Biol. , vol.75 , pp. 1-10
    • Axelrod, D.1
  • 35
    • 0026320864 scopus 로고
    • Lateral movements of membrane glycoproteins restricted by dynamic cytoplasmic barriers
    • M. Edidin, S.C. Kuo, and M.P. Sheetz Lateral movements of membrane glycoproteins restricted by dynamic cytoplasmic barriers Science 254 1991 1379 1382 (Pubitemid 21917474)
    • (1991) Science , vol.254 , Issue.5036 , pp. 1379-1382
    • Edidin, M.1    Kuo, S.C.2    Sheetz, M.P.3
  • 36
    • 0027661274 scopus 로고
    • Protein lateral mobility as a reflection of membrane microstructure
    • F. Zhang, G.M. Lee, and K. Jacobson Protein lateral mobility as a reflection of membrane microstructure Bioessays 15 1993 579 588
    • (1993) Bioessays , vol.15 , pp. 579-588
    • Zhang, F.1    Lee, G.M.2    Jacobson, K.3
  • 37
    • 80855144806 scopus 로고    scopus 로고
    • Toward the fourth dimension of membrane protein structure: Insights into dynamics from spin-labeling EPR spectroscopy
    • H.S. Mchaourab, P.R. Steed, and K. Kazmier Toward the fourth dimension of membrane protein structure: insights into dynamics from spin-labeling EPR spectroscopy Structure 19 2011 1549 1561
    • (2011) Structure , vol.19 , pp. 1549-1561
    • McHaourab, H.S.1    Steed, P.R.2    Kazmier, K.3
  • 39
    • 0024367272 scopus 로고
    • Membrane structure and dynamics
    • A. Watts Membrane structure and dynamics Curr. Opin. Cell Biol. 1 1989 691 700 (Pubitemid 19225786)
    • (1989) Current Opinion in Cell Biology , vol.1 , Issue.4 , pp. 691-700
    • Watts, A.1
  • 40
    • 0033853080 scopus 로고    scopus 로고
    • A century of thinking about cell membranes
    • DOI 10.1146/annurev.physiol.62.1.919
    • P. de Weer A century of thinking about cell membranes Annu. Rev. Physiol. 62 2000 919 926 (Pubitemid 30618287)
    • (2000) Annual Review of Physiology , vol.62 , pp. 919-926
    • De Weer, P.1
  • 41
    • 0017750496 scopus 로고
    • Refinement of the fluid-mosaic model of membrane structure
    • J.N. Israelachvili Refinement of the fluid-mosaic model of membrane structure Biochim. Biophys. Acta 469 1977 221 225 (Pubitemid 8169802)
    • (1977) Biochimica et Biophysica Acta , vol.469 , pp. 221-225
    • Israelachvili, J.N.1
  • 42
    • 1842297533 scopus 로고    scopus 로고
    • Dynamic receptor superstructures at the plasma membrane
    • DOI 10.1017/S0033583596003307
    • S. Damjanovich, R. Gáspár Jr., and C. Pieri Dynamic receptor superstructures at the plasma membrane Q. Rev. Biophys. 30 1997 67 106 (Pubitemid 27190366)
    • (1997) Quarterly Reviews of Biophysics , vol.30 , Issue.1 , pp. 67-106
    • Damjanovich, S.1    Gaspar Jr., R.2    Pieri, C.3
  • 43
    • 0029005840 scopus 로고
    • Revisiting the fluid mosaic model of membranes
    • K. Jacobson, E.D. Sheets, and R. Simson Revisiting the fluid mosaic model of membranes Science 268 1995 1441 1442
    • (1995) Science , vol.268 , pp. 1441-1442
    • Jacobson, K.1    Sheets, E.D.2    Simson, R.3
  • 45
    • 0038298778 scopus 로고    scopus 로고
    • Is a fluid-mosaic model of biological membranes fully relevant? Studies on lipid organization in model and biological membranes
    • A. Winiewska, J. Draus, and W.K. Subczynski Is the fluid-mosaic model of biological membranes fully relevant? Studies on lipid organization in model and biological membranes Cell. Mol. Biol. Lett. 8 2003 147 159 (Pubitemid 36534577)
    • (2003) Cellular and Molecular Biology Letters , vol.8 , Issue.1 , pp. 147-159
    • Wisniewska, A.1    Draus, J.2    Subczynski, W.K.3
  • 46
    • 0026639372 scopus 로고
    • The structure and function of membranes - A personal memoir
    • S.J. Singer The structure and function of membranes - a personal memoir J. Membr. Biol. 129 1992 3 12
    • (1992) J. Membr. Biol. , vol.129 , pp. 3-12
    • Singer, S.J.1
  • 47
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturing
    • W. Kauzmann Some factors in the interpretation of protein denaturing Adv. Protein Chem. 14 1959 1 63
    • (1959) Adv. Protein Chem. , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 48
    • 33750239249 scopus 로고    scopus 로고
    • The physical chemistry of biological membranes
    • DOI 10.1038/nchembio1106-564, PII NCHEMBIO1106564
    • J. Zimmerberg, and K. Gawrisch The physical chemistry of biological membranes Nat. Chem. Biol. 2 2006 564 567 (Pubitemid 44610336)
    • (2006) Nature Chemical Biology , vol.2 , Issue.11 , pp. 564-567
    • Zimmerberg, J.1    Gawrisch, K.2
  • 49
    • 0002657418 scopus 로고
    • The molecular organization of membranes
    • L.I. Rothfield, Academic Press New York
    • S.J. Singer The molecular organization of membranes L.I. Rothfield, Structure and Function of Biological Membranes 1971 Academic Press New York 145 222
    • (1971) Structure and Function of Biological Membranes , pp. 145-222
    • Singer, S.J.1
  • 50
    • 0025224551 scopus 로고
    • The structure and insertion of integral proteins in membranes
    • S.J. Singer The structure and insertion of integral proteins in membranes Annu. Rev. Cell Biol. 6 1990 247 296
    • (1990) Annu. Rev. Cell Biol. , vol.6 , pp. 247-296
    • Singer, S.J.1
  • 51
    • 0023928974 scopus 로고
    • Transcending the impenetrable: How proteins come to terms with membranes
    • G. von Heijne Transcending the impenetrable: how proteins come to terms with membranes Biochim. Biophys. Acta 947 1988 307 333
    • (1988) Biochim. Biophys. Acta , vol.947 , pp. 307-333
    • Von Heijne, G.1
  • 52
    • 0027080146 scopus 로고
    • Forces involved in the assembly and stabilization of membrane proteins
    • W.A. Cramer, D.M. Engelman, G. von Heijne, and D.C. Rees Forces involved in the assembly and stabilization of membrane proteins FASEB J. 6 1992 3397 3402 (Pubitemid 23007105)
    • (1992) FASEB Journal , vol.6 , Issue.15 , pp. 3397-3402
    • Cramer, W.A.1    Engelman, D.M.2    Von Heijne, G.3    Rees, D.C.4
  • 53
    • 33845343261 scopus 로고    scopus 로고
    • Membrane-protein topology
    • DOI 10.1038/nrm2063, PII NRM2063
    • G. von Heijne Membrane-protein topology Nat. Rev. Mol. Cell Biol. 7 2006 909 918 (Pubitemid 44871417)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.12 , pp. 909-918
    • Von Heijne, G.1
  • 56
    • 0018797519 scopus 로고
    • Lipid polymorphism and the functional roles of lipids in biological membranes
    • P.R. Cullis, and B. Kruijff Lipid polymorphism and the functional roles of lipids in biological membranes Biochim. Biophys. Acta 559 1979 399 420
    • (1979) Biochim. Biophys. Acta , vol.559 , pp. 399-420
    • Cullis, P.R.1    Kruijff, B.2
  • 57
    • 0026132695 scopus 로고
    • General features of phospholipids phase transitions
    • D. Marsh General features of phospholipids phase transitions Chem. Phys. Lipids 57 1991 109 120
    • (1991) Chem. Phys. Lipids , vol.57 , pp. 109-120
    • Marsh, D.1
  • 58
    • 0023239664 scopus 로고
    • Lipid intermolecular hydrogen bonding: Influence on structural organization and membrane function
    • J.M. Boggs Lipid intermolecular hydrogen bonding: influence on structural organization and membrane function Biochim. Biophys. Acta 906 1987 353 404 (Pubitemid 17140656)
    • (1987) Biochimica et Biophysica Acta - Reviews on Biomembranes , vol.906 , Issue.3 , pp. 353-404
    • Boggs, J.M.1
  • 59
    • 77956393723 scopus 로고    scopus 로고
    • An outlook on the organization of lipids in membranes: Searching for a realistic connection with the organization of biological membranes
    • L.A. Bagatolli, J.H. Ipsen, A.C. Simonsen, and O.G. Mouritsen An outlook on the organization of lipids in membranes: searching for a realistic connection with the organization of biological membranes Prog. Lipid Res. 49 2010 378 389
    • (2010) Prog. Lipid Res. , vol.49 , pp. 378-389
    • Bagatolli, L.A.1    Ipsen, J.H.2    Simonsen, A.C.3    Mouritsen, O.G.4
  • 60
    • 0032527642 scopus 로고    scopus 로고
    • Structure and origin of ordered lipid domains in biological membranes
    • DOI 10.1007/s002329900397
    • D.A. Brown, and E. London Structure of ordered lipid domains in biological membranes J. Membr. Biol. 164 1998 103 114 (Pubitemid 28336989)
    • (1998) Journal of Membrane Biology , vol.164 , Issue.2 , pp. 103-114
    • Brown, D.A.1    London, E.2
  • 62
    • 40749132024 scopus 로고    scopus 로고
    • Functional role of glycosphingolipids and gangliosides in control of cell adhesion, motility, growth, through glycosynaptic microdomains
    • A.R. Todeschini, and S.I. Hakomori Functional role of glycosphingolipids and gangliosides in control of cell adhesion, motility, growth, through glycosynaptic microdomains Biochim. Biophys. Acta 1780 2008 421 433
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 421-433
    • Todeschini, A.R.1    Hakomori, S.I.2
  • 63
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipid rafts: From model membranes to cells
    • DOI 10.1146/annurev.biophys.32.110601.142439
    • M. Edidin The state of lipid rafts: from model membranes to cells Annu. Rev. Biophys. Biomol. Struct. 32 2003 257 283 (Pubitemid 37056230)
    • (2003) Annual Review of Biophysics and Biomolecular Structure , vol.32 , pp. 257-283
    • Edidin, M.1
  • 64
    • 29144484142 scopus 로고    scopus 로고
    • Partitioning of membrane molecules between raft and non-raft domains: Insights from model-membrane studies
    • DOI 10.1016/j.bbamcr.2005.09.003, PII S0167488905001989, Lipid Refts: From Model Membranes to Cells
    • J.R. Silvius Partitioning of membrane molecules between raft and non-raft domains: insights from model-membrane studies Biochim. Biophys. Acta 1746 2005 193 202 (Pubitemid 41815016)
