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Volumn 317, Issue , 2015, Pages 67-96

New Insights into the Organization of Plasma Membrane and Its Role in Signal Transduction

Author keywords

Actin; Clusters; Cytoskeleton; Diffusion; GPI anchored proteins; Rafts; Signaling; Single molecule imaging

Indexed keywords

ACTIN; CYTOSKELETON PROTEIN; DIMER; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; HOMODIMER; MEMBRANE RECEPTOR; OLIGOMER; MEMBRANE PROTEIN;

EID: 84925003660     PISSN: 19376448     EISSN: None     Source Type: Book Series    
DOI: 10.1016/bs.ircmb.2015.02.004     Document Type: Article
Times cited : (15)

References (137)
  • 1
    • 77649248897 scopus 로고    scopus 로고
    • Plasma membrane topography and interpretation of single-particle tracks
    • Adler J., Shevchuk A.I., Novak P., Korchev Y.E., Parmryd I. Plasma membrane topography and interpretation of single-particle tracks. Nat. Methods 2010, 7:170-171.
    • (2010) Nat. Methods , vol.7 , pp. 170-171
    • Adler, J.1    Shevchuk, A.I.2    Novak, P.3    Korchev, Y.E.4    Parmryd, I.5
  • 2
    • 0026658542 scopus 로고
    • Lateral diffusion and percolation in two-phase, two-component lipid bilayers. Topology of the solid-phase domains in-plane and across the lipid bilayer
    • Almeida P.F., Vaz W.L., Thompson T.E. Lateral diffusion and percolation in two-phase, two-component lipid bilayers. Topology of the solid-phase domains in-plane and across the lipid bilayer. Biochemistry 1992, 31:7198-7210.
    • (1992) Biochemistry , vol.31 , pp. 7198-7210
    • Almeida, P.F.1    Vaz, W.L.2    Thompson, T.E.3
  • 4
    • 0242331729 scopus 로고    scopus 로고
    • Imaging coexisting fluid domains in biomembrane models coupling curvature and line tension
    • Baumgart T., Hess S.T., Webb W.W. Imaging coexisting fluid domains in biomembrane models coupling curvature and line tension. Nature 2003, 425:821-824.
    • (2003) Nature , vol.425 , pp. 821-824
    • Baumgart, T.1    Hess, S.T.2    Webb, W.W.3
  • 5
    • 44949124597 scopus 로고    scopus 로고
    • Galectin-1 is a novel structural component and a major regulator of H-ras nanoclusters
    • Belanis L., Plowman S.J., Roblat B., Hancock J.F., Kloog Y. Galectin-1 is a novel structural component and a major regulator of H-ras nanoclusters. Mol. Biol. Cell 2008, 19:1404-1414.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1404-1414
    • Belanis, L.1    Plowman, S.J.2    Roblat, B.3    Hancock, J.F.4    Kloog, Y.5
  • 8
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown D.A., Rose J.K. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 1992, 68:533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 9
    • 1542379962 scopus 로고    scopus 로고
    • The membrane domains occupied by glycosylphosphatidylinositol-anchored prion protein and Thy-1 differ in lipid composition
    • Brugger B., Graham C., Leibrecht I., Mombelli E., Jen A., Wieland F., Morris R. The membrane domains occupied by glycosylphosphatidylinositol-anchored prion protein and Thy-1 differ in lipid composition. J. Biol. Chem. 2004, 279:7530-7536.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7530-7536
    • Brugger, B.1    Graham, C.2    Leibrecht, I.3    Mombelli, E.4    Jen, A.5    Wieland, F.6    Morris, R.7
  • 11
    • 84901992341 scopus 로고    scopus 로고
    • Direct visualization of the action of Triton X-100 on giant vesicles of erythrocyte membrane lipids
    • Casadei B.R., Domingues C.C., de Paula E., Riske K.A. Direct visualization of the action of Triton X-100 on giant vesicles of erythrocyte membrane lipids. Biophys. J. 2014, 106:2417-2425.
    • (2014) Biophys. J. , vol.106 , pp. 2417-2425
    • Casadei, B.R.1    Domingues, C.C.2    de Paula, E.3    Riske, K.A.4
  • 12
    • 33749544508 scopus 로고    scopus 로고
    • Transient anchorage of cross-linked glycosyl-phosphatidylinositol-anchored proteins depends on cholesterol, Src family kinases, caveolin, and phosphoinositides
    • Chen Y., Thelin W.R., Yang B., Milgram S.L., Jacobson K. Transient anchorage of cross-linked glycosyl-phosphatidylinositol-anchored proteins depends on cholesterol, Src family kinases, caveolin, and phosphoinositides. J. Cell Biol. 2006, 175:169-178.
    • (2006) J. Cell Biol. , vol.175 , pp. 169-178
    • Chen, Y.1    Thelin, W.R.2    Yang, B.3    Milgram, S.L.4    Jacobson, K.5
  • 13
    • 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
    • Chen Y., Veracini L., Benistant C., Jacobson K. 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. 2009, 122:3966-3972.
    • (2009) J. Cell Sci. , vol.122 , pp. 3966-3972
    • Chen, Y.1    Veracini, L.2    Benistant, C.3    Jacobson, K.4
  • 14
    • 77950460037 scopus 로고    scopus 로고
    • Spatial control of EGF receptor activation by reversible dimerization on living cells
    • Chung I., Akita R., Vandlen R., Toomre D., Schlessinger J., Mellman I. Spatial control of EGF receptor activation by reversible dimerization on living cells. Nature 2010, 464:783-787.
    • (2010) Nature , vol.464 , pp. 783-787
    • Chung, I.1    Akita, R.2    Vandlen, R.3    Toomre, D.4    Schlessinger, J.5    Mellman, I.6
  • 15
    • 33745758667 scopus 로고    scopus 로고
    • Lateral diffusion anisotropy and membrane lipid/skeleton interaction in outer hair cells
    • de Monvel J.B., Brownell W.E., Ulfendahl M. Lateral diffusion anisotropy and membrane lipid/skeleton interaction in outer hair cells. Biophys. J. 2006, 91:364-381.
