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Volumn 99, Issue 3, 2010, Pages 853-861

Noninvasive measurements of integrin microclustering under altered membrane cholesterol levels

Author keywords

[No Author keywords available]

Indexed keywords

CHOLESTEROL; INTEGRIN;

EID: 77955702228     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.05.027     Document Type: Article
Times cited : (11)

References (62)
  • 1
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • Giancotti, F. G., and E. Ruoslahti. 1999. Integrin signaling. Science. 285:1028-1032.
    • (1999) Science , vol.285 , pp. 1028-1032
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 2
    • 70249147673 scopus 로고    scopus 로고
    • Intracellular detection and immune signaling pathways of DNA vaccines
    • Tang, C. K., and G. A. Pietersz. 2009. Intracellular detection and immune signaling pathways of DNA vaccines. Expert Rev. Vaccines. 8:1161-1170.
    • (2009) Expert Rev. Vaccines. , vol.8 , pp. 1161-1170
    • Tang, C.K.1    Pietersz, G.A.2
  • 3
    • 70349462469 scopus 로고    scopus 로고
    • Olfactory perception: Receptors, cells, and circuits
    • Su, C. Y., K. Menuz, and J. R. Carlson. 2009. Olfactory perception: receptors, cells, and circuits. Cell. 139:45-59.
    • (2009) Cell , vol.139 , pp. 45-59
    • Su, C.Y.1    Menuz, K.2    Carlson, J.R.3
  • 4
    • 69249137477 scopus 로고    scopus 로고
    • Endocytosis and signalling: Intertwining molecular networks
    • Sorkin, A., and M. von Zastrow. 2009. Endocytosis and signalling: intertwining molecular networks. Nat. Rev. Mol. Cell Biol. 10:609-622.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 609-622
    • Sorkin, A.1    Von Zastrow, M.2
  • 5
    • 70349336151 scopus 로고    scopus 로고
    • B cell receptor and BAFF receptor signaling regulation of B cell homeostasis
    • Khan, W. N. 2009. B cell receptor and BAFF receptor signaling regulation of B cell homeostasis. J. Immunol. 183:3561-3567.
    • (2009) J. Immunol. , vol.183 , pp. 3561-3567
    • Khan, W.N.1
  • 6
    • 0033824065 scopus 로고    scopus 로고
    • Avidity regulation of integrins: The driving force in leukocyte adhesion
    • van Kooyk, Y., and C. G. Figdor. 2000. Avidity regulation of integrins: the driving force in leukocyte adhesion. Curr. Opin. Cell Biol. 12: 542-547.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 542-547
    • Van Kooyk, Y.1    Figdor, C.G.2
  • 7
    • 33646137152 scopus 로고    scopus 로고
    • Immunological synapse and microclusters: The site for recognition and activation of T cells
    • Saito, T., and T. Yokosuka. 2006. Immunological synapse and microclusters: the site for recognition and activation of T cells. Curr. Opin. Immunol. 18:305-313.
    • (2006) Curr. Opin. Immunol. , vol.18 , pp. 305-313
    • Saito, T.1    Yokosuka, T.2
  • 10
    • 35148901559 scopus 로고    scopus 로고
    • Electron microscopy of integrins
    • Adair, B. D., and M. Yeager. 2007. Electron microscopy of integrins. Methods Enzymol. 426:337-373.
    • (2007) Methods Enzymol. , vol.426 , pp. 337-373
    • Adair, B.D.1    Yeager, M.2
  • 11
    • 0033578822 scopus 로고    scopus 로고
    • The actin cytoskeleton regulates LFA-1 ligand binding through avidity rather than affinity changes
    • van Kooyk, Y., S. J. van Vliet, and C. G. Figdor. 1999. The actin cytoskeleton regulates LFA-1 ligand binding through avidity rather than affinity changes. J. Biol. Chem. 274:26869-26877.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26869-26877
    • Van Kooyk, Y.1    Van Vliet, S.J.2    Figdor, C.G.3
  • 12
    • 0030840113 scopus 로고    scopus 로고
    • Mutational evidence for control of cell adhesion through integrin diffusion/clustering, independent of ligand binding
    • Yauch, R. L., D. P. Felsenfeld, M. E. Hemler. 1997. Mutational evidence for control of cell adhesion through integrin diffusion/clustering, independent of ligand binding. J. Exp. Med. 186:1347-1355.
