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Volumn 61, Issue 2, 2004, Pages 105-116

Raft and cytoskeleton associations of an ABC transporter: P-glycoprotein

Author keywords

Actin cytoskeleton; Adenosine triphosphate binding cassette 1; Detergent resistance; Fab fragment; Flow cytometry; Fluorescence resonance energy transfer; LS 174 T colon carcinoma cell; MDR1; P glycoprotein; Raft; UIC2 monoclonal antibody

Indexed keywords

ABC TRANSPORTER; ACTIN; CD59 ANTIGEN; CHOLESTEROL; CYTOSKELETON PROTEIN; DETERGENT; GANGLIOSIDE GM1; GLYCOPROTEIN P; HERMES ANTIGEN; MONOCLONAL ANTIBODY;

EID: 5444271640     PISSN: 15524922     EISSN: None     Source Type: Journal    
DOI: 10.1002/cyto.a.20081     Document Type: Article
Times cited : (81)

References (66)
  • 1
    • 0027218689 scopus 로고
    • Biochemistry of multidrug resistance mediated by the multidrug transporter
    • Gottesman MM, Pastan I. Biochemistry of multidrug resistance mediated by the multidrug transporter. Annu Rev Biochem 1993;62:385-427.
    • (1993) Annu Rev Biochem , vol.62 , pp. 385-427
    • Gottesman, M.M.1    Pastan, I.2
  • 2
    • 0036074018 scopus 로고    scopus 로고
    • Mammalian ABC transporters in health and disease
    • Borst P, Elferink RO. Mammalian ABC transporters in health and disease. Annu Rev Biochem 2002;71:537-592.
    • (2002) Annu Rev Biochem , vol.71 , pp. 537-592
    • Borst, P.1    Elferink, R.O.2
  • 3
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker JE, Saraste M, Runswick MJ, Gay NJ. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1982;1:945-951.
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 5
    • 0007544439 scopus 로고    scopus 로고
    • MDR1 P-glycoprotein is a lipid translocase of broad specificity, while MDR3 P-glycoprotein specifically translocates phosphatidylcholine
    • van Helvoort A, Smith AJ, Sprong H, Fritzsche I, Schinkel AH, Borst P, van Meer G. MDR1 P-glycoprotein is a lipid translocase of broad specificity, while MDR3 P-glycoprotein specifically translocates phosphatidylcholine. Cell 1996;87:507-517.
    • (1996) Cell , vol.87 , pp. 507-517
    • Van Helvoort, A.1    Smith, A.J.2    Sprong, H.3    Fritzsche, I.4    Schinkel, A.H.5    Borst, P.6    Van Meer, G.7
  • 7
    • 0033958086 scopus 로고    scopus 로고
    • Multiple physiological functions for multidrug transporter P-glycoprotein?
    • Johnstone RW, Ruefli AA, Smyth MJ. Multiple physiological functions for multidrug transporter P-glycoprotein? Trends Biochem Sci 2000;25:1-6.
    • (2000) Trends Biochem Sci , vol.25 , pp. 1-6
    • Johnstone, R.W.1    Ruefli, A.A.2    Smyth, M.J.3
  • 8
    • 0346243995 scopus 로고    scopus 로고
    • Analysis of P-glycoprotein-mediated membrane transport in human peripheral blood lymphocytes using the UIC2 shift assay
    • Park SW, Lomri N, Simeoni LA, Fruehauf JP, Mechetner E. Analysis of P-glycoprotein-mediated membrane transport in human peripheral blood lymphocytes using the UIC2 shift assay. Cytometry 2003;53A:67-78.