    • (2006) Biophys. J. , vol.91 , pp. 364-381
    • de Monvel, J.B.1    Brownell, W.E.2    Ulfendahl, M.3
  • 17
    • 0035845497 scopus 로고    scopus 로고
    • Partitioning of Thy-1, GM1, and crosslinked phospholipid analogs into lipid rafts reconstituted in supported model membrane monolayers
    • Dietrich C., Volovyk Z.N., Levi M., Thompson N.L., Jacobson K. Partitioning of Thy-1, GM1, and crosslinked phospholipid analogs into lipid rafts reconstituted in supported model membrane monolayers. Proc. Natl. Acad. Sci. U.S.A. 2001, 98:10642-10647.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 10642-10647
    • Dietrich, C.1    Volovyk, Z.N.2    Levi, M.3    Thompson, N.L.4    Jacobson, K.5
  • 18
    • 0029310846 scopus 로고
    • Numerical simulations of the effect of hydrodynamic interactions on diffusivities of integral membrane proteins
    • Dodd T.L., Hammaer D.A., Sangani A.S., Koch D.L. Numerical simulations of the effect of hydrodynamic interactions on diffusivities of integral membrane proteins. J. Fluid Mech. 1995, 293:147-180.
    • (1995) J. Fluid Mech. , vol.293 , pp. 147-180
    • Dodd, T.L.1    Hammaer, D.A.2    Sangani, A.S.3    Koch, D.L.4
  • 19
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipid rafts: from model membranes to cells
    • Edidin M. The state of lipid rafts: from model membranes to cells. Annu. Rev. Biophys. Biomol. Struct. 2003, 32:257-283.
    • (2003) Annu. Rev. Biophys. Biomol. Struct. , vol.32 , pp. 257-283
    • Edidin, M.1
  • 21
    • 0032552072 scopus 로고    scopus 로고
    • Microdomains of GPI-anchored proteins in living cells revealed by crosslinking
    • Friedrichson T., Kurzchalia T.V. Microdomains of GPI-anchored proteins in living cells revealed by crosslinking. Nature 1998, 394:802-805.
    • (1998) Nature , vol.394 , pp. 802-805
    • Friedrichson, T.1    Kurzchalia, T.V.2
  • 22
    • 33847328318 scopus 로고    scopus 로고
    • Modulation of lateral diffusion in the plasma membrane by protein density
    • Frick M., Schmidt K., Nichols B.J. Modulation of lateral diffusion in the plasma membrane by protein density. Curr. Biol. 2007, 17:462-467.
    • (2007) Curr. Biol. , vol.17 , pp. 462-467
    • Frick, M.1    Schmidt, K.2    Nichols, B.J.3
  • 23
    • 34250368055 scopus 로고    scopus 로고
    • Ganglioside GM1 and GM3 on the living cell membrane form clusters susceptible to cholesterol depletion and chilling
    • Fujita A., Cheng J., Hirakawa M., Furukawa K., Kusunoki S., Fujimoto T. Ganglioside GM1 and GM3 on the living cell membrane form clusters susceptible to cholesterol depletion and chilling. Mol. Cell. Biol. 2007, 18:2112-2122.
    • (2007) Mol. Cell. Biol. , vol.18 , pp. 2112-2122
    • Fujita, A.1    Cheng, J.2    Hirakawa, M.3    Furukawa, K.4    Kusunoki, S.5    Fujimoto, T.6
  • 24
    • 0037054546 scopus 로고    scopus 로고
    • Phospholipids undergo hop diffusion in compartmentalized cell membrane
    • Fujiwara T., Ritchie K., Murakoshi H., Jacobson K., Kusumi A. Phospholipids undergo hop diffusion in compartmentalized cell membrane. J. Cell Biol. 2002, 157:1071-1081.
    • (2002) J. Cell Biol. , vol.157 , pp. 1071-1081
    • Fujiwara, T.1    Ritchie, K.2    Murakoshi, H.3    Jacobson, K.4    Kusumi, A.5
  • 26
    • 84908587487 scopus 로고    scopus 로고
    • Ligand binding alters dimerization and sequestering of urokinase receptors in raft-mimicking lipid mixtures
    • Ge Y., Siegel A.P., Jordan R., Naumann C.A. Ligand binding alters dimerization and sequestering of urokinase receptors in raft-mimicking lipid mixtures. Biophys. J. 2014, 107:2101-2111.
    • (2014) Biophys. J. , vol.107 , pp. 2101-2111
    • Ge, Y.1    Siegel, A.P.2    Jordan, R.3    Naumann, C.A.4
  • 29
    • 0035104119 scopus 로고    scopus 로고
    • LPS induction of gene expression in human monocytes
    • Guha M., Mackman N. LPS induction of gene expression in human monocytes. Cell Signal. 2001, 13:85-94.
    • (2001) Cell Signal. , vol.13 , pp. 85-94
    • Guha, M.1    Mackman, N.2
  • 30
    • 34548796570 scopus 로고    scopus 로고
    • Imaging and shape analysis of GUVs as model plasma membranes: effect of trans DOPC on membrane properties
    • Gudheti M.V., Mlodzianoski M., Hess S.T. Imaging and shape analysis of GUVs as model plasma membranes: effect of trans DOPC on membrane properties. Biophys. J. 2007, 93:2011-2023.
    • (2007) Biophys. J. , vol.93 , pp. 2011-2023
    • Gudheti, M.V.1    Mlodzianoski, M.2    Hess, S.T.3
  • 31
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder T., Scheiffele P., Verkade P., Simons K. Lipid domain structure of the plasma membrane revealed by patching of membrane components. J. Cell Biol. 1998, 141:929-942.