    • (2005) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1746 , Issue.3 , pp. 193-202
    • Silvius, J.R.1
  • 65
    • 33745801153 scopus 로고    scopus 로고
    • Lipid rafts: Contentious only from simplistic standpoints
    • DOI 10.1038/nrm1925, PII NRM1925
    • J.F. Hancock Lipid rafts: contentious only from simplistic standpoints Nat. Rev. Mol. Cell Biol. 7 2006 456 462 (Pubitemid 44050099)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.6 , pp. 456-462
    • Hancock, J.F.1
  • 66
    • 58149473633 scopus 로고    scopus 로고
    • The liquid-ordered phase in membranes
    • P.J. Quinn, and C. Wolf The liquid-ordered phase in membranes Biochim. Biophys. Acta 1788 2009 33 46
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 33-46
    • Quinn, P.J.1    Wolf, C.2
  • 67
    • 84860448210 scopus 로고    scopus 로고
    • Membrane organization and lipid rafts
    • 10.1101/cshperspect.a004697
    • K. Simons, and J.L. Sampaio Membrane organization and lipid rafts Cold Spring Harb. Perspect. Biol. 3 2010 a004697 10.1101/cshperspect.a004697
    • (2010) Cold Spring Harb. Perspect. Biol. , vol.3 , pp. 004697
    • Simons, K.1    Sampaio, J.L.2
  • 68
    • 84858425043 scopus 로고    scopus 로고
    • Lipid-lipid interactions in bilayer membranes: Married couples and casual liaisons
    • P.J. Quinn Lipid-lipid interactions in bilayer membranes: married couples and casual liaisons Prog. Lipid Res. 31 2012 179 198
    • (2012) Prog. Lipid Res. , vol.31 , pp. 179-198
    • Quinn, P.J.1
  • 69
    • 0021474573 scopus 로고
    • Mattress model of lipid-protein interactions in membranes
    • O.G. Mouritsen, and M. Bloom Mattress model of lipid-protein interactions in membranes Biophys. J. 46 1984 141 153
    • (1984) Biophys. J. , vol.46 , pp. 141-153
    • Mouritsen, O.G.1    Bloom, M.2
  • 70
    • 0029914157 scopus 로고    scopus 로고
    • Measured effects of diacylglycerol on structural and elastic properties of phospholipid membranes
    • S. Leikin, M.M. Kozlov, N.L. Fuller, and R.P. Rand Measured effects of diacylglycerol on structural and elastic properties of phospholipids membranes Biophys. J. 71 1996 2623 2632 (Pubitemid 26367725)
    • (1996) Biophysical Journal , vol.71 , Issue.5 , pp. 2623-2632
    • Leikin, S.1    Kozlov, M.M.2    Fuller, N.L.3    Rand, R.P.4
  • 71
    • 0038290760 scopus 로고    scopus 로고
    • Protein-lipid interplay in fusion and fission of biological membranes
    • DOI 10.1146/annurev.biochem.72.121801.161504
    • L.V. Chernomordik, and M.M. Kozlov Protein-lipid interplay in fusion and fission of biological membranes Annu. Rev. Biochem. 72 2003 175 207 (Pubitemid 36930445)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 175-207
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 72
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • DOI 10.1038/nature04396
    • H.T. McMahon, and J.L. Gallop Membrane curvature and mechanisms of dynamic cell membrane modeling Nature 438 2005 590 596 (Pubitemid 41740562)
    • (2005) Nature , vol.438 , Issue.7068 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 73
    • 33750239249 scopus 로고    scopus 로고
    • The physical chemistry of biological membranes
    • DOI 10.1038/nchembio1106-564, PII NCHEMBIO1106564
    • J. Zimmerberg, and K. Gawrich The physical chemistry of biological membranes Nat. Chem. Biol. 11 2006 564 567 (Pubitemid 44610336)
    • (2006) Nature Chemical Biology , vol.2 , Issue.11 , pp. 564-567
    • Zimmerberg, J.1    Gawrisch, K.2
  • 74
    • 33644846421 scopus 로고    scopus 로고
    • How proteins produce cellular membrane curvature
    • DOI 10.1038/nrm1784, PII N1784
    • J. Zimmerberg, and M.M. Kozlov How proteins produce cellular membrane curvature Nat. Rev. Mol. Cell Biol. 7 2006 9 19 (Pubitemid 43361568)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.1 , pp. 9-19
    • Zimmerberg, J.1    Kozlov, M.M.2
  • 75
    • 79953740665 scopus 로고    scopus 로고
    • Thermodynamics and mechanics of membrane curvature generation and sensing by proteins and lipids
    • T. Baumgart, B.R. Capraro, C. Zhu, and S.L. Das Thermodynamics and mechanics of membrane curvature generation and sensing by proteins and lipids Annu. Rev. Phys. Chem. 62 2011 483 506
    • (2011) Annu. Rev. Phys. Chem. , vol.62 , pp. 483-506
    • Baumgart, T.1    Capraro, B.R.2    Zhu, C.3    Das, S.L.4
  • 76
    • 64249110493 scopus 로고    scopus 로고
    • The BAR domain superfamily: Membrane-molding macromolecules
    • A. Frost, V.M. Unger, and P. De Camilli The BAR domain superfamily: membrane-molding macromolecules Cell 137 2009 191 196
    • (2009) Cell , vol.137 , pp. 191-196
    • Frost, A.1    Unger, V.M.2    De Camilli, P.3
  • 77
    • 33745737926 scopus 로고    scopus 로고
    • Membrane deformation by protein coats
    • DOI 10.1016/j.ceb.2006.06.003, PII S0955067406000792
    • B. Antonny Membrane deformation by protein coats Curr. Opin. Cell Biol. 18 2006 386 394 (Pubitemid 44016053)
    • (2006) Current Opinion in Cell Biology , vol.18 , Issue.4 , pp. 386-394
    • Antonny, B.1
  • 78
    • 0019336926 scopus 로고
    • Membrane asymmetry: A survey and critical appraisal of the methodology. II. Methods for assessing the unequal distribution of lipids
    • A.-H. Ftemadi Membrane asymmetry: a survey and critical appraisal of the methodology. II. Methods for assessing the unequal distribution of lipids Biochim. Biophys. Acta 604 1980 423 475
    • (1980) Biochim. Biophys. Acta , vol.604 , pp. 423-475
    • Ftemadi, A.-H.1
  • 79
    • 0015058203 scopus 로고
    • Ferritin-conjugated plant agglutinins as specific saccharide stains for electron microscopy: Application to saccharides bound to cell membranes
    • G.L. Nicolson, and S.J. Singer Ferritin-conjugated plant agglutinins as specific saccharide stains for electron microscopy: application to saccharides bound to cell membranes Proc. Natl. Acad. Sci. U. S. A. 68 1971 942 946
    • (1971) Proc. Natl. Acad. Sci. U. S. A. , vol.68 , pp. 942-946
    • Nicolson, G.L.1    Singer, S.J.2
  • 80
    • 0015254893 scopus 로고
    • Biological membranes: The dynamics of their organization
    • P. Siekevitz Biological membranes: the dynamics of their organization Annu. Rev. Physiol. 54 1972 117 140
    • (1972) Annu. Rev. Physiol. , vol.54 , pp. 117-140
    • Siekevitz, P.1
  • 82
    • 0015952653 scopus 로고
    • The distribution and asymmetry of saccharides on mammalian cell membrane surfaces utilizing ferritin-conjugated plant agglutinins as specific saccharide stains
    • G.L. Nicolson, and S.J. Singer The distribution and asymmetry of saccharides on mammalian cell membrane surfaces utilizing ferritin-conjugated plant agglutinins as specific saccharide stains J. Cell Biol. 60 1974 236 248
    • (1974) J. Cell Biol. , vol.60 , pp. 236-248
    • Nicolson, G.L.1    Singer, S.J.2
  • 83
    • 0016372224 scopus 로고
    • Topographical distribution of complex carbohydrates in the erythrocyte membrane
    • T.L. Steck, and G. Dawson Topographical distribution of complex carbohydrates in the erythrocyte membrane J. Biol. Chem. 249 1974 2135 2142
    • (1974) J. Biol. Chem. , vol.249 , pp. 2135-2142
    • Steck, T.L.1    Dawson, G.2
  • 84
    • 0016226796 scopus 로고
    • The organization of proteins in the human red blood cell membrane
    • T.L. Steck The organization of proteins in the human red blood cell membrane J. Cell Biol. 62 1974 1 19
    • (1974) J. Cell Biol. , vol.62 , pp. 1-19
    • Steck, T.L.1
  • 85
    • 0016813642 scopus 로고
    • Asymmetric exchange of vesicle phospholipids catalyzed by the phosphatidylcholine exchange protein. Measurement of inside-outside transitions
    • J.E. Rothman, and E.A. Davidowiec Asymmetric exchange of vesicle phospholipids catalyzed by the phosphatidylcholine exchange protein. Measurement of inside-outside transitions Biochemistry 14 1975 2809 2816
    • (1975) Biochemistry , vol.14 , pp. 2809-2816
    • Rothman, J.E.1    Davidowiec, E.A.2
  • 86
    • 0017356323 scopus 로고
    • Membrane asymmetry
    • J.E. Rothman, and J. Lenard Membrane asymmetry Science 195 1977 743 753
    • (1977) Science , vol.195 , pp. 743-753
    • Rothman, J.E.1    Lenard, J.2
  • 87
    • 0016747571 scopus 로고
    • Mammalian plasma membranes
    • M.S. Bretscher, and M.C. Raff Mammalian plasma membranes Nature 258 1975 43 49
    • (1975) Nature , vol.258 , pp. 43-49
    • Bretscher, M.S.1    Raff, M.C.2
  • 89
    • 0142218366 scopus 로고    scopus 로고
    • Regulation of transbilayer plasma membrane phospholipid asymmetry
    • DOI 10.1194/jlr.R200019-JLR200
    • D.L. Daleke Regulation of transbilayer plasma membrane phospholipid asymmetry J. Lipid Res. 44 2003 233 242 (Pubitemid 37303867)
    • (2003) Journal of Lipid Research , vol.44 , Issue.2 , pp. 233-242
    • Daleke, D.L.1
  • 90
    • 80052103076 scopus 로고    scopus 로고
    • Flipping and flopping - Lipids on the move
    • F.J. Sharom Flipping and flopping - lipids on the move IUBMB Life 63 2011 736 746
    • (2011) IUBMB Life , vol.63 , pp. 736-746
    • Sharom, F.J.1
  • 92
    • 0033342531 scopus 로고    scopus 로고
    • Recent advances in the understanding of membrane protein assembly and structure
    • G. von Heijne Recent advances in the understanding of membrane protein assembly and structure Q. Rev. Biophys. 32 2000 285 307
    • (2000) Q. Rev. Biophys. , vol.32 , pp. 285-307
    • Von Heijne, G.1
  • 93
    • 0015817606 scopus 로고
    • Cis- and trans-membrane control of cell surface topography
    • G.L. Nicolson Cis- and trans-membrane control of cell surface topography J. Supramol. Struct. 1 1973 410 416
    • (1973) J. Supramol. Struct. , vol.1 , pp. 410-416
    • Nicolson, G.L.1