    • (1997) J. Exp. Med. , vol.186 , pp. 1347-1355
    • Yauch, R.L.1    Felsenfeld, D.P.2    Hemler, M.E.3
  • 13
    • 0032578007 scopus 로고    scopus 로고
    • Complementary roles for receptor clustering and conformational change in the adhesive and signaling functions of integrin αIIb β3
    • Hato, T., N. Pampori, and S. J. Shattil. 1998. Complementary roles for receptor clustering and conformational change in the adhesive and signaling functions of integrin αIIb β3. J. Cell Biol. 141:1685-1695.
    • (1998) J. Cell Biol. , vol.141 , pp. 1685-1695
    • Hato, T.1    Pampori, N.2    Shattil, S.J.3
  • 14
    • 0033823060 scopus 로고    scopus 로고
    • The renaissance of fluorescence resonance energy transfer
    • Selvin, P. R. 2000. The renaissance of fluorescence resonance energy transfer. Nat. Struct. Biol. 7:730-734.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 730-734
    • Selvin, P.R.1
  • 15
    • 0037674763 scopus 로고    scopus 로고
    • Detection of integrin αIIbβ 3 clustering in living cells
    • Buensuceso, C., M. de Virgilio, and S. J. Shattil. 2003. Detection of integrin αIIbβ 3 clustering in living cells. J. Biol. Chem. 278: 15217-15224.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15217-15224
    • Buensuceso, C.1    De Virgilio, M.2    Shattil, S.J.3
  • 16
    • 11244274075 scopus 로고    scopus 로고
    • The primacy of affinity over clustering in regulation of adhesiveness of the integrin αLβ2
    • Kim, M., C. V. Carman, T. A. Springer. 2004. The primacy of affinity over clustering in regulation of adhesiveness of the integrin αLβ2. J. Cell Biol. 167:1241-1253.
    • (2004) J. Cell Biol. , vol.167 , pp. 1241-1253
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3
  • 17
    • 34247362125 scopus 로고    scopus 로고
    • General in vivo assay for the study of integrin cell membrane receptor microclustering
    • Smith, E. A., T. A. Bunch, and D. L. Brower. 2007. General in vivo assay for the study of integrin cell membrane receptor microclustering. Anal. Chem. 79:3142-3147.
    • (2007) Anal. Chem. , vol.79 , pp. 3142-3147
    • Smith, E.A.1    Bunch, T.A.2    Brower, D.L.3
  • 18
    • 71449102495 scopus 로고    scopus 로고
    • Identifying cytoplasmic proteins that affect receptor clustering using fluorescence resonance energy transfer and RNA interference
    • Dibya, D., S. Sander, and E. A. Smith. 2009. Identifying cytoplasmic proteins that affect receptor clustering using fluorescence resonance energy transfer and RNA interference. Anal. Bioanal. Chem. 395: 2303-2311.
    • (2009) Anal. Bioanal. Chem. , vol.395 , pp. 2303-2311
    • Dibya, D.1    Sander, S.2    Smith, E.A.3
  • 19
    • 0029959355 scopus 로고    scopus 로고
    • Intracellular signals direct integrin localization to sites of function in embryonic muscles
    • Martin-Bermudo, M. D., and N. H. Brown. 1996. Intracellular signals direct integrin localization to sites of function in embryonic muscles. J. Cell Biol. 134:217-226.
    • (1996) J. Cell Biol. , vol.134 , pp. 217-226
    • Martin-Bermudo, M.D.1    Brown, N.H.2
  • 20
    • 0035940359 scopus 로고    scopus 로고
    • Oligomerization of the integrin αIIbβ3: Roles of the transmembrane and cytoplasmic domains
    • Li, R., C. R. Babu, W. F. DeGrado. 2001. Oligomerization of the integrin αIIbβ3: roles of the transmembrane and cytoplasmic domains. Proc. Natl. Acad. Sci. USA. 98:12462-12467.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12462-12467
    • Li, R.1    Babu, C.R.2    DeGrado, W.F.3
  • 21
    • 0017744051 scopus 로고
    • Band 3-protein from human erythrocyte membranes strongly interacts with cholesterol
    • Klappauf, E., and D. Schubert. 1977. Band 3-protein from human erythrocyte membranes strongly interacts with cholesterol. FEBS Lett. 80:423-425.
