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Volumn 144, Issue 3, 1999, Pages 549-561

Evidence that distinct states of the integrin α6β1 interact with laminin and an ADAM

Author keywords

'avidity affinity modulation'; ADAM; Cell adhesion; Fertilin ; Integrin

Indexed keywords

CELL SURFACE PROTEIN; FERTILIN; INTEGRIN; LAMININ; MANGANESE CHLORIDE; PHORBOL MYRISTATE; UNCLASSIFIED DRUG;

EID: 0033535043     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.144.3.549     Document Type: Article
Times cited : (87)

References (76)
  • 2
    • 0031952651 scopus 로고    scopus 로고
    • Are changes in integrin affinity and conformation overemphasized?
    • Bazzoni, G., and M.E. Hemler. 1998. Are changes in integrin affinity and conformation overemphasized? Trends Biochem. Sci. 23:30-34.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 30-34
    • Bazzoni, G.1    Hemler, M.E.2
  • 3
    • 0030062129 scopus 로고    scopus 로고
    • Characterization of novel complexes on the cell surface between integrins and proteins with 4 transmembrane domains (TM4 proteins)
    • Berditchevski, F., M.M. Zutter, and M.E. Hemler. 1996. Characterization of novel complexes on the cell surface between integrins and proteins with 4 transmembrane domains (TM4 proteins). Mol. Biol. Cell. 7:193-207.
    • (1996) Mol. Biol. Cell. , vol.7 , pp. 193-207
    • Berditchevski, F.1    Zutter, M.M.2    Hemler, M.E.3
  • 4
    • 0027260907 scopus 로고
    • The integrin VLA-2 binds echovirus 1 and extracellular matrix ligands by different mechanisms
    • Bergelson, J.M., B.M. Chan, R.W. Finberg, and M.E. Hemler. 1993. The integrin VLA-2 binds echovirus 1 and extracellular matrix ligands by different mechanisms. J. Clin. Invest. 92:232-239.
    • (1993) J. Clin. Invest. , vol.92 , pp. 232-239
    • Bergelson, J.M.1    Chan, B.M.2    Finberg, R.W.3    Hemler, M.E.4
  • 5
    • 0030986652 scopus 로고    scopus 로고
    • A model for sperm-egg binding and fusion based on ADAMs and integrins
    • Bigler, D., M. Chen, S. Waters, and J.M. White. 1997. A model for sperm-egg binding and fusion based on ADAMs and integrins. Trends Cell Biol. 7:220-225.
    • (1997) Trends Cell Biol. , vol.7 , pp. 220-225
    • Bigler, D.1    Chen, M.2    Waters, S.3    White, J.M.4
  • 6
    • 0031698581 scopus 로고    scopus 로고
    • ADAMs: Focus on the protease domains. Curr
    • Black, R.A., and J.M. White. 1998. ADAMs: focus on the protease domains. Curr. Opin. Cell Biol. 10:654-659.
    • (1998) Opin. Cell Biol. , vol.10 , pp. 654-659
    • Black, R.A.1    White, J.M.2
  • 7
    • 0025371355 scopus 로고
    • Proteolytic processing of a protein involved in sperm-egg fusion correlates with the acquisition of fertilization competence
    • Blobel, C.P., D.G. Myles, P. Primakoff, and J.M. White. 1990. Proteolytic processing of a protein involved in sperm-egg fusion correlates with the acquisition of fertilization competence. J. Cell Biol. 111:69-78.
    • (1990) J. Cell Biol. , vol.111 , pp. 69-78
    • Blobel, C.P.1    Myles, D.G.2    Primakoff, P.3    White, J.M.4
  • 8
    • 0026510747 scopus 로고
    • A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion
    • Blobel, C.P., T.G. Wolfsberg, C.W. Turck, D.G. Myles, P. Primakoff, and J.M. White. 1992. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature. 356:248-252.