  • 94
    • 0015144392 scopus 로고
    • The localization of spectrin on the inner surface of human red blood cell membranes by ferritin-conjugated antibodies
    • G.L. Nicolson, V.T. Marchesi, and S.J. Singer The localization of spectrin on the inner surface of human red blood cell membranes by ferritin-conjugated antibodies J. Cell Biol. 51 1971 266 272
    • (1971) J. Cell Biol. , vol.51 , pp. 266-272
    • Nicolson, G.L.1    Marchesi, V.T.2    Singer, S.J.3
  • 95
    • 0015440669 scopus 로고
    • A rapid method for determining the topological distribution of anionic sites on membrane surfaces
    • G.L. Nicolson A rapid method for determining the topological distribution of anionic sites on membrane surfaces J. Supramol. Struct. 1 1972 159 164
    • (1972) J. Supramol. Struct. , vol.1 , pp. 159-164
    • Nicolson, G.L.1
  • 96
    • 0015857064 scopus 로고
    • Anionic sites of human erythrocyte membranes. II. Anti-spectrin-induced transmembrane aggregation of the binding sites for positively charged colloidal particles
    • G.L. Nicolson, and R.G. Painter Anionic sites of human erythrocyte membranes. II. Anti-spectrin-induced transmembrane aggregation of the binding sites for positively charged colloidal particles J. Cell Biol. 59 1973 395 406
    • (1973) J. Cell Biol. , vol.59 , pp. 395-406
    • Nicolson, G.L.1    Painter, R.G.2
  • 97
    • 0016149580 scopus 로고
    • Lectin binding and perturbation of the cell membrane outer surface induces a transmembrane organizational alteration at the inner surface
    • T.H. Ji, and G.L. Nicolson Lectin binding and perturbation of the cell membrane outer surface induces a transmembrane organizational alteration at the inner surface Proc. Natl. Acad. Sci. U. S. A. 71 1974 2212 2216
    • (1974) Proc. Natl. Acad. Sci. U. S. A. , vol.71 , pp. 2212-2216
    • Ji, T.H.1    Nicolson, G.L.2
  • 98
    • 0022379986 scopus 로고
    • The mammalian spermatozoon: A model for the study of regional specificity in plasma membrane organization and function
    • DOI 10.1016/0040-8166(85)90035-7
    • R.N. Peterson, and L.D. Russell The mammalian spermatozoon: a model for the study of regional specificity in plasma membrane organization and function Tissue Cell 17 1985 769 791 (Pubitemid 16175255)
    • (1985) Tissue and Cell , vol.17 , Issue.6 , pp. 769-791
    • Peterson, R.N.1    Russell, L.D.2
  • 99
    • 0016257799 scopus 로고
    • Mobility and the restriction of mobility of plasma membrane lectin-binding components
    • G.L. Nicolson, and R. Yanagimachi Mobility and the restriction of mobility of plasma membrane lectin-binding components Science 184 1974 1294 1296
    • (1974) Science , vol.184 , pp. 1294-1296
    • Nicolson, G.L.1    Yanagimachi, R.2
  • 100
    • 0015884025 scopus 로고
    • Electron microscopic observations of the distribution of acidic anionic residues on hamster spermatozoa and eggs before and during fertilization
    • R. Yanagimachi, G.L. Nicolson, Y.D. Noda, and M. Fujimoto Electron microscopic observations of the distribution of acidic anionic residues on hamster spermatozoa and eggs before and during fertilization J. Ultrastruct. Res. 43 1973 344 353
    • (1973) J. Ultrastruct. Res. , vol.43 , pp. 344-353
    • Yanagimachi, R.1    Nicolson, G.L.2    Noda, Y.D.3    Fujimoto, M.4
  • 101
    • 0024295775 scopus 로고
    • Restricted lateral diffusion of PH-20, a PI-anchored sperm membrane protein
    • B.M. Phelps, P. Primakoff, D.E. Koppel, M.G. Low, and D.G. Myles Restricted lateral diffusion of PH-20, a PI-anchored sperm membrane protein Science 240 1988 1780 1782
    • (1988) Science , vol.240 , pp. 1780-1782
    • Phelps, B.M.1    Primakoff, P.2    Koppel, D.E.3    Low, M.G.4    Myles, D.G.5
  • 103
    • 67650418109 scopus 로고    scopus 로고
    • Cytoskeleton-membrane interactions in membrane raft structure
    • G.R. Chichili, and W. Rodgers Cytoskeleton-membrane interactions in membrane raft structure Cell. Mol. Life Sci. 66 2009 2319 2328
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 2319-2328
    • Chichili, G.R.1    Rodgers, W.2
  • 104
    • 48249134102 scopus 로고    scopus 로고
    • Mediation, modulation, and consequences of membrane-cytoskeletal interactions
    • G.J. Doherty, and H.T. McMahon Mediation, modulation, and consequences of membrane-cytoskeletal interactions Annu. Rev. Biophys. 37 2008 65 95
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 65-95
    • Doherty, G.J.1    McMahon, H.T.2
  • 105
    • 84868149349 scopus 로고    scopus 로고
    • Making parallel lines meet. Transferring information from microtubules to extracellular matrix
    • T.I. Baskin, and Y. Gu Making parallel lines meet. Transferring information from microtubules to extracellular matrix Cell Adhes. Migr. 6 2012 404 408
    • (2012) Cell Adhes. Migr. , vol.6 , pp. 404-408
    • Baskin, T.I.1    Gu, Y.2
  • 106
    • 84866397855 scopus 로고    scopus 로고
    • Targeting and transport: How microtubules control focal adhesion dynamics
    • S. Stehbens, and T. Wittmann Targeting and transport: how microtubules control focal adhesion dynamics J. Cell Biol. 198 2012 481 489
    • (2012) J. Cell Biol. , vol.198 , pp. 481-489
    • Stehbens, S.1    Wittmann, T.2
  • 107
    • 84871881434 scopus 로고    scopus 로고
    • Phosphoinositide lipid polarity: Linking the plasma membrane to the cytocortex
    • M.P. Krahn, and A. Wodarz Phosphoinositide lipid polarity: linking the plasma membrane to the cytocortex Essays Biochem. 53 2012 15 27
    • (2012) Essays Biochem. , vol.53 , pp. 15-27
    • Krahn, M.P.1    Wodarz, A.2
  • 108
    • 84866867380 scopus 로고    scopus 로고
    • Regulation from within: The cytoskeleton in transmembrane signaling
    • K. Jaqaman, and S. Grinstein Regulation from within: the cytoskeleton in transmembrane signaling Trends Cell Biol. 22 2012 515 526
    • (2012) Trends Cell Biol. , vol.22 , pp. 515-526
    • Jaqaman, K.1    Grinstein, S.2
  • 109
    • 84870188756 scopus 로고    scopus 로고
    • Dynamic organizing principals of the plasma membrane that regulate signal transduction: Commemorating the fortieth anniversary of Singer and Nicolson's fluid-mosaic model
    • A. Kusumi, T.K. Fujiwara, R. Chadda, M. Xie, T.A. Tsunoyama, Z. Kalay, R.S. Kasai, and K.G. Suzuki Dynamic organizing principals of the plasma membrane that regulate signal transduction: commemorating the fortieth anniversary of Singer and Nicolson's fluid-mosaic model Annu. Rev. Cell Dev. Biol. 28 2012 215 250
    • (2012) Annu. Rev. Cell Dev. Biol. , vol.28 , pp. 215-250
    • Kusumi, A.1    Fujiwara, T.K.2    Chadda, R.3    Xie, M.4    Tsunoyama, T.A.5    Kalay, Z.6    Kasai, R.S.7    Suzuki, K.G.8
  • 110
    • 84866397855 scopus 로고    scopus 로고
    • Targeting and transport: How microtubules control focal adhesion dynamics
    • S. Stehbens, and T. Wittmann Targeting and transport: how microtubules control focal adhesion dynamics J. Cell Biol. 198 2012 481 489
    • (2012) J. Cell Biol. , vol.198 , pp. 481-489
    • Stehbens, S.1    Wittmann, T.2
  • 111
    • 84255195050 scopus 로고    scopus 로고
    • Bridging membrane and cytoskeleton dynamics in the secretory and endocytic pathways
    • M. Anitei, and B. Hoflack Bridging membrane and cytoskeleton dynamics in the secretory and endocytic pathways Nat. Cell Biol. 14 2011 11 19
    • (2011) Nat. Cell Biol. , vol.14 , pp. 11-19
    • Anitei, M.1    Hoflack, B.2
  • 112
    • 0015122451 scopus 로고
    • The two-dimensional topographic distribution of H-2 histocompatibility alloantigens on mouse red blood cell membranes
    • G.L. Nicolson, R.H. Hyman, and S.J. Singer The two-dimensional topographic distribution of H-2 histocompatibility alloantigens on mouse red blood cell membranes J. Cell Biol. 50 1971 905 910
    • (1971) J. Cell Biol. , vol.50 , pp. 905-910
    • Nicolson, G.L.1    Hyman, R.H.2    Singer, S.J.3
  • 113
    • 0015402443 scopus 로고
    • Antigen cap formation in cultured fibroblasts: A reflection of membrane fluidity and cell motility
    • M. Edidin, and A. Weiss Antigen cap formation in cultured fibroblasts: a reflection of membrane fluidity and cell motility Proc. Natl. Acad. Sci. U. S. A. 69 1972 2456 2459
    • (1972) Proc. Natl. Acad. Sci. U. S. A. , vol.69 , pp. 2456-2459
    • Edidin, M.1    Weiss, A.2
  • 114
    • 0016577241 scopus 로고
    • Local anesthetics affect transmembrane cytoskeletal control of mobility and distribution of cell surface receptors
    • G. Poste, D. Papahadjopoulos, and G.L. Nicolson Local anesthetics affect transmembrane cytoskeletal control of mobility and distribution of cell surface receptors Proc. Natl. Acad. Sci. U. S. A. 72 1975 4430 4434
    • (1975) Proc. Natl. Acad. Sci. U. S. A. , vol.72 , pp. 4430-4434
    • Poste, G.1    Papahadjopoulos, D.2    Nicolson, G.L.3
  • 116
    • 0015415283 scopus 로고
    • Ligand-induced movement of lymphocyte membrane macromolecules. I. Analysis by immunofluorescence and ultrastructural radioautography
    • E.R. Unanue, W.D. Perkins, and M.J. Karnovsky Ligand-induced movement of lymphocyte membrane macromolecules. I. Analysis by immunofluorescence and ultrastructural radioautography J. Exp. Med. 136 1972 885 906
    • (1972) J. Exp. Med. , vol.136 , pp. 885-906
    • Unanue, E.R.1    Perkins, W.D.2    Karnovsky, M.J.3
  • 117
    • 0022976907 scopus 로고
    • Recycling class I MHC antigens: Dynamics of internalization, acidification, and ligand-degradation in murine T lymphoblasts
    • D.B. Tse, C.R. Cantor, J. McDowell, and B. Pernis Recycling class I MHC antigens: dynamics of internalization, acidification, and ligand-degradation in murine T lymphoblasts J. Mol. Cell. Immunol. 2 1986 315 329 (Pubitemid 17198664)