    • (2003) Cytometry , vol.53 A , pp. 67-78
    • Park, S.W.1    Lomri, N.2    Simeoni, L.A.3    Fruehauf, J.P.4    Mechetner, E.5
  • 9
    • 0036678454 scopus 로고    scopus 로고
    • The multidrug transporter, P-glycoprotein, actively mediates cholesterol redistribution in the cell membrane
    • Garrigues A, Escargueil AE, Orlowski S. The multidrug transporter, P-glycoprotein, actively mediates cholesterol redistribution in the cell membrane. Proc Natl Acad Sci USA 2002;99:10347-10352.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 10347-10352
    • Garrigues, A.1    Escargueil, A.E.2    Orlowski, S.3
  • 10
    • 0030878573 scopus 로고    scopus 로고
    • Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains
    • Harder T, Simons K. Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains. Curr Opin Cell Biol 1997;9:534-542.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 534-542
    • Harder, T.1    Simons, K.2
  • 11
    • 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
  • 12
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown DA, London E. Functions of lipid rafts in biological membranes. Annu Rev Cell Dev Biol 1998;14:111-136.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 14
    • 0036900081 scopus 로고    scopus 로고
    • Membrane rafts in immunoreceptor signaling: New doubts, new proofs?
    • Horejsi V. Membrane rafts in immunoreceptor signaling: new doubts, new proofs? Trends Immunol 2002;23:562-564.
    • (2002) Trends Immunol , vol.23 , pp. 562-564
    • Horejsi, V.1
  • 15
    • 0037013717 scopus 로고    scopus 로고
    • Landing of immune receptors and signal proteins on lipid rafts: A safe way to be spatio-temporally coordinated?
    • Matko J, Szollosi J. Landing of immune receptors and signal proteins on lipid rafts: a safe way to be spatio-temporally coordinated? Immunol Lett 2002;82:3-15.
    • (2002) Immunol Lett , vol.82 , pp. 3-15
    • Matko, J.1    Szollosi, J.2
  • 16
    • 0028057494 scopus 로고
    • Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae
    • Parton RG. Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae. J Histochem Cytochem 1994;42:155-166.
    • (1994) J Histochem Cytochem , vol.42 , pp. 155-166
    • Parton, R.G.1
  • 17
    • 0037166323 scopus 로고    scopus 로고
    • Sequestration of epidermal growth factor receptors in non-caveolar lipid rafts inhibits ligand binding
    • Roepstorff K, Thomsen P, Sandvig K, van Deurs B. Sequestration of epidermal growth factor receptors in non-caveolar lipid rafts inhibits ligand binding. J Biol Chem 2002;277:18954-18960.
    • (2002) J Biol Chem , vol.277 , pp. 18954-18960
    • Roepstorff, K.1    Thomsen, P.2    Sandvig, K.3    Van Deurs, B.4
  • 19
    • 0032586012 scopus 로고    scopus 로고
    • Transport of (glyco)sphingolipids in and between cellular membranes; multidrug transporters and lateral domains
    • van Meer G, Sillence D, Sprong H, Kalin N, Raggers R. Transport of (glyco)sphingolipids in and between cellular membranes; multidrug transporters and lateral domains. Biosci Rep 1999;19:327-333.
    • (1999) Biosci Rep , vol.19 , pp. 327-333
    • Van Meer, G.1    Sillence, D.2    Sprong, H.3    Kalin, N.4    Raggers, R.5
  • 20
    • 0037429690 scopus 로고    scopus 로고
    • Relationship between cholesterol trafficking and signaling in rafts and caveolae
    • Fielding CJ, Fielding PE. Relationship between cholesterol trafficking and signaling in rafts and caveolae. Biochim Biophys Acta 2003;1610: 219-228.
    • (2003) Biochim Biophys Acta , vol.1610 , pp. 219-228
    • Fielding, C.J.1    Fielding, P.E.2
  • 22
    • 0024163069 scopus 로고
    • Membrane Ig-cytoskeletal interactions. 1. Flow cytofluorimetric and biochemical analysis of membrane IgM-cytoskeletal interactions
    • Albrecht DL, Noelle RJ. Membrane Ig-cytoskeletal interactions. 1. Flow cytofluorimetric and biochemical analysis of membrane IgM-cytoskeletal interactions. J Immunol 1988;141:3915-3922.