    • (1992) Nature , vol.356 , pp. 248-252
    • Blobel, C.P.1    Wolfsberg, T.G.2    Turck, C.W.3    Myles, D.G.4    Primakoff, P.5    White, J.M.6
  • 9
    • 0030566746 scopus 로고    scopus 로고
    • Where the outside meets the inside: Integrins as activators and targets of signal transduction cascades
    • Brown, E., and N. Hogg. 1996. Where the outside meets the inside: integrins as activators and targets of signal transduction cascades. Immunol. Lett. 54: 189-193.
    • (1996) Immunol. Lett. , vol.54 , pp. 189-193
    • Brown, E.1    Hogg, N.2
  • 11
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark, E.A., and J.S. Brugge. 1995. Integrins and signal transduction pathways: the road taken. Science. 268:233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 12
    • 0026571678 scopus 로고
    • Distribution patterns of extracellular matrix components and adhesion receptors are intricately modulated during first trimester cytotrophoblast differentiation along the invasive pathway, in vivo
    • Damsky, C.H., M.L. Fitzgerald, and S.J. Fisher. 1992. Distribution patterns of extracellular matrix components and adhesion receptors are intricately modulated during first trimester cytotrophoblast differentiation along the invasive pathway, in vivo. J. Clin. Invest. 89:210-222.
    • (1992) J. Clin. Invest. , vol.89 , pp. 210-222
    • Damsky, C.H.1    Fitzgerald, M.L.2    Fisher, S.J.3
  • 13
    • 0028900697 scopus 로고
    • Jararhagin and jaracetin: Novel snake venom inhibitors of the integrin collagen receptor. α2β1
    • DeLuca, M., C.M. Ward, K. Ohmori, R.K. Andrews, and M.C. Berndt. 1995. Jararhagin and jaracetin: novel snake venom inhibitors of the integrin collagen receptor. α2β1. Biochem. Biophys. Res. Commun. 206:570-576.
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 570-576
    • DeLuca, M.1    Ward, C.M.2    Ohmori, K.3    Andrews, R.K.4    Berndt, M.C.5
  • 14
    • 0029161166 scopus 로고
    • An alternatively spliced exon in the extracellular domain of the human α6 integrin subunit: Functional analysis of the α6 integrin variants
    • Delwel, G.O., I. Kuikman, and A. Sonnenberg. 1995. An alternatively spliced exon in the extracellular domain of the human α6 integrin subunit: functional analysis of the α6 integrin variants. Cell Adhes. Commun. 3:143-161.
    • (1995) Cell Adhes. Commun. , vol.3 , pp. 143-161
    • Delwel, G.O.1    Kuikman, I.2    Sonnenberg, A.3
  • 15
    • 0029665071 scopus 로고    scopus 로고
    • Cleavage of the α6A subunit is essential for activation of the α6Aβ1 integrin by phorbol-12-myristate-13-acetate
    • Delwel, G.O., F. Hogervorst, and A. Sonnenberg. 1996. Cleavage of the α6A subunit is essential for activation of the α6Aβ1 integrin by phorbol-12-myristate-13-acetate. J. Biol. Chem. 271:7293-7296.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7293-7296
    • Delwel, G.O.1    Hogervorst, F.2    Sonnenberg, A.3
  • 16
    • 0028446566 scopus 로고
    • The dynamic regulation of integrin adhesiveness
    • Diamond, M.S., and T.A. Springer. 1994. The dynamic regulation of integrin adhesiveness. Curr. Biol. 4:506-517.