    • (1986) Journal of Molecular and Cellular Immunology , vol.2 , Issue.6 , pp. 315-329
    • Tse, D.B.1    Cantor, C.R.2    McDowell, J.3    Pernis, B.4
  • 118
    • 0029553517 scopus 로고
    • Molecular interactions in the submembrane plaque of cell-cell and cell-matrix adhesions
    • B. Geiger, S. Yehuda-Levenberg, and A.D. Bershadsky Molecular interactions in the submembrane plaque of cell-cell and cell-matrix adhesions Acta Anat. (Basel) 154 1995 42 62
    • (1995) Acta Anat. (Basel) , vol.154 , pp. 42-62
    • Geiger, B.1    Yehuda-Levenberg, S.2    Bershadsky, A.D.3
  • 119
    • 0032559341 scopus 로고    scopus 로고
    • A structural scaffolding of intermediate filaments in health and disease
    • E. Fuchs, and D.W. Cleveland A structural scaffolding of intermediate filaments in health and disease Science 279 1998 1897 1907
    • (1998) Science , vol.279 , pp. 1897-1907
    • Fuchs, E.1    Cleveland, D.W.2
  • 120
    • 0018745363 scopus 로고
    • Lectin-mediated agglutination of murine lymphoma cells. Cell surface deformability and reversibility of agglutination by saccharides
    • G.L. Nicolson, and G. Poste Lectin-mediated agglutination of murine lymphoma cells. Cell surface deformability and reversibility of agglutination by saccharides Biochim. Biophys. Acta 554 1979 520 531 (Pubitemid 9234265)
    • (1979) Biochimica et Biophysica Acta , vol.554 , Issue.2 , pp. 520-531
    • Nicolson, G.L.1    Poste, G.2
  • 121
    • 70649099318 scopus 로고    scopus 로고
    • Glycosaminoglycan chains affect exocytic and endocytic protein traffic
    • S. Kobialka, N. Beuret, H. Ben-Tekya, and M. Spiess Glycosaminoglycan chains affect exocytic and endocytic protein traffic Traffic 10 2009 1845 1855
    • (2009) Traffic , vol.10 , pp. 1845-1855
    • Kobialka, S.1    Beuret, N.2    Ben-Tekya, H.3    Spiess, M.4
  • 122
    • 0024253418 scopus 로고
    • Selective anchoring in the specific plasma membrane domain: A role in epithelial cell polarity
    • DOI 10.1083/jcb.107.6.2363
    • P.J. Salas, D.E. Vega-Salas, J. Hochman, E. Rodriguez-Boulan, and M. Edidin Selective anchoring in the specific plasma membrane domain: a role in epithelial cell polarity J. Cell Biol. 107 1988 2363 2376 (Pubitemid 19015114)
    • (1988) Journal of Cell Biology , vol.107 , Issue.6 , pp. 2363-2376
    • Salas, P.J.I.1    Vega-Salas, D.E.2    Hochman, J.3    Rodriguez-Boulan, E.4    Edidin, M.5
  • 123
    • 84869102195 scopus 로고    scopus 로고
    • Finding the weakest link - Exploring integrin-mediated mechanical molecular pathways
    • P. Roca-Cusach, T. Iskratsch, and M.P. Sheetz Finding the weakest link - exploring integrin-mediated mechanical molecular pathways J. Cell Sci. 125 2012 3025 3038
    • (2012) J. Cell Sci. , vol.125 , pp. 3025-3038
    • Roca-Cusach, P.1    Iskratsch, T.2    Sheetz, M.P.3
  • 124
    • 78851471723 scopus 로고    scopus 로고
    • Effects of shear stress and stretch on endothelial function
    • J. Ando, and K. Yamamoto Effects of shear stress and stretch on endothelial function Antioxid. Redox Signal. 15 2011 1389 1403
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 1389-1403
    • Ando, J.1    Yamamoto, K.2
  • 125
    • 0020637998 scopus 로고
    • Membrane-cytoskeletal interaction
    • B. Geiger Membrane-cytoskeletal interaction Biochim. Biophys. Acta 737 1983 305 341
    • (1983) Biochim. Biophys. Acta , vol.737 , pp. 305-341
    • Geiger, B.1
  • 126
    • 0026497661 scopus 로고
    • Cytoskeleton-plasma membrane interactions
    • E.J. Luna, and A.L. Hitt Cytoskeleton-plasma membrane interactions Science 258 1992 955 964
    • (1992) Science , vol.258 , pp. 955-964
    • Luna, E.J.1    Hitt, A.L.2
  • 127
    • 0035344650 scopus 로고    scopus 로고
    • Cell control by membrane-cytoskeleton adhesion
    • DOI 10.1038/35073095
    • M.P. Sheetz Cell control by membrane-cytoskeleton adhesion Nat. Rev. Mol. Cell Biol. 2 2001 392 396 (Pubitemid 33674052)
    • (2001) Nature Reviews Molecular Cell Biology , vol.2 , Issue.5 , pp. 392-396
    • Sheetz, M.P.1
  • 128
    • 44349102027 scopus 로고    scopus 로고
    • The septin family of GTPases: Architecture and dynamics
    • DOI 10.1038/nrm2407, PII NRM2407
    • C.S. Weirich, J.P. Erzberger, and Y. Barral The septin family of GTPases: architecture and dynamics Nat. Rev. Mol. Cell Biol. 9 2008 478 489 (Pubitemid 351733401)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.6 , pp. 478-489
    • Weirich, C.S.1    Erzberger, J.P.2    Barral, Y.3
  • 130
    • 84857457272 scopus 로고    scopus 로고
    • Septins: The fourth component of the cytoskeleton
    • S. Mostowy, and P. Cossart Septins: the fourth component of the cytoskeleton Nat. Rev. Mol. Cell Biol. 13 2012 183 194
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 183-194
    • Mostowy, S.1    Cossart, P.2
  • 131
    • 64549158361 scopus 로고    scopus 로고
    • Septins and the lateral compartmentalization of eukaryotic membranes
    • F. Caudron, and Y. Barral Septins and the lateral compartmentalization of eukaryotic membranes Dev. Cell 16 2009 493 506
    • (2009) Dev. Cell , vol.16 , pp. 493-506
    • Caudron, F.1    Barral, Y.2
  • 132
    • 0000636835 scopus 로고
    • Yolk protein uptake in the oocyte of the mosquito Aedes aegypti L
    • T.E. Roth, and K.R. Porter Yolk protein uptake in the oocyte of the mosquito Aedes aegypti L J. Cell Biol. 20 1964 313 332
    • (1964) J. Cell Biol. , vol.20 , pp. 313-332
    • Roth, T.E.1    Porter, K.R.2
  • 133
    • 0014147041 scopus 로고
    • Functions of coated vesicles during protein absorption in the rate vas deferens
    • D.S. Friend, and M.G. Farquhar Functions of coated vesicles during protein absorption in the rate vas deferens J. Cell Biol. 35 1967 357 376
    • (1967) J. Cell Biol. , vol.35 , pp. 357-376
    • Friend, D.S.1    Farquhar, M.G.2
  • 134
    • 0016834909 scopus 로고
    • Coated vesicles from pig brain: Purification and biochemical characterization
    • B.M. Pearse Coated vesicles from pig brain: purification and biochemical characterization J. Mol. Biol. 97 1975 93 98
    • (1975) J. Mol. Biol. , vol.97 , pp. 93-98
    • Pearse, B.M.1
  • 136
    • 0034677633 scopus 로고    scopus 로고
    • Decoding of sorting signals by coatomer through a GTPase switch in the COPI coat complex
    • J. Goldberg Decoding of sorting signals by coatomer through a GTPase switch in the COPI coat complex Cell 100 2000 671 679
    • (2000) Cell , vol.100 , pp. 671-679
    • Goldberg, J.1
  • 137
    • 84872959202 scopus 로고    scopus 로고
    • Caveolae as plasma membrane sensors, protectors and organizers
    • R.G. Parton, and M.A. del Pozo Caveolae as plasma membrane sensors, protectors and organizers Nat. Rev. Mol. Cell Biol. 14 2013 98 112
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 98-112
    • Parton, R.G.1    Del Pozo, M.A.2
  • 138
    • 84874710481 scopus 로고    scopus 로고
    • Phagocytosis and cytokinesis: Do cells use common tools to cut and to eat? Highlights on common themes and differences
    • C. Deschamps, A. Echard, and F. Niedergang Phagocytosis and cytokinesis: do cells use common tools to cut and to eat? Highlights on common themes and differences Traffic 14 2013 355 364
    • (2013) Traffic , vol.14 , pp. 355-364
    • Deschamps, C.1    Echard, A.2    Niedergang, F.3
  • 139
    • 84872352440 scopus 로고    scopus 로고
    • Role of phospholipids in endocytosis, phagocytosis and macropinocytosis
    • M. Bohdanowicz, and S. Grinstein Role of phospholipids in endocytosis, phagocytosis and macropinocytosis Physiol. Rev. 93 2013 69 106
    • (2013) Physiol. Rev. , vol.93 , pp. 69-106
    • Bohdanowicz, M.1    Grinstein, S.2
  • 140
    • 84871874253 scopus 로고    scopus 로고
    • The role of secretory and endocytic pathways in the maintenance of cell polarity
    • S.F. Ang, and H. Fölsch The role of secretory and endocytic pathways in the maintenance of cell polarity Essays Biochem. 53 2012 29 39
    • (2012) Essays Biochem. , vol.53 , pp. 29-39
    • Ang, S.F.1    Fölsch, H.2
  • 142
    • 84862883553 scopus 로고    scopus 로고
    • Information processing during phagocytosis
    • D.M. Underhill, and H.S. Goodridge Information processing during phagocytosis Nat. Rev. Immunol. 12 2012 492 502
    • (2012) Nat. Rev. Immunol. , vol.12 , pp. 492-502
    • Underhill, D.M.1    Goodridge, H.S.2
  • 143
    • 80053130680 scopus 로고    scopus 로고
    • New insights into the T cell synapse from single molecule techniques
    • M.L. Dustin, and D. Depoil New insights into the T cell synapse from single molecule techniques Nat. Rev. Immunol. 11 2011 672 684
    • (2011) Nat. Rev. Immunol. , vol.11 , pp. 672-684
    • Dustin, M.L.1    Depoil, D.2
  • 144
    • 84869111112 scopus 로고    scopus 로고
    • United we stand: Integrating the actin cytoskeleton and cell-matrix adhesions in cellular mechanotransduction
    • U.S. Schwarz, and M.L. Gardel United we stand: integrating the actin cytoskeleton and cell-matrix adhesions in cellular mechanotransduction J. Cell Sci. 125 2012 3051 3060
    • (2012) J. Cell Sci. , vol.125 , pp. 3051-3060
    • Schwarz, U.S.1    Gardel, M.L.2
  • 145
    • 77956020315 scopus 로고    scopus 로고
    • Regulation of actin cytoskeleton dynamics in cells
    • S.H. Lee, and R. Dominguez Regulation of actin cytoskeleton dynamics in cells Mol. Cells 29 2010 311 325
    • (2010) Mol. Cells , vol.29 , pp. 311-325
    • Lee, S.H.1    Dominguez, R.2
  • 146
    • 3543083870 scopus 로고    scopus 로고
    • The co-workers of actin filaments: From cell structures to signals
    • DOI 10.1038/nrm1437