    • (1988) J Immunol , vol.141 , pp. 3915-3922
    • Albrecht, D.L.1    Noelle, R.J.2
  • 23
    • 0025735032 scopus 로고
    • Association of various T cell-surface molecules with the cytoskeleton. Effect of cross-linking and activation
    • Geppert TD, Lipsky PE. Association of various T cell-surface molecules with the cytoskeleton. Effect of cross-linking and activation. J Immunol 1991;146:3298-3305.
    • (1991) J Immunol , vol.146 , pp. 3298-3305
    • Geppert, T.D.1    Lipsky, P.E.2
  • 24
    • 0030979617 scopus 로고    scopus 로고
    • Flow cytometric detection of the association between cell surface receptors and the cytoskeleton
    • Nebe B, Bohn W, Pommerenke H, Rychly J. Flow cytometric detection of the association between cell surface receptors and the cytoskeleton. Cytometry 1997;28:66-73.
    • (1997) Cytometry , vol.28 , pp. 66-73
    • Nebe, B.1    Bohn, W.2    Pommerenke, H.3    Rychly, J.4
  • 25
    • 0030222116 scopus 로고    scopus 로고
    • Cell surface organization by the membrane skeleton
    • Kusumi A, Sako Y. Cell surface organization by the membrane skeleton. Curr Opin Cell Biol 1996;8:566-574.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 566-574
    • Kusumi, A.1    Sako, Y.2
  • 26
    • 0030566759 scopus 로고    scopus 로고
    • A photobleaching energy transfer analysis of CD8/MHC-1 and LFA-1/ICAM-1 interactions in CTL-target cell conjugates
    • Bacso Z, Bene L, Bodnar A, Matko J, Damjanovich S. A photobleaching energy transfer analysis of CD8/MHC-1 and LFA-1/ICAM-1 interactions in CTL-target cell conjugates. Immunol Lett 1996;54:151-156.
    • (1996) Immunol Lett , vol.54 , pp. 151-156
    • Bacso, Z.1    Bene, L.2    Bodnar, A.3    Matko, J.4    Damjanovich, S.5
  • 29
    • 0037244775 scopus 로고    scopus 로고
    • Lipids as a target for drugs modulating multidrug resistance of cancer cells
    • Hendrich AB, Michalak K. Lipids as a target for drugs modulating multidrug resistance of cancer cells. Curr Drug Targets 2003;4:23-30.
    • (2003) Curr Drug Targets , vol.4 , pp. 23-30
    • Hendrich, A.B.1    Michalak, K.2
  • 30
    • 0026669363 scopus 로고
    • Characterization of the azidopine and vinblastine binding site of P-glycoprotein
    • Bruggemann EP, Currier SJ, Gottesman MM, Pastan I. Characterization of the azidopine and vinblastine binding site of P-glycoprotein. J Biol Chem 1992;267:21020-21016.
    • (1992) J Biol Chem , vol.267 , pp. 21020-121016
    • Bruggemann, E.P.1    Currier, S.J.2    Gottesman, M.M.3    Pastan, I.4
  • 31
    • 0028332661 scopus 로고
    • Calcein accumulation as a fluorometric functional assay of the multidrug transporter
    • Hollo Z, Homolya L, Davis CW, Sarkadi B. Calcein accumulation as a fluorometric functional assay of the multidrug transporter. Biochim Biophys Acta 1994;1191:384-388.
    • (1994) Biochim Biophys Acta , vol.1191 , pp. 384-388
    • Hollo, Z.1    Homolya, L.2    Davis, C.W.3    Sarkadi, B.4
  • 33
    • 0026555706 scopus 로고
    • Structural and functional analysis of monomorphic determinants recognized by monoclonal antibodies reacting with the HLA class I alpha 3 domain
    • Tanabe M, Sekimata M, Ferrone S, Takiguchi M. Structural and functional analysis of monomorphic determinants recognized by monoclonal antibodies reacting with the HLA class I alpha 3 domain. J Immunol 1992;148:3202-3209.