    • (1977) FEBS Lett. , vol.80 , pp. 423-425
    • Klappauf, E.1    Schubert, D.2
  • 22
    • 0020441513 scopus 로고
    • Influence of cholesterol on the rotation and self-association of band 3 in the human erythrocyte membrane
    • Mühlebach, T., and R. J. Cherry. 1982. Influence of cholesterol on the rotation and self-association of band 3 in the human erythrocyte membrane. Biochemistry. 21:4225-4228.
    • (1982) Biochemistry , vol.21 , pp. 4225-4228
    • Mühlebach, T.1    Cherry, R.J.2
  • 24
    • 11244339619 scopus 로고    scopus 로고
    • Cholesterol depletion suppresses the translational diffusion of class II major histocompatibility complex proteins in the plasma membrane
    • Vrljic, M., S. Y. Nishimura, H. M. McConnell. 2005. Cholesterol depletion suppresses the translational diffusion of class II major histocompatibility complex proteins in the plasma membrane. Biophys. J. 88:334-347.
    • (2005) Biophys. J. , vol.88 , pp. 334-347
    • Vrljic, M.1    Nishimura, S.Y.2    McConnell, H.M.3
  • 25
    • 0022389171 scopus 로고
    • Cholesterol and the cell membrane
    • Yeagle, P. L. 1985. Cholesterol and the cell membrane. Biochim. Biophys. Acta. 822:267-287.
    • (1985) Biochim. Biophys. Acta. , vol.822 , pp. 267-287
    • Yeagle, P.L.1
  • 26
    • 0033552651 scopus 로고    scopus 로고
    • How does the plasma membrane participate in cellular signaling by receptors for immunoglobulin E?
    • Baird, B., E. D. Sheets, and D. Holowka. 1999. How does the plasma membrane participate in cellular signaling by receptors for immunoglobulin E? Biophys. Chem. 82:109-119.
    • (1999) Biophys. Chem. , vol.82 , pp. 109-119
    • Baird, B.1    Sheets, E.D.2    Holowka, D.3
  • 27
    • 0033998793 scopus 로고    scopus 로고
    • The role of lipid rafts in T cell antigen receptor (TCR) signalling
    • Janes, P.W., S. C. Ley, P. S. Kabouridis. 2000. The role of lipid rafts in T cell antigen receptor (TCR) signalling. Semin. Immunol. 12:23-34.
    • (2000) Semin. Immunol. , vol.12 , pp. 23-34
    • Janes, P.W.1    Ley, S.C.2    Kabouridis, P.S.3
  • 28
    • 0033601228 scopus 로고    scopus 로고
    • Integrin leukocyte functionassociated antigen-1-mediated cell binding can be activated by clustering of membrane rafts
    • Krauss, K., and P. Altevogt. 1999. Integrin leukocyte functionassociated antigen-1-mediated cell binding can be activated by clustering of membrane rafts. J. Biol. Chem. 274:36921-36927.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36921-36927
    • Krauss, K.1    Altevogt, P.2
  • 30
    • 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., R. H. Baloh, E. M. Johnson, Jr. 2000. GFRα-mediated localization of RET to lipid rafts is required for effective downstream signaling, differentiation, and neuronal survival. Neuron. 25:611-623.
    • (2000) Neuron , vol.25 , pp. 611-623
    • Tansey, M.G.1    Baloh, R.H.2    Johnson Jr., E.M.3
  • 31
    • 0029120852 scopus 로고
    • Cellular cholesterol efflux mediated by cyclodextrins
    • Kilsdonk, E. P., P. G. Yancey, G. H. Rothblat. 1995. Cellular cholesterol efflux mediated by cyclodextrins. J. Biol. Chem. 270: 17250-17256.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17250-17256
    • Kilsdonk, E.P.1    Yancey, P.G.2    Rothblat, G.H.3
  • 32
    • 0026671979 scopus 로고
    • Drosophila PS2 integrin mediates RGD-dependent cell-matrix interactions
    • Bunch, T. A., and D. L. Brower. 1992. Drosophila PS2 integrin mediates RGD-dependent cell-matrix interactions. Development. 116: 239-247.