    • C. Revenu, R. Athman, S. Robine, and D. Louvard The co-workers of actin filaments: from cell structures to signals Nat. Rev. Mol. Cell Biol. 5 2004 635 646 (Pubitemid 39025064)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.8 , pp. 635-646
    • Revenu, C.1    Athman, R.2    Robine, S.3    Louvard, D.4
  • 148
    • 77956064817 scopus 로고    scopus 로고
    • Cell adhesion: Integrating cytoskeletal dynamics and cellular tension
    • J.T. Parsons, A.R. Horwitz, and M.A. Schwartz Cell adhesion: integrating cytoskeletal dynamics and cellular tension Nat. Rev. Mol. Cell Biol. 11 2010 633 643
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 633-643
    • Parsons, J.T.1    Horwitz, A.R.2    Schwartz, M.A.3
  • 149
    • 80051770283 scopus 로고    scopus 로고
    • Dissecting cell adhesion architecture using advanced imaging techniques
    • P.E. Morton, and M. Parsons Dissecting cell adhesion architecture using advanced imaging techniques Cell Adhes. Migr. 5 2011 351 359
    • (2011) Cell Adhes. Migr. , vol.5 , pp. 351-359
    • Morton, P.E.1    Parsons, M.2
  • 150
    • 84869102195 scopus 로고    scopus 로고
    • Finding the weakest link - Exploring integrin-mediated mechanical molecular pathways
    • P. Roca-Cusachs, T. Iskratsch, and M.P. Sheetz Finding the weakest link - exploring integrin-mediated mechanical molecular pathways J. Cell Sci. 125 2012 3025 3038
    • (2012) J. Cell Sci. , vol.125 , pp. 3025-3038
    • Roca-Cusachs, P.1    Iskratsch, T.2    Sheetz, M.P.3
  • 152
    • 84860858416 scopus 로고    scopus 로고
    • Exosomes: Current knowledge of their composition, biological functions, and diagnostic and therapeutic potentials
    • A.V. Vlassov, S. Magdaleno, R. Setterquist, and R. Conrad Exosomes: current knowledge of their composition, biological functions, and diagnostic and therapeutic potentials Biochim. Biophys. Acta 1820 2012 940 948
    • (2012) Biochim. Biophys. Acta , vol.1820 , pp. 940-948
    • Vlassov, A.V.1    Magdaleno, S.2    Setterquist, R.3    Conrad, R.4
  • 153
    • 84872149261 scopus 로고    scopus 로고
    • Extracellular vesicles in physiological and pathological conditions
    • Y. Yuana, A. Sturk, and R. Nieuwland Extracellular vesicles in physiological and pathological conditions Blood Rev. 27 2013 31 39
    • (2013) Blood Rev. , vol.27 , pp. 31-39
    • Yuana, Y.1    Sturk, A.2    Nieuwland, R.3
  • 154
    • 0026087533 scopus 로고
    • Structure-activity relationships for transmembrane signaling: The receptor's turn
    • M.D. Hollenberg Structure-activity relationships for transmembrane signaling: the receptor's turn FASEB J. 5 1991 178 186 (Pubitemid 21892877)
    • (1991) FASEB Journal , vol.5 , Issue.2 , pp. 178-186
    • Hollenberg, M.D.1
  • 155
    • 0020406143 scopus 로고
    • Interactions between membrane skeleton proteins and the intrinsic domain of the erythrocyte membrane
    • C.W.M. Haest Interactions between membrane skeleton proteins and the intrinsic domain of the erythrocyte membrane Biochim. Biophys. Acta 694 1982 331 352 (Pubitemid 13150550)
    • (1982) Biochimica et Biophysica Acta , vol.694 , Issue.4 , pp. 331-352
    • Haest, C.W.M.1
  • 156
    • 0034644509 scopus 로고    scopus 로고
    • Signaling networks: The origins of cellular multitasking
    • J.D. Jordan, E.M. Landau, and R. Iyengar Signaling networks: the origins of cellular multitasking Cell 103 2000 193 200
    • (2000) Cell , vol.103 , pp. 193-200
    • Jordan, J.D.1    Landau, E.M.2    Iyengar, R.3
  • 157
    • 0033913213 scopus 로고    scopus 로고
    • Signaling pathways in insulin action: Molecular targets of insulin resistance
    • J.E. Pessin, and A.R. Saltiel Signaling pathways in insulin action: molecular targets of insulin resistance J. Clin. Investig. 106 2000 165 169 (Pubitemid 30483117)
    • (2000) Journal of Clinical Investigation , vol.106 , Issue.2 , pp. 165-169
    • Pessin, J.E.1    Saltiel, A.R.2
  • 158
    • 33646440929 scopus 로고    scopus 로고
    • Building signaling complexes at the membrane
    • W. Cho Building signaling complexes at the membrane Sci. STKE 2006 2006 pe7
    • (2006) Sci. STKE , vol.2006 , pp. 7
    • Cho, W.1
  • 160
    • 0035479910 scopus 로고    scopus 로고
    • Assembly and mechanosensory function of focal contacts
    • DOI 10.1016/S0955-0674(00)00255-6
    • B. Geiger, and A. Bershadsky Assembly and mechanosensory function of focal contacts Curr. Opin. Cell Biol. 13 2001 584 592 (Pubitemid 32817017)
    • (2001) Current Opinion in Cell Biology , vol.13 , Issue.5 , pp. 584-592
    • Geiger, B.1    Bershadsky, A.2
  • 162
    • 84865974846 scopus 로고    scopus 로고
    • Membrane physiology and the biophysics in the next decade: An open balcony to multiple scenarios
    • (Article 23)
    • M.L. Diaz Membrane physiology and the biophysics in the next decade: an open balcony to multiple scenarios Front. Physiol. 1 2010 1 2 (Article 23)
    • (2010) Front. Physiol. , vol.1 , pp. 1-2
    • Diaz, M.L.1
  • 163
    • 39849092445 scopus 로고    scopus 로고
    • CLC chloride channels and transporters: From genes to protein structure, pathology and physiology
    • DOI 10.1080/10409230701829110, PII 791049831
    • T.J. Jentsch CLC chloride channels and transporters: from genes to protein structure, pathology and physiology Crit. Rev. Biochem. Mol. Biol. 43 2008 3 36 (Pubitemid 351315859)
    • (2008) Critical Reviews in Biochemistry and Molecular Biology , vol.43 , Issue.1 , pp. 3-36
    • Jentsch, T.J.1
  • 164
    • 0015236391 scopus 로고
    • Disposition of the major proteins in the isolated erythrocyte membrane
    • T.L. Steck, G. Faribanks, and D.F. Wallach Disposition of the major proteins in the isolated erythrocyte membrane Biochemistry 10 1971 2617 2624
    • (1971) Biochemistry , vol.10 , pp. 2617-2624
    • Steck, T.L.1    Faribanks, G.2    Wallach, D.F.3
  • 165
    • 1642316966 scopus 로고    scopus 로고
    • The cooperative role of membrane skeleton and bilayer in the mechanical behaviour of red blood cells
    • DOI 10.1016/j.bioelechem.2003.08.002, PII S1567539403000884
    • S. Svetina, D. Kuzman, R.E. Waugh, P. Ziherl, and B. Zeks The cooperative role of membrane skeleton and bilayer in the mechanical behavior of red blood cells Bioelectrochem. 62 2004 107 113 (Pubitemid 38376148)
    • (2004) Bioelectrochemistry , vol.62 , Issue.2 , pp. 107-113
    • Svetina, S.1    Kuzman, D.2    Waugh, R.E.3    Ziherl, P.4    Zeks, B.5
  • 166
    • 58149158216 scopus 로고    scopus 로고
    • Red cell membrane: Past, present, and future
    • N. Mohandas, and P.G. Gallagher Red cell membrane: past, present, and future Blood 112 2008 3939 3948
    • (2008) Blood , vol.112 , pp. 3939-3948
    • Mohandas, N.1    Gallagher, P.G.2
  • 167
    • 84861329313 scopus 로고    scopus 로고
    • Refined views of the multi-protein complexes in the erythrocyte membrane
    • T.J. Mankelow, T.J. Satchwell, and N.M. Burton Refined views of the multi-protein complexes in the erythrocyte membrane Blood Cells Mol. Dis. 49 2012 1 10
    • (2012) Blood Cells Mol. Dis. , vol.49 , pp. 1-10
    • Mankelow, T.J.1    Satchwell, T.J.2    Burton, N.M.3
  • 168
    • 78651149939 scopus 로고
    • Mechanical properties of the red cell membrane. I. Membrane stiffness and intracellular pressure
    • R.P. Rand, and A.C. Burton Mechanical properties of the red cell membrane. I. Membrane stiffness and intracellular pressure Biophys. J. 4 1964 115 135
    • (1964) Biophys. J. , vol.4 , pp. 115-135
    • Rand, R.P.1    Burton, A.C.2
  • 169
    • 0028263839 scopus 로고
    • Mechanical properties of the red cell membrane in relation to molecular structure and genetic defects
    • N. Mohandas, and E. Evans Mechanical properties of the red cell membrane in relation to molecular structure and genetic defects Annu. Rev. Biophys. Biomol. Struct. 23 1994 787 818 (Pubitemid 24217386)
    • (1994) Annual Review of Biophysics and Biomolecular Structure , vol.23 , pp. 787-818
    • Mohandas, N.1    Evans, E.2
  • 170
    • 0033976553 scopus 로고    scopus 로고
    • New insights into erythrocyte membrane organization and microelasticity
    • DOI 10.1097/00062752-200003000-00008
    • D.E. Discher New insights into erythrocyte membrane organization and microelasticity Curr. Opin. Hematol. 7 2000 117 122 (Pubitemid 30106544)
    • (2000) Current Opinion in Hematology , vol.7 , Issue.2 , pp. 117-122
    • Discher, D.E.1
  • 171
    • 0014411415 scopus 로고
    • Selective solubilization of a protein of the red cell membrane
    • V.T. Marchesi, and E. Steers Jr. Selective solubilization of a protein of the red cell membrane Science 159 1968 203 204
    • (1968) Science , vol.159 , pp. 203-204
    • Marchesi, V.T.1    Steers, Jr.E.2
  • 172
    • 0027272883 scopus 로고
    • Red blood cell deformability, membrane material properties and shape: Regulation by transmembrane, skeletal and cytosolic proteins and lipids
    • N. Mohandas, and J.A. Chasis Red blood cell deformability, membrane material properties and shape: regulation by transmembrane, skeletal and cytosolic proteins and lipids Semin. Hematol. 30 1993 171 192 (Pubitemid 23216313)
    • (1993) Seminars in Hematology , vol.30 , Issue.3 , pp. 171-192
    • Mohandas, N.1    Chasis, J.A.2
  • 173
    • 77952929975 scopus 로고    scopus 로고
    • Molecular bases of cell-cell junction stability and dynamics
    • M. Cavey, and T. Lecuit Molecular bases of cell-cell junction stability and dynamics Cold Spring Harb. Perspect. Biol. 1 2009 a002998
    • (2009) Cold Spring Harb. Perspect. Biol. , vol.1 , pp. 002998
    • Cavey, M.1    Lecuit, T.2
  • 175
    • 74949087490 scopus 로고    scopus 로고
    • Tight junctions: A barrier to the initiation and progression of breast cancer?
