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Volumn 171, Issue 6, 2003, Pages 3216-3224

Lipid raft localization of cell surface E-selectin is required for ligation-induced activation of phospholipase Cγ

Author keywords

[No Author keywords available]

Indexed keywords

ENDOTHELIAL LEUKOCYTE ADHESION MOLECULE 1; METHYL BETA CYCLODEXTRIN; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHOLIPASE C;

EID: 0042834256     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.171.6.3216     Document Type: Article
Times cited : (68)

References (53)
  • 1
    • 0029870708 scopus 로고    scopus 로고
    • Endothelial-dependent mechanisms in chronic inflammatory leukocyte recruitment
    • Luscinskas, F. W., and M. A. Gimbrone, Jr. 1996. Endothelial-dependent mechanisms in chronic inflammatory leukocyte recruitment. Annu. Rev. Med. 47:413.
    • (1996) Annu. Rev. Med. , vol.47 , pp. 413
    • Luscinskas, F.W.1    Gimbrone M.A., Jr.2
  • 2
    • 0026342111 scopus 로고
    • Leukocyte-endothelial cell recognition: Three (or more) steps to specificity and diversity
    • Butcher, E. C. 1991. Leukocyte-endothelial cell recognition: three (or more) steps to specificity and diversity. Cell 67:1033.
    • (1991) Cell , vol.67 , pp. 1033
    • Butcher, E.C.1
  • 3
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm
    • Springer, T. A. 1994. Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell 76:301.
    • (1994) Cell , vol.76 , pp. 301
    • Springer, T.A.1
  • 5
    • 0032504766 scopus 로고    scopus 로고
    • Importance of E-selectin for firm leukocyte adhesion in vivo
    • Ley, K., M. Allietta, D. C. Bullard, and S. Morgan. 1998. Importance of E-selectin for firm leukocyte adhesion in vivo. Circ. Res. 83:287.
    • (1998) Circ. Res. , vol.83 , pp. 287
    • Ley, K.1    Allietta, M.2    Bullard, D.C.3    Morgan, S.4
  • 7
    • 0032528336 scopus 로고    scopus 로고
    • Phosphorylation of the cytoplasmic domain of E-selectin is regulated during leukocyte-endothelial adhesion
    • Yoshida, M., B. E. Szente, J. M. Kiely, A. Rosenzweig, and M. A. Gimbrone, Jr. 1998. Phosphorylation of the cytoplasmic domain of E-selectin is regulated during leukocyte-endothelial adhesion. J. Immunol. 161:933.
    • (1998) J. Immunol. , vol.161 , pp. 933
    • Yoshida, M.1    Szente, B.E.2    Kiely, J.M.3    Rosenzweig, A.4    Gimbrone M.A., Jr.5
  • 8
    • 0036498903 scopus 로고    scopus 로고
    • Cutting edge: Internalization of transduced E-selectin by cultured human endothelial cells: Comparison of dermal microvascular and umbilical vein cells and identification of a phosphoserine-type di-leucine motif
    • Kluger, M. S., S. L. Shiao, A. L. Bothwell, and J. S. Pober. 2002. Cutting edge: internalization of transduced E-selectin by cultured human endothelial cells: comparison of dermal microvascular and umbilical vein cells and identification of a phosphoserine-type di-leucine motif. J. Immunol. 168:2091.
    • (2002) J. Immunol. , vol.168 , pp. 2091
    • Kluger, M.S.1    Shiao, S.L.2    Bothwell, A.L.3    Pober, J.S.4
  • 9
    • 0034662867 scopus 로고    scopus 로고
    • E-selectin-dependent signaling via the mitogen-activated protein kinase pathway in vascular endothelial cells
    • Hu, Y., J. M. Kiely, B. E. Szente, A. Rosenzweig, and M. A. Gimbrone, Jr. 2000. E-selectin-dependent signaling via the mitogen-activated protein kinase pathway in vascular endothelial cells. J. Immunol. 165:2142.