    • (1992) Development , vol.116 , pp. 239-247
    • Bunch, T.A.1    Brower, D.L.2
  • 33
    • 0036230998 scopus 로고    scopus 로고
    • Disruption of C-terminal cytoplasmic domain of βPS integrin subunit has dominant negative properties in developing Drosophila
    • Jannuzi, A. L., T. A. Bunch, D. L. Brower. 2002. Disruption of C-terminal cytoplasmic domain of βPS integrin subunit has dominant negative properties in developing Drosophila. Mol. Biol. Cell. 13: 1352-1365.
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 1352-1365
    • Jannuzi, A.L.1    Bunch, T.A.2    Brower, D.L.3
  • 34
    • 3342958175 scopus 로고    scopus 로고
    • Identification of integrin β subunit mutations that alter heterodimer function in situ
    • Jannuzi, A. L., T. A. Bunch, D. L. Brower. 2004. Identification of integrin β subunit mutations that alter heterodimer function in situ. Mol. Biol. Cell. 15:3829-3840.
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 3829-3840
    • Jannuzi, A.L.1    Bunch, T.A.2    Brower, D.L.3
  • 35
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E. G., and W. J. Dyer. 1959. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37:911-917.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 36
    • 69949085710 scopus 로고    scopus 로고
    • An adhesion-based method for plasma membrane isolation: Evaluating cholesterol extraction from cells and their membranes
    • Bezrukov, L., P. S. Blank, J. Zimmerberg. 2009. An adhesion-based method for plasma membrane isolation: evaluating cholesterol extraction from cells and their membranes. Anal. Biochem. 394:171-176.
    • (2009) Anal. Biochem. , vol.394 , pp. 171-176
    • Bezrukov, L.1    Blank, P.S.2    Zimmerberg, J.3
  • 37
    • 0033016103 scopus 로고    scopus 로고
    • Fluorometric method for the enzymatic determination of cholesterol
    • Amundson, D. M., and M. Zhou. 1999. Fluorometric method for the enzymatic determination of cholesterol. J. Biochem. Biophys. Methods. 38:43-52.
    • (1999) J. Biochem. Biophys. Methods. , vol.38 , pp. 43-52
    • Amundson, D.M.1    Zhou, M.2
  • 40
    • 2942640371 scopus 로고    scopus 로고
    • Photobleaching-corrected FRET efficiency imaging of live cells
    • Zal, T., and N. R. Gascoigne. 2004. Photobleaching-corrected FRET efficiency imaging of live cells. Biophys. J. 86:3923-3939.
    • (2004) Biophys. J. , vol.86 , pp. 3923-3939
    • Zal, T.1    Gascoigne, N.R.2
  • 41
    • 0031956092 scopus 로고    scopus 로고
    • Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy
    • Gordon, G. W., G. Berry, B. Herman. 1998. Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy. Biophys. J. 74:2702-2713.
    • (1998) Biophys. J. , vol.74 , pp. 2702-2713
    • Gordon, G.W.1    Berry, G.2    Herman, B.3
  • 42
    • 85007669243 scopus 로고    scopus 로고
    • The use of transformation when comparing two means
    • Bland, J. M., and D. G. Altman. 1996. The use of transformation when comparing two means. BMJ. 312:1153.
    • (1996) BMJ , vol.312 , pp. 1153
    • Bland, J.M.1    Altman, D.G.2
  • 43
    • 0021096818 scopus 로고
    • Statistical guidelines for contributors to medical journals
    • Altman, D. G., S. M. Gore, S. J. Pocock. 1983. Statistical guidelines for contributors to medical journals. Br. Med. J. (Clin. Res. Ed.). 286: 1489-1493.
    • (1983) Br. Med. J. (Clin. Res. Ed.) , vol.286 , pp. 1489-1493
    • Altman, D.G.1    Gore, S.M.2    Pocock, S.J.3
  • 44
    • 0004232308 scopus 로고    scopus 로고
    • Prentice Hall, Upper Saddle River, NJ
    • Zar, J. 1999. Biostatistical Analysis. Prentice Hall, Upper Saddle River, NJ.
    • (1999) Biostatistical Analysis
    • Zar, J.1
  • 45
    • 0017192686 scopus 로고
    • Mobility measurement by analysis of fluorescence photobleaching recovery kinetics
    • Axelrod, D., D. E. Koppel, W. W. Webb. 1976. Mobility measurement by analysis of fluorescence photobleaching recovery kinetics. Biophys. J. 16:1055-1069.