    • K. Brennan, G. Offiah, E.A. McSherry, and A.M. Hopkins Tight junctions: a barrier to the initiation and progression of breast cancer? J. Biomed. Biotechnol. 2010 2010 460607
    • (2010) J. Biomed. Biotechnol. , vol.2010 , pp. 460607
    • Brennan, K.1    Offiah, G.2    McSherry, E.A.3    Hopkins, A.M.4
  • 176
    • 67249099003 scopus 로고    scopus 로고
    • Dynamic regulation of epithelial cell fate and barrier function by intercellular junctions
    • S. Koch, and A. Nurat Dynamic regulation of epithelial cell fate and barrier function by intercellular junctions Ann. N.Y. Acad. Sci. 1165 2009 220 227
    • (2009) Ann. N.Y. Acad. Sci. , vol.1165 , pp. 220-227
    • Koch, S.1    Nurat, A.2
  • 177
    • 84859884278 scopus 로고    scopus 로고
    • Regulation of intracellular calcium signaling through calcium interactions with connexin-based channels
    • J.A. Orellana, H.A. Sánchez, K.A. Schalper, V. Figueroa, and J.C. Sáez Regulation of intracellular calcium signaling through calcium interactions with connexin-based channels Adv. Exp. Med. Biol. 740 2012 777 794
    • (2012) Adv. Exp. Med. Biol. , vol.740 , pp. 777-794
    • Orellana, J.A.1    Sánchez, H.A.2    Schalper, K.A.3    Figueroa, V.4    Sáez, J.C.5
  • 178
    • 84870064557 scopus 로고    scopus 로고
    • Gap junction proteins on the move: Connexins, the cytoskeleton and migration
    • L. Matsuuchi, and C.C. Naus Gap junction proteins on the move: connexins, the cytoskeleton and migration Biochim. Biophys. Acta 1828 2013 94 108
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 94-108
    • Matsuuchi, L.1    Naus, C.C.2
  • 179
    • 68349128540 scopus 로고    scopus 로고
    • The junctions that don't fit the scheme: Special symmetrical cell-cell junctions of their own kind
    • W.W. Franke, S. Rickelt, M. Barth, and S. Pieperhoff The junctions that don't fit the scheme: special symmetrical cell-cell junctions of their own kind Cell Tissue Res. 338 2009 1 17
    • (2009) Cell Tissue Res. , vol.338 , pp. 1-17
    • Franke, W.W.1    Rickelt, S.2    Barth, M.3    Pieperhoff, S.4
  • 180
    • 0017304621 scopus 로고
    • Lipid-mediated protein interaction in membranes
    • S. Marcelja Lipid-mediated protein interaction in membranes Biochim. Biophys. Acta 455 1976 1 7
    • (1976) Biochim. Biophys. Acta , vol.455 , pp. 1-7
    • Marcelja, S.1
  • 181
    • 34347262391 scopus 로고    scopus 로고
    • Bilayer thickness and membrane protein function: An energetic perspective
    • DOI 10.1146/annurev.biophys.36.040306.132643
    • Olaf S. Andersen, and R.E. Köppe Bilayer thickness and membrane protein function: an energetic perspective Annu. Rev. Biophys. Biomol. Struct. 36 2007 107 130 (Pubitemid 46998112)
    • (2007) Annual Review of Biophysics and Biomolecular Structure , vol.36 , pp. 107-130
    • Andersen, O.S.1    Koeppe II, R.E.2
  • 183
    • 80054691804 scopus 로고    scopus 로고
    • Lipids, curvature and nano-medicine
    • O.G. Mouritsen Lipids, curvature and nano-medicine Eur. J. Lipid Sci. Technol. 113 2011 1174 1187
    • (2011) Eur. J. Lipid Sci. Technol. , vol.113 , pp. 1174-1187
    • Mouritsen, O.G.1
  • 184
    • 0032877355 scopus 로고    scopus 로고
    • Is the protein/lipid hydrophobic matching principle relevant to membrane organization and functions?
    • DOI 10.1016/S0014-5793(99)01148-5, PII S0014579399011485
    • F. Dumas, M.C. Lebrun, and J.-F. Tocanne Is the protein/lipid hydrophobic matching principle relevant to membrane organization and functions? FEBS Lett. 458 1999 271 277 (Pubitemid 29433818)
    • (1999) FEBS Letters , vol.458 , Issue.3 , pp. 271-277
    • Dumas, F.1    Lebrun, M.C.2    Tocanne, J.-F.3
  • 186
    • 0025035556 scopus 로고
    • Microimmiscibility and three-dimensional dynamic structures of phosphatidylcholine-cholesterol membranes: Translational diffusion of a copper complex in the membrane
    • DOI 10.1021/bi00486a023
    • W.K. Subczynski, W.E. Antholine, J.S. Hyde, and A. Kusumi Microimmiscibility and three-dimensional dynamics structures of phosphatidylcholine-cholesterol membranes: translational diffusion of a copper complex in the membrane Biochemistry 29 1990 7936 7945 (Pubitemid 20281244)
    • (1990) Biochemistry , vol.29 , Issue.34 , pp. 7936-7945
    • Subczynski, W.K.1    Antholine, W.E.2    Hyde, J.S.3    Kusumi, A.4
  • 187
    • 0025931149 scopus 로고
    • Influence of phospholipids unsaturation on the cholesterol distribution in membranes
    • M. Pasenkiewicz-Gierula, W.K. Subcznski, and A. Kusumi Influence of phospholipids unsaturation on the cholesterol distribution in membranes Biochimie 73 1991 1311 1316
    • (1991) Biochimie , vol.73 , pp. 1311-1316
    • Pasenkiewicz-Gierula, M.1    Subcznski, W.K.2    Kusumi, A.3
  • 188
    • 0020455954 scopus 로고
    • Spin-label saturation transfer electron spin resonance detection of transient association of rhodopsin in reconstituted membranes
    • DOI 10.1021/bi00266a039
    • A. Kusumi, and J.S. Hyde Spin-label saturation-transfer electron spin resonance detection of transient association of rhodopsin in reconstituted membranes Biochemistry 21 1982 5978 5983 (Pubitemid 13184197)
    • (1982) Biochemistry , vol.21 , Issue.23 , pp. 5978-5983
    • Kusumi, A.1    Hyde, J.S.2
  • 189
    • 0030771336 scopus 로고    scopus 로고
    • Wetting and capillary condensation as means of protein organization in membranes
    • T. Gill, M.C. Sabra, J.H. Ipsen, and O.G. Mouritsen Wetting and capillary condensation as a means of protein organization in membranes Biophys. J. 73 1997 1728 1741 (Pubitemid 27425704)
    • (1997) Biophysical Journal , vol.73 , Issue.4 , pp. 1728-1741
    • Gil, T.1    Sabra, M.C.2    Ipsen, J.H.3    Mouritsen, O.G.4
  • 190
    • 0036046535 scopus 로고    scopus 로고
    • Plasma membrane phospholipid asymmetry
    • P.J. Quinn Plasma membrane phospholipid asymmetry Subcell. Biochem. 36 2002 39 60
    • (2002) Subcell. Biochem. , vol.36 , pp. 39-60
    • Quinn, P.J.1
  • 191
    • 84875523320 scopus 로고    scopus 로고
    • Stiffened lipid platforms at molecular force foci
    • A. Anishkin, and C. Kung Stiffened lipid platforms at molecular force foci Proc. Natl. Acad. Aci. U.S.A. 110 2013 4886 4892
    • (2013) Proc. Natl. Acad. Aci. U.S.A. , vol.110 , pp. 4886-4892
    • Anishkin, A.1    Kung, C.2
  • 192
    • 0036027683 scopus 로고    scopus 로고
    • Cholesterol interactions with phospholipids in membranes
    • DOI 10.1016/S0163-7827(01)00020-0, PII S0163782701000200
    • H. Ohvo-Rekila, B. Ramstedt, P. Leppimaki, and J.P. Slotte Cholesterol interactions with phospholipids in membranes Progr. Lipid Res. 41 2002 66 97 (Pubitemid 32998278)
    • (2002) Progress in Lipid Research , vol.41 , Issue.1 , pp. 66-97
    • Ohvo-Rekila, H.1    Ramstedt, B.2    Leppimaki, P.3    Peter Slotte, J.4
  • 193
    • 0027892019 scopus 로고
    • Cholesterol and the Golgi apparatus
    • M.S. Bretscher, and S. Munro Cholesterol and the Golgi apparatus Science 261 1993 1280 1281 (Pubitemid 24081166)
    • (1993) Science , vol.261 , Issue.5126 , pp. 1280-1281
    • Bretscher, M.S.1    Munro, S.2
  • 194
    • 36249027008 scopus 로고    scopus 로고
    • Molecular dynamics simulations of bilayers containing mixtures of sphingomyelin with cholesterol and phosphatidylcholine with cholesterol
    • DOI 10.1021/jp074037i
    • Z. Zhang, S.Y. Bhide, and M.L. Berkowitz Molecular dynamics simulations of bilayers containing mixtures of sphingomyelin with cholesterol and phosphatidylcholine with cholesterol J. Phys. Chem. B 111 2007 12888 12897 (Pubitemid 350136480)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.44 , pp. 12888-12897
    • Zhang, Z.1    Bhide, S.Y.2    Berkowitz, M.L.3
  • 195
    • 33846826956 scopus 로고    scopus 로고
    • Insight into the putative specific interactions between cholesterol, sphingomyelin, and palmitoyl-oleoyl phosphatidylcholine
    • DOI 10.1529/biophysj.106.088427
    • J. Aittoniemi, P.S. Niemela, M.T. Hyvonen, M. Karttunen, and I. Vattulainen Insight into the putative specific interactions between cholesterol, sphingomyelin, and palmitoyl-oleoyl phosphatidylcholine Biophys. J. 92 2007 1125 1137 (Pubitemid 46203174)
    • (2007) Biophysical Journal , vol.92 , Issue.4 , pp. 1125-1137
    • Aittoniemi, J.1    Niemela, P.S.2    Hyvonen, M.T.3    Karttunen, M.4    Vattulainen, I.5
  • 197
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • D. Lingwood, and K. Simons Lipid rafts as a membrane-organizing principle Science 327 2010 46 50
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 198
    • 0036027683 scopus 로고    scopus 로고
    • Cholesterol interactions with phospholipids in membranes
    • DOI 10.1016/S0163-7827(01)00020-0, PII S0163782701000200
    • H. Ohvo-Rekilä, B. Ramstedt, P. Leppimäki, and J.P. Slotte Cholesterol interactions with phospholipids in membranes Prog. Lipid Res. 41 2002 66 97 (Pubitemid 32998278)
    • (2002) Progress in Lipid Research , vol.41 , Issue.1 , pp. 66-97
    • Ohvo-Rekila, H.1    Ramstedt, B.2    Leppimaki, P.3    Peter Slotte, J.4
  • 199
    • 33845349236 scopus 로고    scopus 로고