    • (1998) J. Cell Biol. , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 32
    • 0033033321 scopus 로고    scopus 로고
    • Clusters of glycolipid and glycosylphosphatidylinositol-anchored proteins in lymphoid cells: accumulation of actin regulation by local tyrosine phosphorylation
    • Harder T., Simons K. Clusters of glycolipid and glycosylphosphatidylinositol-anchored proteins in lymphoid cells: accumulation of actin regulation by local tyrosine phosphorylation. Eur. J. Immunol. 1999, 29:556-562.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 556-562
    • Harder, T.1    Simons, K.2
  • 33
    • 84892178225 scopus 로고    scopus 로고
    • Interaction of membrane/lipid rafts with the cytoskeleton: impact on signaling and function. Membrane/lipid rafts, mediators of cytoskeletal arrangement and cell signaling
    • Head B.P., Patel H.H., Insel P.A. Interaction of membrane/lipid rafts with the cytoskeleton: impact on signaling and function. Membrane/lipid rafts, mediators of cytoskeletal arrangement and cell signaling. Biochim. Biophys. Acta 2014, 1838:532-545.
    • (2014) Biochim. Biophys. Acta , vol.1838 , pp. 532-545
    • Head, B.P.1    Patel, H.H.2    Insel, P.A.3
  • 34
    • 0036841874 scopus 로고    scopus 로고
    • Triton promotes domain formation in lipid raft mixtures
    • Heerklotz H. Triton promotes domain formation in lipid raft mixtures. Biophys. J. 2002, 83:2693-2701.
    • (2002) Biophys. J. , vol.83 , pp. 2693-2701
    • Heerklotz, H.1
  • 39
    • 84922460988 scopus 로고    scopus 로고
    • Scanning STED-FCS reveals spatiotemporal heterogeneity of lipid interaction in the plasma membrane of living cells
    • Honigmann A., Mueller V., Ta H., Schoenle A., Sezgin E., Hell S.W., Eggeling C. Scanning STED-FCS reveals spatiotemporal heterogeneity of lipid interaction in the plasma membrane of living cells. Nat. Commun. 2014, 5:5412.
    • (2014) Nat. Commun. , vol.5 , pp. 5412
    • Honigmann, A.1    Mueller, V.2    Ta, H.3    Schoenle, A.4    Sezgin, E.5    Hell, S.W.6    Eggeling, C.7
  • 41
    • 33845901815 scopus 로고    scopus 로고
    • Lipid rafts: at a crossroad between cell biology and physics
    • Jacobson K., Mouristen O.G., Anderson R.G. Lipid rafts: at a crossroad between cell biology and physics. Nat. Cell Biol. 2007, 9:7-14.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 7-14
    • Jacobson, K.1    Mouristen, O.G.2    Anderson, R.G.3
  • 48
    • 0030713087 scopus 로고    scopus 로고
    • Erythrocyte membrane vesiculation: model for the molecular mechanism of protein sorting
    • Knowles D.W., Tilley L., Mohandas N., Chasis J.A. Erythrocyte membrane vesiculation: model for the molecular mechanism of protein sorting. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:12969-12974.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 12969-12974
    • Knowles, D.W.1    Tilley, L.2    Mohandas, N.3    Chasis, J.A.4
  • 49
    • 0033587719 scopus 로고    scopus 로고
    • Characterization of lipid bilayer phases by confocal microscopy and fluorescence correlation spectroscopy
    • Korlach J., Schwille P., Webb W.W., Feigenson G.W. Characterization of lipid bilayer phases by confocal microscopy and fluorescence correlation spectroscopy. Proc. Natl. Acad. Sci. U.S.A. 1999, 96:8461-8466.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 8461-8466
    • Korlach, J.1    Schwille, P.2    Webb, W.W.3    Feigenson, G.W.4
  • 50
    • 84870188756 scopus 로고    scopus 로고
    • Dynamic organization principles of the plasma membrane that regulate signal transduction: commemorating the fortieth anniversary of Singer and Nicolson's fluid-mosaic model
    • Kusumi A., Fujiwara T.K., Chadda R., Xie M., Tsunoyama T.A., Kalay Z., Kasai R.S., Suzuki K.G. Dynamic organization principles 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. 2012, 28:215-250.
    • (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
  • 51
    • 84862800913 scopus 로고    scopus 로고
    • Membrane mechanisms for signal transduction: the coupling of the meso-scale raft domains to membrane-skeleton-induced compartments and dynamic protein complexes
    • Kusumi A., Fujiwara T.K., Morone N., Yoshida K.J., Chadda R., Xie M., Kasai R.S., Suzuki K.G. Membrane mechanisms for signal transduction: the coupling of the meso-scale raft domains to membrane-skeleton-induced compartments and dynamic protein complexes. Semin. Cell Dev. Biol. 2012, 23:126-144.
    • (2012) Semin. Cell Dev. Biol. , vol.23 , pp. 126-144
    • Kusumi, A.1    Fujiwara, T.K.2    Morone, N.3    Yoshida, K.J.4    Chadda, R.5    Xie, M.6    Kasai, R.S.7    Suzuki, K.G.8
  • 52
    • 1842432088 scopus 로고    scopus 로고
    • Molecular dynamics and interactions for creation of stimulation-induced stabilized rafts from small unstable steady-state rafts
    • Kusumi A., Koyama-Honda I., Suzuki K. Molecular dynamics and interactions for creation of stimulation-induced stabilized rafts from small unstable steady-state rafts. Traffic 2004, 5:213-230.
    • (2004) Traffic , vol.5 , pp. 213-230
    • Kusumi, A.1    Koyama-Honda, I.2    Suzuki, K.3
  • 53
    • 17844364513 scopus 로고    scopus 로고
    • Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: high-speed single-molecule tracking of membrane molecules
    • Kusumi A., Nakada C., Richie K., Murase K., Suzuki K., Murakoshi H., Kasai R.S., Kondo J., Fujiwara T. Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: high-speed single-molecule tracking of membrane molecules. Annu. Rev. Biophys. Biomol. Struct. 2005, 34:351-378.