    • (2000) J. Immunol. , vol.165 , pp. 2142
    • Hu, Y.1    Kiely, J.M.2    Szente, B.E.3    Rosenzweig, A.4    Gimbrone M.A., Jr.5
  • 10
    • 0035930591 scopus 로고    scopus 로고
    • Molecular events in transmembrane signaling via E-selectin: SHP2 association, adaptor protein complex formation and ERK1/2 activation
    • Hu, Y., B. Szente, J. M. Kiely, and M. A. Gimbrone, Jr. 2001. Molecular events in transmembrane signaling via E-selectin: SHP2 association, adaptor protein complex formation and ERK1/2 activation. J. Biol. Chem. 276;48549.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48549
    • Hu, Y.1    Szente, B.2    Kiely, J.M.3    Gimbrone M.A., Jr.4
  • 12
    • 0031692336 scopus 로고    scopus 로고
    • The caveolae membrane system
    • Anderson, R. G. 1998. The caveolae membrane system. Annu. Rev. Biochem. 67:199.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 199
    • Anderson, R.G.1
  • 14
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown, D. A., and J. K. Rose. 1992. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68:533
    • (1992) Cell , vol.68 , pp. 533
    • Brown, D.A.1    Rose, J.K.2
  • 15
    • 0028820041 scopus 로고
    • A detergent-free method for purifying caveolae membrane from tissue culture cells
    • Smart, E. J., Y. S. Ying, C. Mineo, and R. G. Anderson. 1995. A detergent-free method for purifying caveolae membrane from tissue culture cells. Proc. Natl. Acad. Sci. USA 92:10104.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10104
    • Smart, E.J.1    Ying, Y.S.2    Mineo, C.3    Anderson, R.G.4
  • 16
    • 0029912981 scopus 로고    scopus 로고
    • Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains: Detergent-free purification of caveolae microdomains
    • Song, K. S., S. Li, T. Okamoto, L. A. Quilliam, M. Sargiacomo, and M. P. Lisanti. 1996. Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains: detergent-free purification of caveolae microdomains. J. Biol. Chem. 271:9690.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9690
    • Song, K.S.1    Li, S.2    Okamoto, T.3    Quilliam, L.A.4    Sargiacomo, M.5    Lisanti, M.P.6
  • 17
    • 0036733578 scopus 로고    scopus 로고
    • Cholesterol, lipid rafts, and disease
    • Simons, K., and R. Ehehalt. 2002. Cholesterol, lipid rafts, and disease. J. Clin. Invest. 110:597.
    • (2002) J. Clin. Invest. , vol.110 , pp. 597
    • Simons, K.1    Ehehalt, R.2
  • 18
    • 0035923728 scopus 로고    scopus 로고
    • Distinction between signaling mechanisms in lipid rafts vs. caveolae
    • Sowa, G., M. Pypaert, and W. C. Sessa. 2001. Distinction between signaling mechanisms in lipid rafts vs. caveolae. Proc. Natl. Acad. Sci. USA 98:14072.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14072
    • Sowa, G.1    Pypaert, M.2    Sessa, W.C.3
  • 19
    • 0030711558 scopus 로고    scopus 로고
    • Nitric oxide synthases: Which, where, how, and why?
    • Michel, T., and O. Feron. 1997. Nitric oxide synthases: which, where, how, and why? J. Clin. Invest. 100:2146.