    • (1992) J Immunol , vol.148 , pp. 3202-3209
    • Tanabe, M.1    Sekimata, M.2    Ferrone, S.3    Takiguchi, M.4
  • 34
    • 0021243527 scopus 로고
    • Fluorescence energy transfer measurements on cell surfaces: A critical comparison of steady-state fluorometric and flow cytometric methods
    • Szollosi J, Tron L, Damjanovich S, Helliwell SH, Arndt-Jovin D, Jovin TM. Fluorescence energy transfer measurements on cell surfaces: a critical comparison of steady-state fluorometric and flow cytometric methods. Cytometry 1984;5:210-216.
    • (1984) Cytometry , vol.5 , pp. 210-216
    • Szollosi, J.1    Tron, L.2    Damjanovich, S.3    Helliwell, S.H.4    Arndt-Jovin, D.5    Jovin, T.M.6
  • 35
    • 0030267031 scopus 로고    scopus 로고
    • Supramolecular complexes of MHC class I, MHC class II, CD20, and tetraspan molecules (CD53, CD81, and CD82) at the surface of a B cell line JY
    • Szollosi J, Horejsi V, Bene L, Angelisova P, Damjanovich S. Supramolecular complexes of MHC class I, MHC class II, CD20, and tetraspan molecules (CD53, CD81, and CD82) at the surface of a B cell line JY. J Immunol 1996;157:2939-2946.
    • (1996) J Immunol , vol.157 , pp. 2939-2946
    • Szollosi, J.1    Horejsi, V.2    Bene, L.3    Angelisova, P.4    Damjanovich, S.5
  • 36
    • 12944328730 scopus 로고    scopus 로고
    • Cholesterol-dependent clustering of IL-2Ralpha and its colocalization with HLA and CD48 on T lymphoma cells suggest their functional association with lipid rafts
    • Vereb G, Matko J, Vamosi G, Ibrahim SM, Magyar E, Varga S, Szollosi J, Jenei A, Gaspar R Jr, Waldmann TA, et al. Cholesterol-dependent clustering of IL-2Ralpha and its colocalization with HLA and CD48 on T lymphoma cells suggest their functional association with lipid rafts. Proc Natl Acad Sci USA 2000;97:6013-6018.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6013-6018
    • Vereb, G.1    Matko, J.2    Vamosi, G.3    Ibrahim, S.M.4    Magyar, E.5    Varga, S.6    Szollosi, J.7    Jenei, A.8    Gaspar Jr., R.9    Waldmann, T.A.10
  • 37
    • 0017795758 scopus 로고
    • Fluorescence energy transfer as a spectroscopic ruler
    • Stryer L. Fluorescence energy transfer as a spectroscopic ruler. Annu Rev Biochem 1978;47:819-846.
    • (1978) Annu Rev Biochem , vol.47 , pp. 819-846
    • Stryer, L.1
  • 38
    • 0021273333 scopus 로고
    • Flow cytometric measurement of fluorescence resonance energy transfer on cell surfaces. Quantitative evaluation of the transfer efficiency on a cell-by-cell basis
    • Tron L, Szollosi J, Damjanovich S, Helliwell SH, Arndt-Jovin DJ, Jovin TM. Flow cytometric measurement of fluorescence resonance energy transfer on cell surfaces. Quantitative evaluation of the transfer efficiency on a cell-by-cell basis. Biophys J 1984;45:939-946.
    • (1984) Biophys J , vol.45 , pp. 939-946
    • Tron, L.1    Szollosi, J.2    Damjanovich, S.3    Helliwell, S.H.4    Arndt-Jovin, D.J.5    Jovin, T.M.6
  • 39
    • 0024119672 scopus 로고
    • Luminescence spectroscopic approaches in studying cell surface dynamics
    • Matko J, Szollosi J, Tron L, Damjanovich S. Luminescence spectroscopic approaches in studying cell surface dynamics. Q Rev Biophys 1988;21:479-544.