    • (2005) Annu. Rev. Biophys. Biomol. Struct. , vol.34 , pp. 351-378
    • Kusumi, A.1    Nakada, C.2    Richie, K.3    Murase, K.4    Suzuki, K.5    Murakoshi, H.6    Kasai, R.S.7    Kondo, J.8    Fujiwara, T.9
  • 54
    • 77951923713 scopus 로고    scopus 로고
    • Hierarchical organization of the plasma membrane: investigations by single-molecule tracking vs. fluorescence correlation spectroscopy
    • Kusumi A., Shirai Y.M., Koyama-Honda I., Suzuki K.G., Fujiwara T.K. Hierarchical organization of the plasma membrane: investigations by single-molecule tracking vs. fluorescence correlation spectroscopy. FEBS Lett. 2010, 584:1814-1823.
    • (2010) FEBS Lett. , vol.584 , pp. 1814-1823
    • Kusumi, A.1    Shirai, Y.M.2    Koyama-Honda, I.3    Suzuki, K.G.4    Fujiwara, T.K.5
  • 55
    • 29144483525 scopus 로고    scopus 로고
    • Toward understanding the dynamics of membrane-raft-based molecular interactions
    • Kusumi A., Suzuki K. Toward understanding the dynamics of membrane-raft-based molecular interactions. Biochim. Biophys. Acta 2005, 1746:234-251.
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 234-251
    • Kusumi, A.1    Suzuki, K.2
  • 57
    • 0032820709 scopus 로고    scopus 로고
    • Mobility and cytoskeletal interactions of cell adhesion receptors
    • Kusumi A., Suzuki K., Koyasako K. Mobility and cytoskeletal interactions of cell adhesion receptors. Curr. Opin. Cell Biol. 1999, 11:582-590.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 582-590
    • Kusumi, A.1    Suzuki, K.2    Koyasako, K.3
  • 58
    • 65649122726 scopus 로고    scopus 로고
    • Lattices, rafts, and scaffolds: domain regulation of receptor signaling at the plasma membrane
    • Lajoie P., Goetz J.G., Dennis J.W., Nabi I.R. Lattices, rafts, and scaffolds: domain regulation of receptor signaling at the plasma membrane. J. Cell Biol. 2009, 185:381-385.
    • (2009) J. Cell Biol. , vol.185 , pp. 381-385
    • Lajoie, P.1    Goetz, J.G.2    Dennis, J.W.3    Nabi, I.R.4
  • 61
    • 0019335162 scopus 로고
    • Cholesterol-phosphatidylcholine interactions in multilamellar vesicles
    • Lentz B.R., Barrow D.A., Hoechli M. Cholesterol-phosphatidylcholine interactions in multilamellar vesicles. Biochemistry 1980, 19:1943-1954.
    • (1980) Biochemistry , vol.19 , pp. 1943-1954
    • Lentz, B.R.1    Barrow, D.A.2    Hoechli, M.3
  • 62
    • 82255173996 scopus 로고    scopus 로고
    • Mysteries of the cell. Do lipid rafts exist?
    • Leslie M. Mysteries of the cell. Do lipid rafts exist?. Science 2011, 334:1046-1047.
    • (2011) Science , vol.334 , pp. 1046-1047
    • Leslie, M.1
  • 63
    • 79960972543 scopus 로고    scopus 로고
    • Raft domains of variable properties and compositions in plasma membrane vesicles
    • Levental I., Grzybek M., Simons K. Raft domains of variable properties and compositions in plasma membrane vesicles. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:11411-11416.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 11411-11416
    • Levental, I.1    Grzybek, M.2    Simons, K.3
  • 65
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood D., Simons K. Lipid rafts as a membrane-organizing principle. Science 2010, 327:46-50.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 66
    • 0029795505 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate binding to the pleckstrin homology domain of phospholipase C-δ1 enhances enzyme activity
    • Lomasney J.W., Cheng H.-F., Wang L.P., Kuan Y.S., Liu S.M., Feslk S.W., King K. Phosphatidylinositol 4,5-bisphosphate binding to the pleckstrin homology domain of phospholipase C-δ1 enhances enzyme activity. J. Biol. Chem. 1996, 271:25316-25326.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25316-25326
    • Lomasney, J.W.1    Cheng, H.-F.2    Wang, L.P.3    Kuan, Y.S.4    Liu, S.M.5    Feslk, S.W.6    King, K.7
  • 67
    • 33746725960 scopus 로고    scopus 로고
    • Single-molecule diffusion reveals similar mobility for the Lck. H-ras, and K-ras membrane anchors
    • Lommerse P.H., Vastenhoud K., Pririnen N.J., Magee A.I., Spaink H.P., Schmidt T. Single-molecule diffusion reveals similar mobility for the Lck. H-ras, and K-ras membrane anchors. Biophys. J. 2006, 91:1090-1097.
    • (2006) Biophys. J. , vol.91 , pp. 1090-1097
    • Lommerse, P.H.1    Vastenhoud, K.2    Pririnen, N.J.3    Magee, A.I.4    Spaink, H.P.5    Schmidt, T.6
  • 68
    • 0034707082 scopus 로고    scopus 로고
    • Insolubility of lipids in triton X-100 physical origin and relationship to sphingolipid/cholesterol membrane domains (rafts)
    • London E., Brown D.A. Insolubility of lipids in triton X-100 physical origin and relationship to sphingolipid/cholesterol membrane domains (rafts). Biochim. Biophys. Acta 2000, 1508:182-195.
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 182-195
    • London, E.1    Brown, D.A.2
  • 70
    • 0026597941 scopus 로고
    • Thy-1 multimerization is correlated with neurite outgrowth
    • Mahanthappa N.K., Patterson P.H. Thy-1 multimerization is correlated with neurite outgrowth. Dev. Biol. 1992, 150:60-71.