    • (1997) J. Clin. Invest. , vol.100 , pp. 2146
    • Michel, T.1    Feron, O.2
  • 20
    • 0029901663 scopus 로고    scopus 로고
    • Targeting of nitric oxide synthase to endothelial cell caveolae via palmitoylation: Implications for nitric oxide signaling
    • Garcia-Cardena, G., P. Oh, J. Liu, J. E. Schnitzer, and W. C. Sessa. 1996. Targeting of nitric oxide synthase to endothelial cell caveolae via palmitoylation: implications for nitric oxide signaling. Proc. Natl. Acad. Sci. USA 93:6448.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6448
    • Garcia-Cardena, G.1    Oh, P.2    Liu, J.3    Schnitzer, J.E.4    Sessa, W.C.5
  • 21
    • 0039397709 scopus 로고    scopus 로고
    • Dissecting the interaction between nitric oxide synthase (NOS) and caveolin: Functional significance of the nos caveolin binding domain in vivo
    • Garcia-Cardena, G., P. Martasek, B. S. Masters, P. M. Skidd, J. Couet, S. Li, M. P. Lisanti, and W. C. Sessa. 1997. Dissecting the interaction between nitric oxide synthase (NOS) and caveolin: functional significance of the nos caveolin binding domain in vivo. J. Biol. Chem. 272:25437.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25437
    • Garcia-Cardena, G.1    Martasek, P.2    Masters, B.S.3    Skidd, P.M.4    Couet, J.5    Li, S.6    Lisanti, M.P.7    Sessa, W.C.8
  • 22
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder, T., P. Scheiffele, P. Verkade, and K. Simons. 1998. Lipid domain structure of the plasma membrane revealed by patching of membrane components. J. Cell Biol. 141:929.
    • (1998) J. Cell Biol. , vol.141 , pp. 929
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 23
    • 0024601050 scopus 로고
    • Endothelial leukocyte adhesion molecule 1: An inducible receptor for neutrophils related to complement regulatory proteins and lectins
    • Bevilacqua, M. P., S. Stengelin, M. A. Gimbrone, Jr., and B. Seed. 1989. Endothelial leukocyte adhesion molecule 1: an inducible receptor for neutrophils related to complement regulatory proteins and lectins. Science 243:1160.
    • (1989) Science , vol.243 , pp. 1160
    • Bevilacqua, M.P.1    Stengelin, S.2    Gimbrone M.A., Jr.3    Seed, B.4
  • 24
    • 0032101348 scopus 로고    scopus 로고
    • Membrane compartmentation is required for efficient T cell activation
    • Xavier, R., T. Brennan, Q. Li, C. McCormack, and B. Seed. 1998. Membrane compartmentation is required for efficient T cell activation. Immunity 8:723.
    • (1998) Immunity , vol.8 , pp. 723
    • Xavier, R.1    Brennan, T.2    Li, Q.3    McCormack, C.4    Seed, B.5
  • 25
    • 0032494169 scopus 로고    scopus 로고
    • Endothelial cell E- and P-selectin and vascular cell adhesion molecule-1 function as signaling receptors
    • Lorenzon, P., E. Vecile, E. Nardon, E. Ferrero, J. M. Harlan, F. Tedesco, and A. Dobrina. 1998. Endothelial cell E- and P-selectin and vascular cell adhesion molecule-1 function as signaling receptors. J. Cell Biol. 142:1381.
    • (1998) J. Cell Biol. , vol.142 , pp. 1381
    • Lorenzon, P.1    Vecile, E.2    Nardon, E.3    Ferrero, E.4    Harlan, J.M.5    Tedesco, F.6    Dobrina, A.7
  • 26
    • 0027964503 scopus 로고
    • A novel role for E- and P-selectins: Shape control of endothelial monolayers
    • Kaplanski, G. C. F., A. M. Benoliel, C. Foa, S. Kaplanski, and P. Bongrand. 1994. A novel role for E- and P-selectins: shape control of endothelial monolayers. J. Cell Sci. 107:2449.
    • (1994) J. Cell Sci. , vol.107 , pp. 2449
    • Kaplanski, G.C.F.1    Benoliel, A.M.2    Foa, C.3    Kaplanski, S.4    Bongrand, P.5
  • 27
    • 0033604513 scopus 로고    scopus 로고
    • Phospholipase C-γ as a signal-transducing element
    • Carpenter, G., and Q. Ji. 1999. Phospholipase C-γ as a signal-transducing element. Exp. Cell Res. 253:15.