    • (1988) Q Rev Biophys , vol.21 , pp. 479-544
    • Matko, J.1    Szollosi, J.2    Tron, L.3    Damjanovich, S.4
  • 40
    • 0024342937 scopus 로고
    • Physical association between MHC class I and class II molecules detected on the cell surface by flow cytometric energy transfer
    • Szollosi J, Damjanovich S, Balazs M, Nagy P, Tron L, Fulwyler MJ, Brodsky FM. Physical association between MHC class I and class II molecules detected on the cell surface by flow cytometric energy transfer. J Immunol 1989;143:208-213.
    • (1989) J Immunol , vol.143 , pp. 208-213
    • Szollosi, J.1    Damjanovich, S.2    Balazs, M.3    Nagy, P.4    Tron, L.5    Fulwyler, M.J.6    Brodsky, F.M.7
  • 41
    • 0026550033 scopus 로고
    • Fluorescence resonance energy transfer measurements on cell surfaces. A spectroscopic tool for determining protein interactions
    • Matyus L. Fluorescence resonance energy transfer measurements on cell surfaces. A spectroscopic tool for determining protein interactions. J Photochem Photobiol B 1992;12:323-337.
    • (1992) J Photochem Photobiol B , vol.12 , pp. 323-337
    • Matyus, L.1
  • 43
    • 0028101424 scopus 로고
    • Lateral organization of the ICAM-I molecule at the surface of human lymphoblasts: A possible model for its co-distribution with the IL-2 receptor, class I and class II HLA molecules
    • Bene L, Balazs M, Matko J, Most J, Dierich MP, Szollosi J, Damjanovich S. Lateral organization of the ICAM-I molecule at the surface of human lymphoblasts: a possible model for its co-distribution with the IL-2 receptor, class I and class II HLA molecules. Eur J Immunol 1994;24:2115-2123.
    • (1994) Eur J Immunol , vol.24 , pp. 2115-2123
    • Bene, L.1    Balazs, M.2    Matko, J.3    Most, J.4    Dierich, M.P.5    Szollosi, J.6    Damjanovich, S.7
  • 44
    • 0028948375 scopus 로고
    • Cross-linking of CD4 in a TCR/CD3-juxtaposed inhibitory state: A pFRET study
    • Szabo G Jr, Weaver JL, Pine PS, Rao PE, Aszalos A. Cross-linking of CD4 in a TCR/CD3-juxtaposed inhibitory state: a pFRET study. Biophys J 1995;68:1170-1176.
    • (1995) Biophys J , vol.68 , pp. 1170-1176
    • Szabo Jr., G.1    Weaver, J.L.2    Pine, P.S.3    Rao, P.E.4    Aszalos, A.5
  • 45
    • 0030695442 scopus 로고    scopus 로고
    • Preassembly of interleukin 2 (IL-2) receptor subunits on resting Kit 225 K6 T cells and their modulation by IL-2, IL-7, and IL-15: A fluorescence resonance energy transfer study
    • Damjanovich S, Bene L, Matko J, Alileche A, Goldman CK, Sharrow S, Waldmann TA. Preassembly of interleukin 2 (IL-2) receptor subunits on resting Kit 225 K6 T cells and their modulation by IL-2, IL-7, and IL-15: a fluorescence resonance energy transfer study. Proc Natl Acad Sci USA 1997;94:13134-13139.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13134-13139
    • Damjanovich, S.1    Bene, L.2    Matko, J.3    Alileche, A.4    Goldman, C.K.5    Sharrow, S.6    Waldmann, T.A.7
  • 46
    • 0036298998 scopus 로고    scopus 로고
    • INF-gamma rearranges membrane topography of MHC-I and ICAM-1 in colon carcinoma cells
    • Bacso Z, Bene L, Damjanovich L, Damjanovich S. INF-gamma rearranges membrane topography of MHC-I and ICAM-1 in colon carcinoma cells. Biochem Biophys Res Commun 2002;290:635-640.