    • (1992) Dev. Biol. , vol.150 , pp. 60-71
    • Mahanthappa, N.K.1    Patterson, P.H.2
  • 72
    • 33748579946 scopus 로고    scopus 로고
    • Three-dimensional reconstitution of the membrane skeleton at the plasma membrane interface by electron tomography
    • Morone N., Fujiwara T., Murase K., Kasai R.S., Ike H., Yuasa S., Usukura J., Kusumi A. Three-dimensional reconstitution of the membrane skeleton at the plasma membrane interface by electron tomography. J. Cell. Biol. 2006, 174:851-862.
    • (2006) J. Cell. Biol. , vol.174 , pp. 851-862
    • Morone, N.1    Fujiwara, T.2    Murase, K.3    Kasai, R.S.4    Ike, H.5    Yuasa, S.6    Usukura, J.7    Kusumi, A.8
  • 73
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: elusive or illusive?
    • Munro S. Lipid rafts: elusive or illusive?. Cell 2003, 115:377-388.
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 75
    • 57349169377 scopus 로고    scopus 로고
    • Design of quantum dot-conjugated lipids for long-term, high-speed tracking experiments on cell surfaces
    • Murcia M.J., Minner D.E., Mustata G.M., Ritchie K., Naumann C.A. Design of quantum dot-conjugated lipids for long-term, high-speed tracking experiments on cell surfaces. J. Am. Chem. Soc. 2008, 130:15054-15062.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 15054-15062
    • Murcia, M.J.1    Minner, D.E.2    Mustata, G.M.3    Ritchie, K.4    Naumann, C.A.5
  • 77
    • 84899444997 scopus 로고    scopus 로고
    • The fluid-mosaic model of membrane structure: still relevant to understanding the structure, function and dynamics of biological membranes after more than 40 years
    • Nicolson G.L. The fluid-mosaic model of membrane structure: still relevant to understanding the structure, function and dynamics of biological membranes after more than 40 years. Biochim. Biophys. Acta 2014, 1838:1451-1486.
    • (2014) Biochim. Biophys. Acta , vol.1838 , pp. 1451-1486
    • Nicolson, G.L.1
  • 79
    • 77953011323 scopus 로고    scopus 로고
    • Phase separation of lipid microdomains controlled by polymerized lipid bilayer matrices
    • Okazaki T., Tatsu Y., Morigaki K. Phase separation of lipid microdomains controlled by polymerized lipid bilayer matrices. Langmuir 2010, 26:4126-4129.
    • (2010) Langmuir , vol.26 , pp. 4126-4129
    • Okazaki, T.1    Tatsu, Y.2    Morigaki, K.3
  • 80
    • 77955478311 scopus 로고    scopus 로고
    • CaMKII triggers the diffusional trapping of surface AMPARs through phosphorylation of stargazing
    • Opazo P., Labrecque S., Tigaret C.M., Frouin A., Wiseman P.W., De Koninck P., Choquet D. CaMKII triggers the diffusional trapping of surface AMPARs through phosphorylation of stargazing. Neuron 2010, 67:239-252.
    • (2010) Neuron , vol.67 , pp. 239-252
    • Opazo, P.1    Labrecque, S.2    Tigaret, C.M.3    Frouin, A.4    Wiseman, P.W.5    De Koninck, P.6    Choquet, D.7
  • 81
    • 84871789466 scopus 로고    scopus 로고
    • Sub-resolution lipid domains exist in the plasma membrane and regulate protein diffusion and distribution
    • Owen D.M., Williamson D.J., Mahenau A., Gaus K. Sub-resolution lipid domains exist in the plasma membrane and regulate protein diffusion and distribution. Nat. Commun. 2012, 3:1256.
    • (2012) Nat. Commun. , vol.3 , pp. 1256
    • Owen, D.M.1    Williamson, D.J.2    Mahenau, A.3    Gaus, K.4
  • 83
    • 9444267662 scopus 로고    scopus 로고
    • Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins
    • Paladino S., Samataro D., Pillich R., Tivodar S., Nitsch L., Zurzolo C. Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins. J. Cell Biol. 2004, 167:699-709.
    • (2004) J. Cell Biol. , vol.167 , pp. 699-709
    • Paladino, S.1    Samataro, D.2    Pillich, R.3    Tivodar, S.4    Nitsch, L.5    Zurzolo, C.6
  • 84
    • 0012050693 scopus 로고
    • Lateral and rotational diffusion of bacteriorhodopsin in lipid bilayers: experimental test of the Saffman-Delbruck equations
    • Peters R., Cherry R.J. Lateral and rotational diffusion of bacteriorhodopsin in lipid bilayers: experimental test of the Saffman-Delbruck equations. Proc. Natl. Acad. Sci. U.S.A. 1982, 79:4317-4321.
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 4317-4321
    • Peters, R.1    Cherry, R.J.2
  • 85
    • 84890835535 scopus 로고    scopus 로고
    • Spectroscopic techniques for monitoring protein interactions in living cells
    • Piehler J. Spectroscopic techniques for monitoring protein interactions in living cells. Curr. Opin. Struct. Biol. 2014, 24:54-62.
    • (2014) Curr. Opin. Struct. Biol. , vol.24 , pp. 54-62
    • Piehler, J.1
  • 86
    • 47949104726 scopus 로고    scopus 로고
    • Stress-protective signaling of prion protein is corrupted by scrapie prions
    • Rambold A.S., Muller V., Ron U., Ben-Tal N., Winklhofer K.F., Tatzelt J. Stress-protective signaling of prion protein is corrupted by scrapie prions. EMBO J. 2008, 27:1974-1984.
    • (2008) EMBO J. , vol.27 , pp. 1974-1984
    • Rambold, A.S.1    Muller, V.2    Ron, U.3    Ben-Tal, N.4    Winklhofer, K.F.5    Tatzelt, J.6
  • 87
    • 84928025198 scopus 로고    scopus 로고
    • C signaling and processing by dimerization
    • C signaling and processing by dimerization. Front. Cell Dev. Biol. 2014, 2:57.