    • (1994) Curr. Biol. , vol.4 , pp. 506-517
    • Diamond, M.S.1    Springer, T.A.2
  • 17
    • 0030272026 scopus 로고    scopus 로고
    • Receptors for laminins during epithelial morphogenesis
    • Ekblom, P. 1996. Receptors for laminins during epithelial morphogenesis. Curr. Opin. Cell Biol. 8:700-706.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 700-706
    • Ekblom, P.1
  • 18
    • 0029162781 scopus 로고
    • Mouse sperm-egg plasma membrane interactions: Analysis of roles of egg integrins and the mouse sperm homologue of PH-30 (fertilin) β
    • Evans, J.P., R.M. Schultz, and G.S. Kopf. 1995. Mouse sperm-egg plasma membrane interactions: analysis of roles of egg integrins and the mouse sperm homologue of PH-30 (fertilin) β. J. Cell Sci. 108:3267-3278.
    • (1995) J. Cell Sci. , vol.108 , pp. 3267-3278
    • Evans, J.P.1    Schultz, R.M.2    Kopf, G.S.3
  • 19
    • 0031193325 scopus 로고    scopus 로고
    • Characterization of the binding of recombinant mouse sperm fertilin β subunit to mouse eggs: Evidence for adhesive activity via an egg β1 integrin-mediated interaction
    • Evans, J.P., G.S. Kopf, and R.M. Schultz. 1997. Characterization of the binding of recombinant mouse sperm fertilin β subunit to mouse eggs: evidence for adhesive activity via an egg β1 integrin-mediated interaction. Dev. Biol. 187: 79-93.
    • (1997) Dev. Biol. , vol.187 , pp. 79-93
    • Evans, J.P.1    Kopf, G.S.2    Schultz, R.M.3
  • 20
    • 0028836388 scopus 로고
    • Dynamic regulation of integrins
    • Faull, R., and M.H. Ginsberg. 1995. Dynamic regulation of integrins. Stem Cells (Dayt). 13:38-46.
    • (1995) Stem Cells (Dayt) , vol.13 , pp. 38-46
    • Faull, R.1    Ginsberg, M.H.2
  • 21
    • 0030710958 scopus 로고    scopus 로고
    • Complementation of dominant suppression implicates CD98 in integrin activation
    • Fenczik, C.A., T. Sethl, J.W. Ramos, P.E. Hughes, and M.H. Ginsberg, 1997. Complementation of dominant suppression implicates CD98 in integrin activation. Nature. 390:81-85.
    • (1997) Nature , vol.390 , pp. 81-85
    • Fenczik, C.A.1    Sethl, T.2    Ramos, J.W.3    Hughes, P.E.4    Ginsberg, M.H.5
  • 22
    • 0028331312 scopus 로고
    • + requirements for capacitation and acrosomal exocytosis in mammalian sperm
    • + requirements for capacitation and acrosomal exocytosis in mammalian sperm. Int. Rev. Cytol. 149:1-49.
    • (1994) Int. Rev. Cytol. , vol.149 , pp. 1-49
    • Fraser, L.R.1
  • 23
    • 0030831124 scopus 로고    scopus 로고
    • Evidence that peptides derived from the disintegrin domain of primate fertilin and containing the ECD motif block the binding of human spermatozoa to the zona-free hamster oocyte Int
    • Gichuhi, P.M., W.C.L. Ford, and L. Hall. 1997. Evidence that peptides derived from the disintegrin domain of primate fertilin and containing the ECD motif block the binding of human spermatozoa to the zona-free hamster oocyte Int. J. Androl. 20:165-170.
    • (1997) J. Androl. , vol.20 , pp. 165-170
    • Gichuhi, P.M.1    Ford, W.C.L.2    Hall, L.3
  • 24
    • 0005645395 scopus 로고
    • The receptor for the subgroup A avian leukosis sarcoma virus binds to subgroup A but not to subgroup C envelope glycoprotein
    • Gilbert, J.M., P. Bates, H.E. Varmus, and J.M. White. 1994. The receptor for the subgroup A avian leukosis sarcoma virus binds to subgroup A but not to subgroup C envelope glycoprotein. J. Virol. 67:6889-6892.