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 635-640
    • Bacso, Z.1    Bene, L.2    Damjanovich, L.3    Damjanovich, S.4
  • 47
    • 0024312858 scopus 로고
    • Membrane immunoglobulin-cytoskeletal interactions - II. Biochemical analysis of cytoskeletally associated IgM
    • Albrecht DL, Noelle RJ. Membrane immunoglobulin-cytoskeletal interactions - II. Biochemical analysis of cytoskeletally associated IgM. Mol Immunol 1989;26:575-582.
    • (1989) Mol Immunol , vol.26 , pp. 575-582
    • Albrecht, D.L.1    Noelle, R.J.2
  • 48
    • 0025214329 scopus 로고
    • Membrane Ig-cytoskeletal interactions. III. Receptor cross-linking results in the formation of extensive filamentous arrays of vimentin
    • Albrecht DL, Mills JW, Noelle RJ. Membrane Ig-cytoskeletal interactions. III. Receptor cross-linking results in the formation of extensive filamentous arrays of vimentin. J Immunol 1990;144:3251-3256.
    • (1990) J Immunol , vol.144 , pp. 3251-3256
    • Albrecht, D.L.1    Mills, J.W.2    Noelle, R.J.3
  • 49
    • 0027993199 scopus 로고
    • MHC class II molecules that lack cytoplasmic domains are associated with the cytoskeleton
    • Chia CP, Khrebtukova I, McCluskey J, Wade WF. MHC class II molecules that lack cytoplasmic domains are associated with the cytoskeleton. J Immunol 1994;153:3398-3407.
    • (1994) J Immunol , vol.153 , pp. 3398-3407
    • Chia, C.P.1    Khrebtukova, I.2    McCluskey, J.3    Wade, W.F.4
  • 52
    • 0142134442 scopus 로고    scopus 로고
    • Resistance of cellular membrane antigens to solubilization with Triton X-100 as a marker of their association with lipid rafts - Analysis by flow cytometry
    • Filatov AV, Shmigol IB, Kuzin, H, Sharonov GV, Feofanov AV. Resistance of cellular membrane antigens to solubilization with Triton X-100 as a marker of their association with lipid rafts - analysis by flow cytometry. J Immunol Methods 2003;278:211-219.
    • (2003) J Immunol Methods , vol.278 , pp. 211-219
    • Filatov, A.V.1    Shmigol, I.B.2    Kuzin, H.3    Sharonov, G.V.4    Feofanov, A.V.5
  • 53
    • 0033533744 scopus 로고    scopus 로고
    • Role of actin-filament disassembly in lamellipodium protrusion in motile cells revealed using the drug jasplakinolide
    • Cramer LP. Role of actin-filament disassembly in lamellipodium protrusion in motile cells revealed using the drug jasplakinolide. Curr Biol 1999;9:1095-1105.
    • (1999) Curr Biol , vol.9 , pp. 1095-1105
    • Cramer, L.P.1
  • 54
    • 0024121613 scopus 로고
    • Principles of frequency-domain fluorescence spectroscopy and applications to cell membranes
    • Lakowicz JR. Principles of frequency-domain fluorescence spectroscopy and applications to cell membranes. Subcell Biochem 1988;13:89-126.
    • (1988) Subcell Biochem , vol.13 , pp. 89-126
    • Lakowicz, J.R.1
  • 55
    • 0034983757 scopus 로고    scopus 로고
    • Flow cytometric analysis of the association between blood group-related proteins and the detergent-insoluble material of K562 cells and erythroid precursors
    • Gane P, Le Van Kim C, Bony V, El Nemer W, Mouro I, Nicolas V, Colin Y, Cartron JP. Flow cytometric analysis of the association between blood group-related proteins and the detergent-insoluble material of K562 cells and erythroid precursors. Br J Haematol 2001;113:680-688.
    • (2001) Br J Haematol , vol.113 , pp. 680-688
    • Gane, P.1    Van Le Kim, C.2    Bony, V.3    El Nemer, W.4    Mouro, I.5    Nicolas, V.6    Colin, Y.7    Cartron, J.P.8
  • 56
    • 0014935560 scopus 로고
    • Immunoglobulin determinants on the surface of mouse lymphoid cells
    • Raff MC, Sternberg M, Taylor RB. Immunoglobulin determinants on the surface of mouse lymphoid cells. Nature 1970;225:553-554.