    • (2014) Front. Cell Dev. Biol. , vol.2 , pp. 57
    • Roucou, X.1
  • 90
    • 18544376071 scopus 로고    scopus 로고
    • Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth
    • Santuccione A., Sytnyk V., Leshchyns'ka I., Schachner M. Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth. J. Cell Biol. 2005, 169:341-354.
    • (2005) J. Cell Biol. , vol.169 , pp. 341-354
    • Santuccione, A.1    Sytnyk, V.2    Leshchyns'ka, I.3    Schachner, M.4
  • 91
    • 0025084901 scopus 로고
    • Lateral diffusion in a mixture of mobile and immobile particles. A monte-Carlo study
    • Saxton M.J. Lateral diffusion in a mixture of mobile and immobile particles. A monte-Carlo study. Biophys. J. 1990, 58:1303-1306.
    • (1990) Biophys. J. , vol.58 , pp. 1303-1306
    • Saxton, M.J.1
  • 92
    • 33846844797 scopus 로고    scopus 로고
    • A biological interpretation of transient anomalous subdiffusion. I. Qualitative model
    • Saxton M.J. A biological interpretation of transient anomalous subdiffusion. I. Qualitative model. Biophys. J. 2007, 92:1178-1191.
    • (2007) Biophys. J. , vol.92 , pp. 1178-1191
    • Saxton, M.J.1
  • 93
    • 84873862003 scopus 로고    scopus 로고
    • Steric pressure between membrane-bound proteins opposes lipid phase separation
    • Scheve C.S., Gonzales P.A., Momin N., Stachowiak J.C. Steric pressure between membrane-bound proteins opposes lipid phase separation. J. Am. Chem. Soc. 2013, 135:1185-1188.
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 1185-1188
    • Scheve, C.S.1    Gonzales, P.A.2    Momin, N.3    Stachowiak, J.C.4
  • 94
    • 47749109057 scopus 로고    scopus 로고
    • Equinatoxin II permeabilizing activity depends on the presence of sphingomyelin and lipid phase coexistence
    • Schon P., Garcia-Saez A.J., Malovrh P., Bacia K., Anderluh G., Schwille P. Equinatoxin II permeabilizing activity depends on the presence of sphingomyelin and lipid phase coexistence. Biophys. J. 2008, 95:691-698.
    • (2008) Biophys. J. , vol.95 , pp. 691-698
    • Schon, P.1    Garcia-Saez, A.J.2    Malovrh, P.3    Bacia, K.4    Anderluh, G.5    Schwille, P.6
  • 95
    • 0031964607 scopus 로고    scopus 로고
    • Cholesterol and sphingolipid enhance the triton x-100 insolubility of glycosylphosphatidylinositol-anchored proteins by promoting the formation of detergent-insoluble ordered membrane domains
    • Schroeder R.J., Ahmed S.N., Zhu Y., London E., Brown D.A. Cholesterol and sphingolipid enhance the triton x-100 insolubility of glycosylphosphatidylinositol-anchored proteins by promoting the formation of detergent-insoluble ordered membrane domains. J. Biol. Chem. 1998, 273:1150-1157.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1150-1157
    • Schroeder, R.J.1    Ahmed, S.N.2    Zhu, Y.3    London, E.4    Brown, D.A.5
  • 96
    • 38149122245 scopus 로고    scopus 로고
    • Structural determinants for partitioning of lipids and proteins between coexisting fluid phases in giant plasma membrane vesicles
    • Sengupta P., Hammond A., Holowka D., Baird B. Structural determinants for partitioning of lipids and proteins between coexisting fluid phases in giant plasma membrane vesicles. Biochim. Biophys. Acta 2008, 1778:20-32.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 20-32
    • Sengupta, P.1    Hammond, A.2    Holowka, D.3    Baird, B.4
  • 98
    • 84875846566 scopus 로고    scopus 로고
    • Implications of lipid moiety in oligomerization and immunoreactivities of GPI-anchored proteins
    • Seong J., Wang Y., Kinoshita T., Maeda Y. Implications of lipid moiety in oligomerization and immunoreactivities of GPI-anchored proteins. J. Lipid Res. 2013, 54:1077-1091.
    • (2013) J. Lipid Res. , vol.54 , pp. 1077-1091
    • Seong, J.1    Wang, Y.2    Kinoshita, T.3    Maeda, Y.4
  • 99
    • 84861079568 scopus 로고    scopus 로고
    • Elucidating membrane structure and protein behavior using giant plasma membrane vesicles
    • Sezgin E., Kaiser H.J., Baumgart T., Schiwille P., Simons K., Levental I. Elucidating membrane structure and protein behavior using giant plasma membrane vesicles. Nat. Protoc. 2011, 7:1042-1051.
    • (2011) Nat. Protoc. , vol.7 , pp. 1042-1051
    • Sezgin, E.1    Kaiser, H.J.2    Baumgart, T.3    Schiwille, P.4    Simons, K.5    Levental, I.6
  • 101
    • 1342306818 scopus 로고    scopus 로고
    • Nanoscale organization of multiple GPI-anchored proteins in living cell membranes
    • Sharma P., Varma R., Sarasij R.C., Ira, Gousset K., Krishnamoorthy G., Rao M., Mayor S. Nanoscale organization of multiple GPI-anchored proteins in living cell membranes. Cell 2004, 116:577-589.
    • (2004) Cell , vol.116 , pp. 577-589
    • Sharma, P.1    Varma, R.2    Sarasij, R.C.3    Ira, G.K.4    Krishnamoorthy, G.5    Rao, M.6    Mayor, S.7
  • 102
    • 0020790863 scopus 로고
    • Membrane skeletal dynamics: role in modulation of red cell deformability, mobility of transmembrane proteins, and shape
    • Sheetz M.P. Membrane skeletal dynamics: role in modulation of red cell deformability, mobility of transmembrane proteins, and shape. Semin. Hematol. 1983, 20:175-188.