    • (1976) Biophys. J. , vol.16 , pp. 1055-1069
    • Axelrod, D.1    Koppel, D.E.2    Webb, W.W.3
  • 46
    • 0141756142 scopus 로고    scopus 로고
    • Platelets with wings: The maturation of Drosophila integrin biology
    • Brower, D. L. 2003. Platelets with wings: the maturation of Drosophila integrin biology. Curr. Opin. Cell Biol. 15:607-613.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 607-613
    • Brower, D.L.1
  • 47
    • 0000293138 scopus 로고
    • The absence of sterol synthesis in insects
    • Clark, A. J., and K. Block. 1959. The absence of sterol synthesis in insects. J. Biol. Chem. 234:2578-2582.
    • (1959) J. Biol. Chem. , vol.234 , pp. 2578-2582
    • Clark, A.J.1    Block, K.2
  • 48
    • 0037012907 scopus 로고    scopus 로고
    • Regulation of SREBP processing and membrane lipid production by phospholipids in Drosophila
    • Dobrosotskaya, I. Y., A. C. Seegmiller, R. B. Rawson. 2002. Regulation of SREBP processing and membrane lipid production by phospholipids in Drosophila. Science. 296:879-883.
    • (2002) Science , vol.296 , pp. 879-883
    • Dobrosotskaya, I.Y.1    Seegmiller, A.C.2    Rawson, R.B.3
  • 49
    • 33646196271 scopus 로고    scopus 로고
    • Amino acid changes in Drosophila αPS2βPS integrins that affect ligand affinity
    • Bunch, T. A., T. L. Helsten, D. L. Brower. 2006. Amino acid changes in Drosophila αPS2βPS integrins that affect ligand affinity. J. Biol. Chem. 281:5050-5057.
    • (2006) J. Biol. Chem. , vol.281 , pp. 5050-5057
    • Bunch, T.A.1    Helsten, T.L.2    Brower, D.L.3
  • 50
    • 0345112372 scopus 로고
    • Differentiationdependent expression of phosphatidylserine in mammalian plasma membranes: Quantitative assessment of outer-leaflet lipid by prothrombinase complex formation
    • Connor, J., C. Bucana, A. J. Schroit. 1989. Differentiationdependent expression of phosphatidylserine in mammalian plasma membranes: quantitative assessment of outer-leaflet lipid by prothrombinase complex formation. Proc. Natl. Acad. Sci. USA. 86:3184-3188.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 3184-3188
    • Connor, J.1    Bucana, C.2    Schroit, A.J.3
  • 51
    • 57749085357 scopus 로고    scopus 로고
    • Effect of cellular cholesterol depletion on rabies virus infection
    • Hotta, K., B. Bazartseren, A. Yamada. 2009. Effect of cellular cholesterol depletion on rabies virus infection. Virus Res. 139:85-90.
    • (2009) Virus Res. , vol.139 , pp. 85-90
    • Hotta, K.1    Bazartseren, B.2    Yamada, A.3
  • 52
    • 0037356194 scopus 로고    scopus 로고
    • Determination of plasma membrane fluidity with a fluorescent analogue of sphingomyelin by FRAP measurement using a standard confocal microscope
    • Klein, C., T. Pillot, B. Drouet. 2003. Determination of plasma membrane fluidity with a fluorescent analogue of sphingomyelin by FRAP measurement using a standard confocal microscope. Brain Res. Brain Res. Protoc. 11:46-51.
    • (2003) Brain Res. Brain Res. Protoc. , vol.11 , pp. 46-51
    • Klein, C.1    Pillot, T.2    Drouet, B.3
  • 53
    • 33746307311 scopus 로고    scopus 로고
    • Effect of cholesterol on lateral diffusion of fluorescent lipid probes in native hippocampal membranes
    • Pucadyil, T. J., and A. Chattopadhyay. 2006. Effect of cholesterol on lateral diffusion of fluorescent lipid probes in native hippocampal membranes. Chem. Phys. Lipids. 143:11-21.