    • Sphingolipids and the formation of sterol-enriched ordered membrane domains
    • DOI 10.1016/j.bbamem.2006.05.020, PII S0005273606002045, Sphingolipids, Apoptosis and Disease
    • B. Ramstedt, and J.P. Slotte Sphingolipids and the formation of sterol-enriched ordered membrane domains Biochim. Biophys. Acta 1758 2006 1945 1956 (Pubitemid 44879357)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.12 , pp. 1945-1956
    • Ramstedt, B.1    Slotte, J.P.2
  • 201
    • 77954956306 scopus 로고    scopus 로고
    • Lipidomics: Coming to grips with lipid diversity
    • A. Shevchenko, and K. Simons Lipidomics: coming to grips with lipid diversity Nat. Rev. Mol. Cell Biol. 11 2010 593 598
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 593-598
    • Shevchenko, A.1    Simons, K.2
  • 202
    • 0023788823 scopus 로고
    • Lipid sorting in epithelial cells
    • K. Simons, and G. van Meer Lipid sorting in epithelial cells Biochemistry 27 1988 6197 6202
    • (1988) Biochemistry , vol.27 , pp. 6197-6202
    • Simons, K.1    Van Meer, G.2
  • 203
    • 0023671841 scopus 로고
    • Lipid polarity and sorting in epithelial cells
    • G. van Meer, and K. Simons Lipid polarity and sorting in epithelial cells J. Cell. Biochem. 36 1988 51 58
    • (1988) J. Cell. Biochem. , vol.36 , pp. 51-58
    • Van Meer, G.1    Simons, K.2
  • 204
    • 34247893965 scopus 로고    scopus 로고
    • What happens if cholesterol is made smoother: Importance of methyl substituents in cholesterol ring structure on phosphatidylcholine-sterol interaction
    • DOI 10.1529/biophysj.106.095497
    • T. Rog, M. Pasenkiewicz-Gierula, I. Vattulainen, and M. Karttunen What happens if cholesterol is made smoother: importance of methyl substituents in cholesterol ring structure on phosphatidylcholine-sterol interaction Biophys. J. 92 2007 3346 3357 (Pubitemid 46698629)
    • (2007) Biophysical Journal , vol.92 , Issue.10 , pp. 3346-3357
    • Rog, T.1    Pasenkiewicz-Gierula, M.2    Vattulainen, I.3    Karttunen, M.4
  • 205
    • 1842536499 scopus 로고    scopus 로고
    • Rafts: Scale-dependent, active lipid organization at the cell surface
    • DOI 10.1111/j.1600-0854.2004.00172.x
    • S. Mayor, and M. Rao Rafts; scale-dependent, active lipid organization at the cell surface Traffic 5 2004 231 240 (Pubitemid 38455746)
    • (2004) Traffic , vol.5 , Issue.4 , pp. 231-240
    • Mayor, S.1    Rao, M.2
  • 206
    • 33845901815 scopus 로고    scopus 로고
    • Lipid rafts: At a crossroad between cell biology and physics
    • DOI 10.1038/ncb0107-7, PII NCB0107-7
    • K. Jacobson, O.G. Mouritsen, and R.G.W. Anderson Lipid rafts: at a crossroad between cell biology and physics Nat. Cell Biol. 9 2007 7 14 (Pubitemid 46024188)
    • (2007) Nature Cell Biology , vol.9 , Issue.1 , pp. 7-14
    • Jacobson, K.1    Mouritsen, O.G.2    Anderson, R.G.W.3
  • 207
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • DOI 10.1038/42408
    • K. Simons, and E. Ikonen Functional rafts in cell membranes Nature 387 1997 569 572 (Pubitemid 27248754)
    • (1997) Nature , vol.387 , Issue.6633 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 208
    • 84865169456 scopus 로고    scopus 로고
    • The lipid raft hypothesis revisited: New insights on raft composition and function from super-resolution fluorescence microscopy
    • D.M. Owen, A. Magenau, D. Williamson, and K. Gaus The lipid raft hypothesis revisited: new insights on raft composition and function from super-resolution fluorescence microscopy Bioessays 34 2012 739 747
    • (2012) Bioessays , vol.34 , pp. 739-747
    • Owen, D.M.1    Magenau, A.2    Williamson, D.3    Gaus, K.4
  • 209
    • 66349087046 scopus 로고    scopus 로고
    • The challenge of lipid rafts
    • (Suppl.)
    • L. Pike The challenge of lipid rafts J. Lipid Res. 50 2009 S323 S328 (Suppl.)
    • (2009) J. Lipid Res. , vol.50
    • Pike, L.1
  • 210
    • 77957167810 scopus 로고    scopus 로고
    • Revitalizing membrane rafts: New tools and insights
    • K. Simons, and M.J. Gerl Revitalizing membrane rafts: new tools and insights Nat. Rev. 11 2010 688 699
    • (2010) Nat. Rev. , vol.11 , pp. 688-699
    • Simons, K.1    Gerl, M.J.2
  • 211
    • 35649010379 scopus 로고    scopus 로고
    • Lipid rafts, fluid/fluid phase separation, and their relevance to plasma membrane structure and function
    • DOI 10.1016/j.semcdb.2007.07.010, PII S1084952107001000, Membrane Lipid Microdomains: Roles in Signalling and Disease and 3D Chromatin
    • P. Sengupta, B. Baird, and D. Holowka Lipid rafts, fluid/fluid phase separation, and their relevance to plasma membrane structure and function Semin. Cell Dev. Biol. 18 2007 583 590 (Pubitemid 350026424)
    • (2007) Seminars in Cell and Developmental Biology , vol.18 , Issue.5 , pp. 583-590
    • Sengupta, P.1    Baird, B.2    Holowka, D.3
  • 212
    • 77955081952 scopus 로고    scopus 로고
    • Understanding lipid rafts and other related membrane domains, F1000
    • A.K. Neumann, M.S. Itano, and K. Jacobson Understanding lipid rafts and other related membrane domains, F1000 Biol. Reprod. 2 2010 31 36
    • (2010) Biol. Reprod. , vol.2 , pp. 31-36
    • Neumann, A.K.1    Itano, M.S.2    Jacobson, K.3
  • 213
    • 77956394811 scopus 로고    scopus 로고
    • A lipid matrix model of membrane raft structure
    • P.J. Quinn A lipid matrix model of membrane raft structure Prog. Lipid Res. 49 2010 390 406
    • (2010) Prog. Lipid Res. , vol.49 , pp. 390-406
    • Quinn, P.J.1
  • 214
    • 1842432088 scopus 로고    scopus 로고
    • Molecular dynamics and interactions for creation of stimulation-induced stabilized rafts from small unstable steady-state rafts
    • DOI 10.1111/j.1600-0854.2004.0178.x
    • A. Kusumi, I. Koyama-Honda, and K. Suzuki Molecular dynamics and interactions for creation of stimulation-induced stabilized rafts from small unstable steady-state rafts Traffic 5 2004 213 230 (Pubitemid 38455745)
    • (2004) Traffic , vol.5 , Issue.4 , pp. 213-230
    • Kusumi, A.1    Koyama-Honda, I.2    Suzuki, K.3
  • 215
  • 217
    • 0242268532 scopus 로고    scopus 로고
    • Lipid rafts and caveolae as portals for endocytosis: New insights and common mechanisms
    • DOI 10.1034/j.1600-0854.2003.00128.x
    • R.G. Parton, and A.A. Richards Lipid rafts and caveolae as portals for endocytosis: new insights and common mechanisms Traffic 4 2003 724 738 (Pubitemid 37361854)
    • (2003) Traffic , vol.4 , Issue.11 , pp. 724-738
    • Parton, R.G.1    Richards, A.A.2
  • 218
    • 77957373321 scopus 로고    scopus 로고
    • Quantitative understanding of cell signaling: The importance of membrane organization
    • K. Radhkrishnan, A. Halasz, D. Vlachos, and J.S. Edwards Quantitative understanding of cell signaling: the importance of membrane organization Curr. Opin. Biotechnol. 21 2010 677 682
    • (2010) Curr. Opin. Biotechnol. , vol.21 , pp. 677-682
    • Radhkrishnan, K.1    Halasz, A.2    Vlachos, D.3    Edwards, J.S.4
  • 219
    • 84861770491 scopus 로고    scopus 로고
    • Lipid rafts generate digital-like signal transduction in cell plasma membranes
    • K.G. Suzuki Lipid rafts generate digital-like signal transduction in cell plasma membranes Biotechnol. J. 7 2012 753 761
    • (2012) Biotechnol. J. , vol.7 , pp. 753-761
    • Suzuki, K.G.1
  • 221
    • 33746085241 scopus 로고    scopus 로고
    • Rafts defined: A report on the Keystone symposium on lipid rafts and cell function
    • DOI 10.1194/jlr.E600002-JLR200
    • L.J. Pike Rafts defined: a report on the Keystone symposium on lipid rafts and cell function J. Lipid Res. 47 2006 1597 1598 (Pubitemid 44079915)
    • (2006) Journal of Lipid Research , vol.47 , Issue.7 , pp. 1597-1598
    • Pike, L.J.1
  • 223
    • 1342306818 scopus 로고    scopus 로고
    • Nanoscale Organization of Multiple GPI-Anchored Proteins in Living Cell Membranes
    • DOI 10.1016/S0092-8674(04)00167-9
    • P. Sharma, R. Varma, R.C. Sarsij Ira, Ira, K. Gousett, G. Krishnamoorthy, M. Rao, and S. Mayor Nanoscale organization of multiple GPI-anchored proteins in living cell membranes Cell 20 2004 577 589 (Pubitemid 38264434)
    • (2004) Cell , vol.116 , Issue.4 , pp. 577-589
    • Sharma, P.1    Varma, R.2    Sarasij, R.C.3    Ira4    Gousset, K.5    Krishnamoorthy, G.6    Rao, M.7    Mayor, S.8
  • 225
    • 46749128544 scopus 로고    scopus 로고
    • Both MHC class II and its GPI-anchored form undergo hop diffusion as observed by single-molecule tracking
    • Y.M. Umemura, M. Vrjic, S.Y. Nishimura, T.K. Fujiwara, K.G. Suzuki, and A. Kusumi Both MHC class II and its GPI-anchored form undergo hop diffusion as observed by single-molecule tracking Biophys. J. 95 2008 435 450
    • (2008) Biophys. J. , vol.95 , pp. 435-450
    • Umemura, Y.M.1    Vrjic, M.2    Nishimura, S.Y.3    Fujiwara, T.K.4    Suzuki, K.G.5    Kusumi, A.6
  • 226
    • 33749544508 scopus 로고    scopus 로고
    • Transient anchorage of cross-linked glycosylphosphatidylinositol-anchored proteins depends on cholesterol, Src family kinases, caveolin, and phosphoinositides
    • DOI 10.1083/jcb.200512116