    • (1999) Exp. Cell Res. , vol.253 , pp. 15
    • Carpenter, G.1    Ji, Q.2
  • 28
    • 0035972164 scopus 로고    scopus 로고
    • Real time fluorescence imaging of PLCγ translocation and its interaction with the epidermal growth factor receptor
    • Matsuda, M., H. F. Paterson, R. Rodriguez, A. C. Fensome, M. V. Ellis, K. Swann, and M. Katan. 2001. Real time fluorescence imaging of PLCγ translocation and its interaction with the epidermal growth factor receptor. J. Cell Biol. 153:599.
    • (2001) J. Cell Biol. , vol.153 , pp. 599
    • Matsuda, M.1    Paterson, H.F.2    Rodriguez, R.3    Fensome, A.C.4    Ellis, M.V.5    Swann, K.6    Katan, M.7
  • 29
    • 0032518666 scopus 로고    scopus 로고
    • Activation of phospholipase Cγ by PI 3-kinase-induced PH domain-mediated membrane targeting
    • Falasca, M., S. K. Logan, V. P. Lehto, G. Baccante, M. A. Lemmon, and J. Schlessinger. 1998. Activation of phospholipase Cγ by PI 3-kinase-induced PH domain-mediated membrane targeting. EMBO J. 17:414.
    • (1998) EMBO J. , vol.17 , pp. 414
    • Falasca, M.1    Logan, S.K.2    Lehto, V.P.3    Baccante, G.4    Lemmon, M.A.5    Schlessinger, J.6
  • 32
    • 0032566264 scopus 로고    scopus 로고
    • Phosphorylation of phospholipase Cγ1 on tyrosine residue 783 by platelet-derived growth factor regulates reorganization of the cytoskeleton
    • Yu, H., K. Fukami, T. Itoh, and T. Takenawa. 1998. Phosphorylation of phospholipase Cγ1 on tyrosine residue 783 by platelet-derived growth factor regulates reorganization of the cytoskeleton. Exp. Cell Res. 243:113.
    • (1998) Exp. Cell Res. , vol.243 , pp. 113
    • Yu, H.1    Fukami, K.2    Itoh, T.3    Takenawa, T.4
  • 34
    • 0033993454 scopus 로고    scopus 로고
    • Cholesterol depletion disrupts lipid rafts and modulates the activity of multiple signaling pathways in T lymphocytes
    • Kabouridis, P. S., J. Janzen, A. L. Magee, and S. C. Ley. 2000. Cholesterol depletion disrupts lipid rafts and modulates the activity of multiple signaling pathways in T lymphocytes. Eur. J. Immunol. 30:954.
    • (2000) Eur. J. Immunol. , vol.30 , pp. 954
    • Kabouridis, P.S.1    Janzen, J.2    Magee, A.L.3    Ley, S.C.4
  • 35
    • 0035936884 scopus 로고    scopus 로고
    • Localization of phospholipase C-γ1 signaling in caveolae: Importance in EGF-induced phosphoinositide hydrolysis but not in tyrosine phosphorylation
    • Jang, I. H., J. H. Kim, B. D. Lee, S. S. Bae, M. H. Park, P. G. Suh, and S. H. Ryu. 2001. Localization of phospholipase C-γ1 signaling in caveolae: importance in EGF-induced phosphoinositide hydrolysis but not in tyrosine phosphorylation. FEBS Lett. 491:4.
    • (2001) FEBS Lett. , vol.491 , pp. 4
    • Jang, I.H.1    Kim, J.H.2    Lee, B.D.3    Bae, S.S.4    Park, M.H.5    Suh, P.G.6    Ryu, S.H.7
  • 36
    • 0032987731 scopus 로고    scopus 로고
    • Role of phospholipase C, protein kinase C, and calcium in VEGF-induced venular hyperpermeability
    • Wu, H. M., Y. Yuan, D. C. Zawieja, J. Tinsley, and H. J. Granger. 1999. Role of phospholipase C, protein kinase C, and calcium in VEGF-induced venular hyperpermeability. Am. J. Physiol. 276: H535.