    • (1994) J. Virol. , vol.67 , pp. 6889-6892
    • Gilbert, J.M.1    Bates, P.2    Varmus, H.E.3    White, J.M.4
  • 25
    • 0026582265 scopus 로고
    • α6β1 integrin and laminin E8: An increasingly complex simple story
    • Goodman, S.L. 1992. α6β1 integrin and laminin E8: an increasingly complex simple story. Kidney Int. 41:650-656.
    • (1992) Kidney Int. , vol.41 , pp. 650-656
    • Goodman, S.L.1
  • 28
    • 0031720629 scopus 로고    scopus 로고
    • Integrin associated proteins
    • Hemler, M.E. 1998. Integrin associated proteins. Curr. Opin. Cell Biol. 10:578-585.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 578-585
    • Hemler, M.E.1
  • 29
    • 0024539022 scopus 로고
    • Association of the VLA alpha 6 subunit with a novel protein. A possible alternative to the common VLa beta 1 subunit on certain cell lines
    • Hemler, M.E., C. Crouse, and A. Sonnenberg. 1989. Association of the VLA alpha 6 subunit with a novel protein. A possible alternative to the common VLA beta 1 subunit on certain cell lines. J. Biol. Chem. 264:6529-6535.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6529-6535
    • Hemler, M.E.1    Crouse, C.2    Sonnenberg, A.3
  • 30
    • 0025728732 scopus 로고
    • Integrin expression during human epidermal development in vivo and in vitro
    • Hertle, M.D., J.C. Adams, and F.M. Watt. 1991. Integrin expression during human epidermal development in vivo and in vitro. Development. 112:193-206.
    • (1991) Development , vol.112 , pp. 193-206
    • Hertle, M.D.1    Adams, J.C.2    Watt, F.M.3
  • 32
    • 0027390360 scopus 로고
    • Mechanistic studies of the plasma membrane block to polyspermy in mouse eggs
    • Horvath, P.M., T. Kellom, J. Caulfield, and J. Boldt. 1993. Mechanistic studies of the plasma membrane block to polyspermy in mouse eggs. Mol. Reprod. Dev. 34:65-72.
    • (1993) Mol. Reprod. Dev. , vol.34 , pp. 65-72
    • Horvath, P.M.1    Kellom, T.2    Caulfield, J.3    Boldt, J.4
  • 33
    • 0030909050 scopus 로고    scopus 로고
    • Suppression of integrin activation: A novel function of a Ras/Raf-initiated MAP kinase pathway
    • Hughes, P.E., M.W. Renshaw, M. Pfaff, J. Forsyth, V.M. Keivens, M.A. Schwartz, and M.H. Ginsberg. 1997. Suppression of integrin activation: a novel function of a Ras/Raf-initiated MAP kinase pathway. Cell. 88:521-530.
    • (1997) Cell , vol.88 , pp. 521-530
    • Hughes, P.E.1    Renshaw, M.W.2    Pfaff, M.3    Forsyth, J.4    Keivens, V.M.5    Schwartz, M.A.6    Ginsberg, M.H.7
  • 34
    • 0031282203 scopus 로고    scopus 로고
    • Analysis of the process of localization of fertilin to the sperm posterior head plasma membrane during sperm maturation in the epididymis
    • Hunnicutt, G.R., D.E. Koppel, and D.G. Myles. 1997. Analysis of the process of localization of fertilin to the sperm posterior head plasma membrane during sperm maturation in the epididymis. Dev. Biol. 191:146-159.
    • (1997) Dev. Biol. , vol.191 , pp. 146-159
    • Hunnicutt, G.R.1    Koppel, D.E.2    Myles, D.G.3
  • 35
    • 0026503656 scopus 로고
    • Contact and adhesive specificities in the associations, migrations, and targeting of cells and axons
    • Hynes, R.O., and A.D. Lander. 1992. Contact and adhesive specificities in the associations, migrations, and targeting of cells and axons. Cell. 68:303-322.