    • Y. Chen, W.R. Thelin, B. Yang, S.L. Milgram, and K. Jacobson Transient anchorage of cross-linked glycosyl-phosphatidylinositol-anchored proteins depends on cholesterol, Src family kinases, caveolin and phosphinositides J. Cell Biol. 175 2006 169 178 (Pubitemid 44537208)
    • (2006) Journal of Cell Biology , vol.175 , Issue.1 , pp. 169-178
    • Chen, Y.1    Thelin, W.R.2    Yang, B.3    Milgram, S.L.4    Jacobson, K.5
  • 227
    • 70450236974 scopus 로고    scopus 로고
    • The transmembrane protein CBP plays a role in transiently anchoring small clusters of Thy-1, a GPI-anchored protein, to the cytoskeleton
    • Y. Chen, L. Vercini, C. Benistant, and K. Jacobson The transmembrane protein CBP plays a role in transiently anchoring small clusters of Thy-1, a GPI-anchored protein, to the cytoskeleton J. Cell Sci. 122 2009 3966 3972
    • (2009) J. Cell Sci. , vol.122 , pp. 3966-3972
    • Chen, Y.1    Vercini, L.2    Benistant, C.3    Jacobson, K.4
  • 229
    • 58149235108 scopus 로고    scopus 로고
    • The superlattice model of lateral organization of membranes and its implications on membrane lipid homeostasis
    • P. Somerharju, J.A. Virtanen, K.H. Cheng, and M. Hermansson The superlattice model of lateral organization of membranes and its implications on membrane lipid homeostasis Biochim. Biophys. Acta 1788 2009 12 23
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 12-23
    • Somerharju, P.1    Virtanen, J.A.2    Cheng, K.H.3    Hermansson, M.4
  • 230
    • 84870540191 scopus 로고    scopus 로고
    • Correlative optical and scanning probe microscopes for mapping interactions at membranes
    • C.M. Yip Correlative optical and scanning probe microscopes for mapping interactions at membranes Meth. Mol. Biol. 950 2013 439 456
    • (2013) Meth. Mol. Biol. , vol.950 , pp. 439-456
    • Yip, C.M.1
  • 231
    • 0019802473 scopus 로고
    • Rotational diffusion of membrane proteins: Measurements with bacteriorhodopsin, band-3 proteins and erythrocyte oligosaccharides
    • R.J. Cherry Rotational diffusion of membrane proteins: measurements with bacteriorhodopsin, band-3 proteins and erythrocyte oligosaccharides Biochem. Soc. Symp. 46 1981 183 190 (Pubitemid 12151302)
    • (1981) Biochemical Society Symposia , vol.46 , pp. 183-190
    • Cherry, R.J.1
  • 232
    • 0019052777 scopus 로고
    • Anchorage of a band 3 population at the erythrocyte cytoplasmic membrane surface: Protein rotational diffusion measurements
    • E.A. Nigg, and R.J. Cherry Anchorage of a band 3 population at the erythrocyte cytoplasmic membrane surface: protein rotational diffusion measurements Proc. Natl. Acad. Sci. U. S. A. 77 1980 4702 4706
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 4702-4706
    • Nigg, E.A.1    Cherry, R.J.2
  • 233
    • 0023548717 scopus 로고
    • Lipid fluidity and membrane protein dynamics
    • G. Lenaz Lipid fluidity and membrane protein dynamics Biosci. Rep. 7 1987 823 837 (Pubitemid 18073276)
    • (1987) Bioscience Reports , vol.7 , Issue.11 , pp. 823-837
    • Lenaz, G.1
  • 234
    • 0020790863 scopus 로고
    • Membrane skeletal dynamics: Role in modulation of red cell deformability, mobility of transmembrane proteins, and shape
    • M.P. Sheetz Membrane skeletal dynamics: role in modulation of red cell deformability, mobility of transmembrane proteins, and shape Semin. Hematol. 20 1983 175 188
    • (1983) Semin. Hematol. , vol.20 , pp. 175-188
    • Sheetz, M.P.1
  • 236
    • 84862777193 scopus 로고    scopus 로고
    • The formation and stability of DC-SIGN microdomains require its extracellular moiety
    • P. Liu, X. Wang, M.S. Itano, A.K. Neumann, K. Jacobson, and N.L. Thompson The formation and stability of DC-SIGN microdomains require its extracellular moiety Traffic 13 2012 715 726
    • (2012) Traffic , vol.13 , pp. 715-726
    • Liu, P.1    Wang, X.2    Itano, M.S.3    Neumann, A.K.4    Jacobson, K.5    Thompson, N.L.6
  • 237
    • 79953730584 scopus 로고    scopus 로고
    • Detecting nanodomains in living cell membranes by fluorescence correlation spectroscopy
    • H.-T. He, and D. Marguet Detecting nanodomains in living cell membranes by fluorescence correlation spectroscopy Annu. Rev. Phys. Chem. 62 2011 417 436
    • (2011) Annu. Rev. Phys. Chem. , vol.62 , pp. 417-436
    • He, H.-T.1    Marguet, D.2
  • 238
    • 0027504198 scopus 로고
    • Confined lateral diffusion of membrane receptors as studied by single particle tracking (nanovid microscopy). Effects of calcium-induced differentiation in cultured epithelial cells
    • A. Kusumi, Y. Sako, and M. Yamamoto Confined lateral diffusion of membrane receptors as studied by single particle tracking (nanovid microscopy). Effects of calcium-induced differentiation in cultured epithelial cells Biophys. J. 65 1993 2021 2040 (Pubitemid 23334870)
    • (1993) Biophysical Journal , vol.65 , Issue.5 , pp. 2021-2040
    • Kusumi, A.1    Sako, Y.2    Yamamoto, M.3
  • 239
    • 0026539874 scopus 로고
    • Patches, posts and fences: Proteins and plasma membrane domains
    • M. Edidin Patches, posts and fences: proteins and plasma membrane domains Trends Cell Biol. 2 1992 376 380
    • (1992) Trends Cell Biol. , vol.2 , pp. 376-380
    • Edidin, M.1
  • 240
    • 0017154272 scopus 로고
    • The cancer cell: Dynamic aspects and modifications in cell-surface organization. Part 1
    • G.L. Nicolson, and G. Poste The cancer cell: dynamic aspects and modifications in cell-surface organization. Part 1 N. Engl. J. Med. 295 1976 197 203
    • (1976) N. Engl. J. Med. , vol.295 , pp. 197-203
    • Nicolson, G.L.1    Poste, G.2
  • 241
    • 0022966969 scopus 로고
    • Restriction of the lateral motion of band 3 in the erythrocyte membrane by the cytoskeletal network: Dependence on spectrin association state
    • DOI 10.1021/bi00368a045
    • A. Tsuji, and S. Ohnishi Restriction of the lateral motion of band 3 in the erythrocyte membrane by the cytoskeletal network: dependence on spectrin association state Biochemistry 25 1986 6133 6139 (Pubitemid 17204050)
    • (1986) Biochemistry , vol.25 , Issue.20 , pp. 6133-6139
    • Tsuji, A.1    Ohnishi, S.-I.2
  • 242
    • 0019304034 scopus 로고
    • Lateral mobility of integral membrane proteins is increased in spherocytic erythrocytes
    • M.P. Sheetz, M. Schlindler, and D.E. Koppel Lateral mobility of integral membrane proteins is increased in spherocytic erythrocytes Nature 285 1980 510 511
    • (1980) Nature , vol.285 , pp. 510-511
    • Sheetz, M.P.1    Schlindler, M.2    Koppel, D.E.3
  • 243
    • 0030222116 scopus 로고    scopus 로고
    • Cell surface organization by the membrane skeleton
    • DOI 10.1016/S0955-0674(96)80036-6
    • A. Kusumi, and Y. Sako Cell surface organization by the membrane skeleton Curr. Opin. Cell Biol. 8 1996 566 574 (Pubitemid 26254055)
    • (1996) Current Opinion in Cell Biology , vol.8 , Issue.4 , pp. 566-574
    • Kusumi, A.1    Sako, Y.2
  • 244
    • 65649122726 scopus 로고    scopus 로고
    • Lattices, rafts and scaffolds: Domain regulation of receptor signaling at the plasma membrane
    • P. Lajoie, J.G. Goetz, J.W. Dennis, and I.R. Nabi Lattices, rafts and scaffolds: domain regulation of receptor signaling at the plasma membrane J. Cell Biol. 185 2009 381 385
    • (2009) J. Cell Biol. , vol.185 , pp. 381-385
    • Lajoie, P.1    Goetz, J.G.2    Dennis, J.W.3    Nabi, I.R.4
  • 245
    • 77950460037 scopus 로고    scopus 로고
    • Spatial control of EGF receptor activation by reversible dimerization on living cells
    • I. Chung, R. Akita, R. Vandlen, D. Toomre, J. Schlessinger, and I. Mellman Spatial control of EGF receptor activation by reversible dimerization on living cells Nature 464 2009 783 787
    • (2009) Nature , vol.464 , pp. 783-787
    • Chung, I.1    Akita, R.2    Vandlen, R.3    Toomre, D.4    Schlessinger, J.5    Mellman, I.6
  • 246
    • 0024599261 scopus 로고
    • Lipid regulation of cell membane structure and function
    • P.L. Yeagle Lipid regulation of cell membrane structure and function FASEB J. 3 1989 1833 1842 (Pubitemid 19131783)
    • (1989) FASEB Journal , vol.3 , Issue.7 , pp. 1833-1842
    • Yeagle, P.L.1
  • 247
    • 30644466209 scopus 로고    scopus 로고
    • Membrane-lipid therapy: A new approach in molecular medicine
    • DOI 10.1016/j.molmed.2005.11.004, PII S1471491405002637
    • P.V. Escribá Membrane-lipid therapy: a new approach in molecular medicine Trends Mol. Med. 12 2006 34 43 (Pubitemid 43089654)
    • (2006) Trends in Molecular Medicine , vol.12 , Issue.1 , pp. 34-43
    • Escriba, P.V.1
  • 248
    • 84899439665 scopus 로고    scopus 로고
    • Lipid Replacement Therapy: A natural medicine approach to replacing damaged lipids in cellular membranes and organelles and restoring function
    • G.L. Nicolson, and M.E. Ash Lipid Replacement Therapy: a natural medicine approach to replacing damaged lipids in cellular membranes and organelles and restoring function Biochim. Biophys. Acta 1838 2014 1657 1679
    • (2014) Biochim. Biophys. Acta , vol.1838 , pp. 1657-1679
    • Nicolson, G.L.1    Ash, M.E.2


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