    • (1999) Am. J. Physiol. , vol.276
    • Wu, H.M.1    Yuan, Y.2    Zawieja, D.C.3    Tinsley, J.4    Granger, H.J.5
  • 37
    • 33947267193 scopus 로고    scopus 로고
    • FGF-2 facilitates binding of SH3 domain of PLC-γ1 to vinculin and SH2 domains to FGF receptor in corneal endothelial cells
    • Park, S. Y., E. Barron, P. G. Suh, S. H. Ryu, and E. P. Kay. 1999. FGF-2 facilitates binding of SH3 domain of PLC-γ1 to vinculin and SH2 domains to FGF receptor in corneal endothelial cells. Mol. Vis. 5:18.
    • (1999) Mol. Vis. , vol.5 , pp. 18
    • Park, S.Y.1    Barron, E.2    Suh, P.G.3    Ryu, S.H.4    Kay, E.P.5
  • 38
    • 0035033943 scopus 로고    scopus 로고
    • Cross-linking of brain endothelial intercellular adhesion molecule (ICAM)-1 induces association of ICAM-1 with detergent-insoluble cytoskeletal fraction
    • Amos, C., I. A. Romero, C. Schultze, J. Rousell, J. D. Pearson, J. Greenwood, and P. Adamson. 2001. Cross-linking of brain endothelial intercellular adhesion molecule (ICAM)-1 induces association of ICAM-1 with detergent-insoluble cytoskeletal fraction. Arterioscler. Thromb. Vasc. Biol. 21:810.
    • (2001) Arterioscler. Thromb. Vasc. Biol. , vol.21 , pp. 810
    • Amos, C.1    Romero, I.A.2    Schultze, C.3    Rousell, J.4    Pearson, J.D.5    Greenwood, J.6    Adamson, P.7
  • 39
    • 0035424240 scopus 로고    scopus 로고
    • 2 regulation of surface membrane traffic
    • 2 regulation of surface membrane traffic. Curr. Opin. Cell Biol. 13:493.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 493
    • Martin, T.F.1
  • 40
    • 0029926545 scopus 로고    scopus 로고
    • Localization and turnover of phosphatidylinositol 4, 5-bisphosphate in caveolin-enriched membrane domains
    • Pike, L. J., and L. Casey. 1996. Localization and turnover of phosphatidylinositol 4, 5-bisphosphate in caveolin-enriched membrane domains. J. Biol. Chem. 271:26453.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26453
    • Pike, L.J.1    Casey, L.2
  • 41
    • 0032575524 scopus 로고    scopus 로고
    • Cholesterol depletion delocalizes phosphatidylinositol bisphosphate and inhibits hormone-stimulated phosphatidylinositol turnover
    • Pike, L. J., and J. M. Miller. 1998. Cholesterol depletion delocalizes phosphatidylinositol bisphosphate and inhibits hormone-stimulated phosphatidylinositol turnover. J. Biol. Chem. 273:22298.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22298
    • Pike, L.J.1    Miller, J.M.2
  • 42
    • 0032555599 scopus 로고    scopus 로고
    • Association of ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2): Regulation by phosphatidylinositol 4,5-bisphosphate
    • Heiska, L., K. Alfthan, M. Gronholm, P. Vilja, A. Vaheri, and O. Carpen. 1998. Association of ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2): regulation by phosphatidylinositol 4,5-bisphosphate. J. Biol. Chem. 273:21893.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21893
    • Heiska, L.1    Alfthan, K.2    Gronholm, M.3    Vilja, P.4    Vaheri, A.5    Carpen, O.6
  • 44
    • 0032559637 scopus 로고    scopus 로고
    • Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2
    • Yonemura, S., M. Hirao, Y. Doi, N. Takahashi, T. Kondo, and S. Tsukita. 1998. Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2. J. Cell Biol. 140:885.