    • (1983) Semin. Hematol. , vol.20 , pp. 175-188
    • Sheetz, M.P.1
  • 103
    • 0029906007 scopus 로고    scopus 로고
    • Cholesterol at different bilayer concentrations can promote or antagonize lateral segregation of phospholipids of differing acyl chain length
    • Silvius J.R., del Giudice D., Lafleur M. Cholesterol at different bilayer concentrations can promote or antagonize lateral segregation of phospholipids of differing acyl chain length. Biochemistry 1996, 35:15198-15208.
    • (1996) Biochemistry , vol.35 , pp. 15198-15208
    • Silvius, J.R.1    del Giudice, D.2    Lafleur, M.3
  • 104
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., Ikonen E. Functional rafts in cell membranes. Nature 1997, 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 106
    • 0023788823 scopus 로고
    • Lipid sorting in epithelial cells
    • Simons K., van Meer G. Lipid sorting in epithelial cells. Biochemistry 1988, 27:6197-6202.
    • (1988) Biochemistry , vol.27 , pp. 6197-6202
    • Simons, K.1    van Meer, G.2
  • 108
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer S.J., Nicolson G.L. The fluid mosaic model of the structure of cell membranes. Science 1972, 175:720-731.
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 109
    • 84861770491 scopus 로고    scopus 로고
    • Lipid rafts generate digital-like signal transduction in cell plasma membranes
    • Suzuki K.G.N. Lipid rafts generate digital-like signal transduction in cell plasma membranes. Biotechnol. J. 2012, 7:753-761.
    • (2012) Biotechnol. J. , vol.7 , pp. 753-761
    • Suzuki, K.G.N.1
  • 110
    • 34249066421 scopus 로고    scopus 로고
    • GPI-anchored receptor clusters transiently recruit Lyn and Gα for temporary cluster immobilization and Lyn activation: single-molecule tracking study 1
    • Suzuki K.G.N., Fujiwara T.K., Sanematsu F., Iino R., Edidin M., Kusumi A. GPI-anchored receptor clusters transiently recruit Lyn and Gα for temporary cluster immobilization and Lyn activation: single-molecule tracking study 1. J. Cell Biol. 2007, 177:717-730.
    • (2007) J. Cell Biol. , vol.177 , pp. 717-730
    • Suzuki, K.G.N.1    Fujiwara, T.K.2    Sanematsu, F.3    Iino, R.4    Edidin, M.5    Kusumi, A.6
  • 114
    • 0034622520 scopus 로고    scopus 로고
    • GPI-anchored proteins do not transfer spontaneously from erythrocytes to liposomes. New aspects of reorganization of the cell membrane
    • Suzuki K., Okumura Y. GPI-anchored proteins do not transfer spontaneously from erythrocytes to liposomes. New aspects of reorganization of the cell membrane. Biochemistry 2000, 39:9477-9485.
    • (2000) Biochemistry , vol.39 , pp. 9477-9485
    • Suzuki, K.1    Okumura, Y.2
  • 115
    • 17844389341 scopus 로고    scopus 로고
    • Rapid hop diffusion of a G-protein-coupled receptor in the plasma membrane as revealed by single-molecule techniques
    • Suzuki K., Ricthie K., Kajikawa E., Fujiwara T., Kusumi A. Rapid hop diffusion of a G-protein-coupled receptor in the plasma membrane as revealed by single-molecule techniques. Biophys. J. 2005, 88:3659-3680.
    • (2005) Biophys. J. , vol.88 , pp. 3659-3680
    • Suzuki, K.1    Ricthie, K.2    Kajikawa, E.3    Fujiwara, T.4    Kusumi, A.5
  • 116
    • 0034805172 scopus 로고    scopus 로고
    • Binding of cross-linking glycosylphosphatidylinositol-anchored proteins to discrete actin-associated sites and cholesterol-dependent domains
    • Suzuki K., Sheetz M.P. Binding of cross-linking glycosylphosphatidylinositol-anchored proteins to discrete actin-associated sites and cholesterol-dependent domains. Biophys. J. 2001, 81:2181-2189.
    • (2001) Biophys. J. , vol.81 , pp. 2181-2189
    • Suzuki, K.1    Sheetz, M.P.2
  • 117
    • 0033945750 scopus 로고    scopus 로고
    • Outer membrane monolayer domains from two-dimensional surface scanning resistance measurements
    • Suzuki K., Sterba R.E., Sheetz M.P. Outer membrane monolayer domains from two-dimensional surface scanning resistance measurements. Biophys. J. 2000, 79:448-459.
    • (2000) Biophys. J. , vol.79 , pp. 448-459
    • Suzuki, K.1    Sterba, R.E.2    Sheetz, M.P.3
  • 119
    • 0033625038 scopus 로고    scopus 로고
    • GFRα-mediated localization of RET to lipid rafts is required for effective downstream signaling, differentiation, and neuronal survival
    • Tansey M.G., Baloh R.H., Milbrandt J., Johnson E.M. GFRα-mediated localization of RET to lipid rafts is required for effective downstream signaling, differentiation, and neuronal survival. Neuron 2000, 25:611-623.
    • (2000) Neuron , vol.25 , pp. 611-623
    • Tansey, M.G.1    Baloh, R.H.2    Milbrandt, J.3    Johnson, E.M.4
  • 120
    • 33750533178 scopus 로고    scopus 로고
    • CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse
    • Tavano R., Contento R., Baranda S.J., Soligo M., Tuosto L., Manes S., Viola A. CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse. Nat. Cell Biol. 2006, 8:1270-1276.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1270-1276
    • Tavano, R.1    Contento, R.2    Baranda, S.J.3    Soligo, M.4    Tuosto, L.5    Manes, S.6    Viola, A.7
  • 122
    • 0028360654 scopus 로고
    • The mode of anchorage to the cell surface determines both the function and the membrane location of Thy-1 glycoprotein
    • Tiveron M.C., Nosten-Bertrand M., Jani H., Gamett D., Hirst E.M., Grosveid F., Morris R.J. The mode of anchorage to the cell surface determines both the function and the membrane location of Thy-1 glycoprotein. J. Cell Sci. 1994, 107:1783-1796.