    • (1992) Cell , vol.68 , pp. 303-322
    • Hynes, R.O.1    Lander, A.D.2
  • 36
    • 0030273873 scopus 로고    scopus 로고
    • Snake venom metalloproteinases: Structure, function, and relationship to the ADAMs family of proteins
    • Jia, L.G., K. Shimokawa, J.B. Bjarnason, and J.W. Fox. 1996. Snake venom metalloproteinases: structure, function, and relationship to the ADAMs family of proteins. Toxicon. 34:1269-1276.
    • (1996) Toxicon , vol.34 , pp. 1269-1276
    • Jia, L.G.1    Shimokawa, K.2    Bjarnason, J.B.3    Fox, J.W.4
  • 37
    • 0029949611 scopus 로고    scopus 로고
    • Inhibition of collagen-induced platelet aggregation as the result of cleavage of α2β1-integrin by the snake venom metalloproteinase jararhagin
    • Kamiguti, A.S., C.R. Hay, and M. Zuzel. 1996. Inhibition of collagen-induced platelet aggregation as the result of cleavage of α2β1-integrin by the snake venom metalloproteinase jararhagin. Biochem. J. 320:635-641.
    • (1996) Biochem. J. , vol.320 , pp. 635-641
    • Kamiguti, A.S.1    Hay, C.R.2    Zuzel, M.3
  • 38
    • 0029913643 scopus 로고    scopus 로고
    • Adhesion-activating phorbol ester increases the mobility of leukocyte integrin LFA-1 in cultured lymphocytes
    • Kucik, D.F., M.L. Dustin, J.M. Miller, and E.J. Brown. 1996. Adhesion-activating phorbol ester increases the mobility of leukocyte integrin LFA-1 in cultured lymphocytes. J. Clin. Invest. 97:2139-2144.
    • (1996) J. Clin. Invest. , vol.97 , pp. 2139-2144
    • Kucik, D.F.1    Dustin, M.L.2    Miller, J.M.3    Brown, E.J.4
  • 39
    • 0030860515 scopus 로고    scopus 로고
    • The actin cytoskeleton is required for receptor-mediated endocytosis in mammalian cells
    • Lamaze, C., L.M. Fujimoto, H.L. Yin, and S.L. Schmid. 1997. The actin cytoskeleton is required for receptor-mediated endocytosis in mammalian cells. J. Biol. Chem. 272:20332-20335.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20332-20335
    • Lamaze, C.1    Fujimoto, L.M.2    Yin, H.L.3    Schmid, S.L.4
  • 40
    • 0023388241 scopus 로고
    • Actin-plasma membrane associations in mouse eggs and oocytes
    • Longo, F.J. 1987. Actin-plasma membrane associations in mouse eggs and oocytes. J. Exp. Zool. 243:299-309.
    • (1987) J. Exp. Zool. , vol.243 , pp. 299-309
    • Longo, F.J.1
  • 41
    • 0031018338 scopus 로고    scopus 로고
    • Dual role of the actin cytoskeleton in regulating cell adhesion mediated by the integrin lymphocyte function-associated molecule-1
    • Lub, M., Y. van Kooyk, S.J. van Vliet, and C.G. Figdor. 1997. Dual role of the actin cytoskeleton in regulating cell adhesion mediated by the integrin lymphocyte function-associated molecule-1. Mol. Biol. Cell. 8:341-351.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 341-351
    • Lub, M.1    Van Kooyk, Y.2    Van Vliet, S.J.3    Figdor, C.G.4
  • 42
    • 0031282021 scopus 로고    scopus 로고
    • Evidence for distinct serine protease activities with a potential role in processing the sperm protein fertilin
    • Lum, L., and C.P. Blobel. 1997. Evidence for distinct serine protease activities with a potential role in processing the sperm protein fertilin. Dev. Biol. 191: 131-145.