    • (1998) J. Cell Biol. , vol.140 , pp. 885
    • Yonemura, S.1    Hirao, M.2    Doi, Y.3    Takahashi, N.4    Kondo, T.5    Tsukita, S.6
  • 45
    • 0344416986 scopus 로고    scopus 로고
    • Monocyte adhesion and spreading on human endothelial cells is dependent on Rho-regulated receptor clustering
    • Wojciak-Stothard, B., L. Williams, and A. J. Ridley. 1999. Monocyte adhesion and spreading on human endothelial cells is dependent on Rho-regulated receptor clustering. J. Cell Biol. 145:1293.
    • (1999) J. Cell Biol. , vol.145 , pp. 1293
    • Wojciak-Stothard, B.1    Williams, L.2    Ridley, A.J.3
  • 46
    • 0034665316 scopus 로고    scopus 로고
    • ICAM-1-coupled cytoskeletal rearrangements and transendothelial lymphocyte migration involve intracellular calcium signaling in brain endothelial cell lines
    • Etienne-Manneville, S., J. B. Manneville, P. Adamson, B. Wilbourn, J. Greenwood, and P. O. Couraud. 2000. ICAM-1-coupled cytoskeletal rearrangements and transendothelial lymphocyte migration involve intracellular calcium signaling in brain endothelial cell lines. J. Immunol. 165:3375.
    • (2000) J. Immunol. , vol.165 , pp. 3375
    • Etienne-Manneville, S.1    Manneville, J.B.2    Adamson, P.3    Wilbourn, B.4    Greenwood, J.5    Couraud, P.O.6
  • 47
    • 4243619507 scopus 로고    scopus 로고
    • The Src-cortactin pathway is required for clustering of E-selectin and ICAM-1 in endothelial cells
    • Tilghman, R. W., and R. L. Hoover. 2002. The Src-cortactin pathway is required for clustering of E-selectin and ICAM-1 in endothelial cells. FASEB J. 7:7.
    • (2002) FASEB J. , vol.7 , pp. 7
    • Tilghman, R.W.1    Hoover, R.L.2
  • 48
    • 0037077718 scopus 로고    scopus 로고
    • E-selectin and ICAM-1 are incorporated into detergent-insoluble membrane domains following clustering in endothelial cells
    • Tilghman, R., and R. Hoover. 2002. E-selectin and ICAM-1 are incorporated into detergent-insoluble membrane domains following clustering in endothelial cells. FEBS Lett. 525:83.
    • (2002) FEBS Lett. , vol.525 , pp. 83
    • Tilghman, R.1    Hoover, R.2
  • 49
    • 0037087307 scopus 로고    scopus 로고
    • Lipid microdomain clustering induces a redistribution of antigen recognition and adhesion molecules on human T lymphocytes
    • Mitchell, J. S., O. Kanca, and B. W. McIntyre. 2002. Lipid microdomain clustering induces a redistribution of antigen recognition and adhesion molecules on human T lymphocytes. J. Immunol. 168:2737.
    • (2002) J. Immunol. , vol.168 , pp. 2737
    • Mitchell, J.S.1    Kanca, O.2    McIntyre, B.W.3
  • 51
    • 0028113411 scopus 로고
    • Signal transduction of a G protein-coupled receptor in caveolae: Colocalization of endothelin and its receptor with caveolin
    • Chun, M., U. K. Liyanage, M. P. Lisanti, and H. F. Lodish. 1994. Signal transduction of a G protein-coupled receptor in caveolae: colocalization of endothelin and its receptor with caveolin. Proc. Natl. Acad. Sci. USA 91:11728.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11728
    • Chun, M.1    Liyanage, U.K.2    Lisanti, M.P.3    Lodish, H.F.4


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