    • (2006) Chem. Phys. Lipids. , vol.143 , pp. 11-21
    • Pucadyil, T.J.1    Chattopadhyay, A.2
  • 54
    • 40949113166 scopus 로고    scopus 로고
    • Differential regulation of the lateral mobility of plasma membrane phospholipids by the extracellular matrix and cholesterol
    • Ramprasad, O. G., N. Rangaraj, G. Pande. 2008. Differential regulation of the lateral mobility of plasma membrane phospholipids by the extracellular matrix and cholesterol. J. Cell. Physiol. 215: 550-561.
    • (2008) J. Cell. Physiol. , vol.215 , pp. 550-561
    • Ramprasad, O.G.1    Rangaraj, N.2    Pande, G.3
  • 55
    • 0022550412 scopus 로고
    • Changes in sperm plasma membrane lipid diffusibility after hyperactivation during in vitro capacitation in the mouse
    • Wolf, D. E., S. S. Hagopian, and S. Ishijima. 1986. Changes in sperm plasma membrane lipid diffusibility after hyperactivation during in vitro capacitation in the mouse. J. Cell Biol. 102:1372-1377.
    • (1986) J. Cell Biol. , vol.102 , pp. 1372-1377
    • Wolf, D.E.1    Hagopian, S.S.2    Ishijima, S.3
  • 56
    • 27144546706 scopus 로고    scopus 로고
    • Lipid bilayers on polyacrylamide brushes for inclusion of membrane proteins
    • Smith, E. A., J. W. Coym, M. J. Wirth. 2005. Lipid bilayers on polyacrylamide brushes for inclusion of membrane proteins. Langmuir. 21:9644-9650.
    • (2005) Langmuir , vol.21 , pp. 9644-9650
    • Smith, E.A.1    Coym, J.W.2    Wirth, M.J.3
  • 57
    • 0036500126 scopus 로고    scopus 로고
    • The involvement of lipid rafts in the regulation of integrin function
    • Leitinger, B., and N. Hogg. 2002. The involvement of lipid rafts in the regulation of integrin function. J. Cell Sci. 115:963-972.
    • (2002) J. Cell Sci. , vol.115 , pp. 963-972
    • Leitinger, B.1    Hogg, N.2
  • 58
    • 0033597141 scopus 로고    scopus 로고
    • Association of sterol- and glycosylphosphatidylinositol-linked proteins with Drosophila raft lipid microdomains
    • Rietveld, A., S. Neutz, S. Eaton. 1999. Association of sterol- and glycosylphosphatidylinositol-linked proteins with Drosophila raft lipid microdomains. J. Biol. Chem. 274:12049-12054.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12049-12054
    • Rietveld, A.1    Neutz, S.2    Eaton, S.3
  • 59
    • 77950600389 scopus 로고    scopus 로고
    • Limited cholesterol depletion causes aggregation of plasma membrane lipid rafts inducing T cell activation
    • Mahammad, S., J. Dinic, I. Parmryd. 2010. Limited cholesterol depletion causes aggregation of plasma membrane lipid rafts inducing T cell activation. Biochim. Biophys. Acta. 1801:625-634.
    • (2010) Biochim. Biophys. Acta. , vol.1801 , pp. 625-634
    • Mahammad, S.1    Dinic, J.2    Parmryd, I.3
  • 60
    • 65649146880 scopus 로고    scopus 로고
    • Integrin signalling at a glance
    • Harburger, D. S., and D. A. Calderwood. 2009. Integrin signalling at a glance. J. Cell Sci. 122:159-163.
    • (2009) J. Cell Sci. , vol.122 , pp. 159-163
    • Harburger, D.S.1    Calderwood, D.A.2
  • 61
    • 66849101632 scopus 로고    scopus 로고
    • Adhesion signaling-crosstalk between integrins, Src and Rho
    • Huveneers, S., and E. H. Danen. 2009. Adhesion signaling-crosstalk between integrins, Src and Rho. J. Cell Sci. 122:1059-1069.
    • (2009) J. Cell Sci. , vol.122 , pp. 1059-1069
    • Huveneers, S.1    Danen, E.H.2
  • 62
    • 61449220945 scopus 로고    scopus 로고
    • Genetic and cell biological analysis of integrin outside-in signaling
    • Legate, K. R., S. A. Wickström, and R. Fässler. 2009. Genetic and cell biological analysis of integrin outside-in signaling. Genes Dev. 23:397-418.
    • (2009) Genes Dev. , vol.23 , pp. 397-418
    • Legate, K.R.1    Wickström, S.A.2    Fässler, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.