    • (1970) Nature , vol.225 , pp. 553-554
    • Raff, M.C.1    Sternberg, M.2    Taylor, R.B.3
  • 57
    • 0015443616 scopus 로고
    • Distribution of immunoglobulin on the surface of mouse lymphoid cells as determined by immunoferritin electron microscopy. Antibody-induced, temperature-dependent redistribution and its implications for membrane structure
    • de Petris S, Raff MC. Distribution of immunoglobulin on the surface of mouse lymphoid cells as determined by immunoferritin electron microscopy. Antibody-induced, temperature-dependent redistribution and its implications for membrane structure. Eur J Immunol 1972;2:523-535.
    • (1972) Eur J Immunol , vol.2 , pp. 523-535
    • De Petris, S.1    Raff, M.C.2
  • 58
    • 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
  • 59
    • 0034695916 scopus 로고    scopus 로고
    • Induction of caveolae in the apical plasma membrane of Madin-Darby canine kidney cells
    • Verkade P, Harder T, Lafont F, Simons K. Induction of caveolae in the apical plasma membrane of Madin-Darby canine kidney cells. J Cell Biol 2000;148:727-739.
    • (2000) J Cell Biol , vol.148 , pp. 727-739
    • Verkade, P.1    Harder, T.2    Lafont, F.3    Simons, K.4
  • 60
    • 0037105388 scopus 로고    scopus 로고
    • Colocalization of the B cell receptor and CD20 followed by activation-dependent dissociation in distinct lipid rafts
    • Petrie RJ, Deans JP. Colocalization of the B cell receptor and CD20 followed by activation-dependent dissociation in distinct lipid rafts. J Immunol 2002;169:2886-2891.
    • (2002) J Immunol , vol.169 , pp. 2886-2891
    • Petrie, R.J.1    Deans, J.P.2
  • 62
    • 0037844879 scopus 로고    scopus 로고
    • Microvillar membrane microdomains exist at physiological temperature. Role of galectin-4 as lipid raft stabilizer revealed by "superrafts."
    • Braccia A, Villani M, Immerdal L, Niels-Christiansen LL, Nystrom BT, Hansen GH, Danielsen EM. Microvillar membrane microdomains exist at physiological temperature. Role of galectin-4 as lipid raft stabilizer revealed by "superrafts." J Biol Chem 2003;278:15679-15684.
    • (2003) J Biol Chem , vol.278 , pp. 15679-15684
    • Braccia, A.1    Villani, M.2    Immerdal, L.3    Niels-Christiansen, L.L.4    Nystrom, B.T.5    Hansen, G.H.6    Danielsen, E.M.7
  • 63
    • 0033005974 scopus 로고    scopus 로고
    • Regulation of cortical structure by the ezrin-radixin-moesin protein family
    • Bretscher A. Regulation of cortical structure by the ezrin-radixin-moesin protein family. Curr Opin Cell Biol 1999;11:109-116.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 109-116
    • Bretscher, A.1
  • 64
    • 0036532117 scopus 로고    scopus 로고
    • Ion transport proteins anchor and regulate the cytoskeleton
    • Denker SP, Barber DL. Ion transport proteins anchor and regulate the cytoskeleton. Curr Opin Cell Biol 2002;14:214-220.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 214-220
    • Denker, S.P.1    Barber, D.L.2
  • 65
    • 0036468423 scopus 로고    scopus 로고
    • ERM proteins and NF2 tumor suppressor: The Yin and Yang of cortical actin organization and cell growth signaling
    • Gautreau A, Louvard D, Arpin M. ERM proteins and NF2 tumor suppressor: the Yin and Yang of cortical actin organization and cell growth signaling. Curr Opin Cell Biol 2002;14:104-109.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 104-109
    • Gautreau, A.1    Louvard, D.2    Arpin, M.3


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