    • (1994) J. Cell Sci. , vol.107 , pp. 1783-1796
    • Tiveron, M.C.1    Nosten-Bertrand, M.2    Jani, H.3    Gamett, D.4    Hirst, E.M.5    Grosveid, F.6    Morris, R.J.7
  • 123
    • 0032563615 scopus 로고    scopus 로고
    • Regulation mechanism of the lateral diffusion of band 3 in erythrocyte membranes by the membrane skeleton
    • Tomishige M., Sako Y., Kusumi A. Regulation mechanism of the lateral diffusion of band 3 in erythrocyte membranes by the membrane skeleton. J. Cell Biol. 1998, 142:989-1000.
    • (1998) J. Cell Biol. , vol.142 , pp. 989-1000
    • Tomishige, M.1    Sako, Y.2    Kusumi, A.3
  • 124
    • 46749128544 scopus 로고    scopus 로고
    • Both MHC class II and its GPI-anchored form undergo hop diffusion as observed by single-molecule tracking
    • Umemura Y.M., Vrljic M., Nishimura S.Y., Fujiwara T.K., Suzuki K.G., Kusumi A. Both MHC class II and its GPI-anchored form undergo hop diffusion as observed by single-molecule tracking. Biophys. J. 2008, 95:435-450.
    • (2008) Biophys. J. , vol.95 , pp. 435-450
    • Umemura, Y.M.1    Vrljic, M.2    Nishimura, S.Y.3    Fujiwara, T.K.4    Suzuki, K.G.5    Kusumi, A.6
  • 125
    • 0023671841 scopus 로고
    • Lipid polarity and sorting in epithelial cells
    • van Meer G., Simons K. Lipid polarity and sorting in epithelial cells. J. Cell. Biochem. 1988, 36:51-58.
    • (1988) J. Cell. Biochem. , vol.36 , pp. 51-58
    • van Meer, G.1    Simons, K.2
  • 128
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma R., Mayor S. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 1998, 20:798-801.
    • (1998) Nature , vol.20 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 130
    • 18144386926 scopus 로고    scopus 로고
    • Miscibility phase diagrams of giant vesicles containing sphingomyelin
    • Veatch S.L., Keller S.L. Miscibility phase diagrams of giant vesicles containing sphingomyelin. Phys. Rev. Lett. 2005, 94:148101.
    • (2005) Phys. Rev. Lett. , vol.94 , pp. 148101
    • Veatch, S.L.1    Keller, S.L.2
  • 131
  • 132
    • 11244339619 scopus 로고    scopus 로고
    • Cholesterol depletion suppresses the translational diffusion of class II major histocompatibility complex proteins in the plasma membrane
    • Vrljic M., Nishimura S.Y., Moerner W.E., McConnell H.M. Cholesterol depletion suppresses the translational diffusion of class II major histocompatibility complex proteins in the plasma membrane. Biophys. J. 2005, 88:334-347.
    • (2005) Biophys. J. , vol.88 , pp. 334-347
    • Vrljic, M.1    Nishimura, S.Y.2    Moerner, W.E.3    McConnell, H.M.4
  • 133
    • 79953223640 scopus 로고    scopus 로고
    • Partitioning of synaptotagmin I C2 domains between liquid-ordered and liquid disordered inner leaflet lipid phases
    • Wan C., Kiessling V., Cafiso D.S., Tamm L.K. Partitioning of synaptotagmin I C2 domains between liquid-ordered and liquid disordered inner leaflet lipid phases. Biochemistry 2011, 50:2478-2485.
    • (2011) Biochemistry , vol.50 , pp. 2478-2485
    • Wan, C.1    Kiessling, V.2    Cafiso, D.S.3    Tamm, L.K.4
  • 134
    • 0033602098 scopus 로고    scopus 로고
    • A diffusion barrier maintains distribution of membrane proteins in polarized neurons
    • Wickler B., Forschner P., Mellman I. A diffusion barrier maintains distribution of membrane proteins in polarized neurons. Nature 1999, 397:698-701.
    • (1999) Nature , vol.397 , pp. 698-701
    • Wickler, B.1    Forschner, P.2    Mellman, I.3
  • 135
    • 0034931126 scopus 로고    scopus 로고
    • Three-dimensional structures of prion proteins
    • Wuthrich K., Riek R. Three-dimensional structures of prion proteins. Ad. Protein Chem. 2001, 57:55-82.
    • (2001) Ad. Protein Chem. , vol.57 , pp. 55-82
    • Wuthrich, K.1    Riek, R.2
  • 136
    • 0031042904 scopus 로고    scopus 로고
    • 2+ differentially regulates the ligand-affinity states of type 1 and type 3 inositol 1,4,5-triphosphate receptors
    • 2+ differentially regulates the ligand-affinity states of type 1 and type 3 inositol 1,4,5-triphosphate receptors. Biochem. J. 1997, 322:591-596.
    • (1997) Biochem. J. , vol.322 , pp. 591-596
    • Yoneshima, H.1    Miyawaki, A.2    Michikawa, T.3    Furuichi, T.4    Mikoshiba, K.5
  • 137
    • 40449112970 scopus 로고    scopus 로고
    • Intracellular water-specific MR of microbead-adherent cells: the HeLa cell intracellular water exchange lifetime
    • Zhao L., Kroenke C.D., Song J., Piwnica-Worms D., Ackerman J.J., Neil J.J. Intracellular water-specific MR of microbead-adherent cells: the HeLa cell intracellular water exchange lifetime. NMR Biomed. 2008, 21:159-164.
    • (2008) NMR Biomed. , vol.21 , pp. 159-164
    • Zhao, L.1    Kroenke, C.D.2    Song, J.3    Piwnica-Worms, D.4    Ackerman, J.J.5    Neil, J.J.6


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