    • (1997) Dev. Biol. , vol.191 , pp. 131-145
    • Lum, L.1    Blobel, C.P.2
  • 43
    • 0028430978 scopus 로고
    • Sperm entry into fertilized mouse eggs
    • Maluchnik, D., and E. Borsuk. 1994. Sperm entry into fertilized mouse eggs. Zygote. 2:129-131.
    • (1994) Zygote , vol.2 , pp. 129-131
    • Maluchnik, D.1    Borsuk, E.2
  • 44
  • 45
    • 0026213743 scopus 로고
    • Laminin binding proteins
    • Mercurio, A.M., and L.M. Shaw. 1991. Laminin binding proteins. Bioessays. 13: 469-473.
    • (1991) Bioessays , vol.13 , pp. 469-473
    • Mercurio, A.M.1    Shaw, L.M.2
  • 46
    • 0028325475 scopus 로고
    • Identification of a binding site in the disintegrin domain of fertilin required for sperm egg fusion
    • Myles, D.G., L.H. Kimmel, C.P. Blobel, J.M. White, and P. Primakoff. 1994. Identification of a binding site in the disintegrin domain of fertilin required for sperm egg fusion. Proc. Natl. Acad. Sci. USA. 91:4195-4198.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4195-4198
    • Myles, D.G.1    Kimmel, L.H.2    Blobel, C.P.3    White, J.M.4    Primakoff, P.5
  • 47
    • 0028150753 scopus 로고
    • Disintegrins and other naturally occurring antagonists of platelet fibrinogen receptors
    • Niewiarowski, S., M.A. McLane, M. Kloczewiak, and G.J. Stewart. 1994. Disintegrins and other naturally occurring antagonists of platelet fibrinogen receptors. Semin. Hematol. 31:289-300.
    • (1994) Semin. Hematol. , vol.31 , pp. 289-300
    • Niewiarowski, S.1    McLane, M.A.2    Kloczewiak, M.3    Stewart, G.J.4
  • 48
    • 0025151870 scopus 로고
    • Evidence that protcolysis of the surface is an initial step in the mechanism of formation of sperm cell surface domains
    • Phelps, B.M., D.E. Koppel, P. Primakoff, and D.G. Myles. 1990. Evidence that protcolysis of the surface is an initial step in the mechanism of formation of sperm cell surface domains. J. Cell Biol. 111:1839-1847.
    • (1990) J. Cell Biol. , vol.111 , pp. 1839-1847
    • Phelps, B.M.1    Koppel, D.E.2    Primakoff, P.3    Myles, D.G.4
  • 49
    • 0032189153 scopus 로고    scopus 로고
    • Integrins take partners: Cross-talk between integrals and other membrane receptors
    • Porter, J.C., and N. Hogg. 1998. Integrins take partners: cross-talk between integrals and other membrane receptors. Trends Cell Biol. 8:390-396.
    • (1998) Trends Cell Biol. , vol.8 , pp. 390-396
    • Porter, J.C.1    Hogg, N.2
  • 50
    • 0029903961 scopus 로고    scopus 로고
    • Xenopus embryonic cell adhesion to fibronectin: Position-specific activation of RGD/synergy site-dependent migratory behavior at gastrulation
    • Ramos, J.W., and D.W. DeSimone. 1996. Xenopus embryonic cell adhesion to fibronectin: position-specific activation of RGD/synergy site-dependent migratory behavior at gastrulation. J. Cell Biol. 134:227-240.
    • (1996) J. Cell Biol. , vol.134 , pp. 227-240
    • Ramos, J.W.1    DeSimone, D.W.2
  • 51
    • 0022373626 scopus 로고
    • Localization of nonerythroid spectrin and actin in mouse oocytes and preimplantation embryos
    • Reima, I., and E. Lehtonen. 1985. Localization of nonerythroid spectrin and actin in mouse oocytes and preimplantation embryos. Differentiation. 30:68-75.
    • (1985) Differentiation , vol.30 , pp. 68-75
    • Reima, I.1    Lehtonen, E.2
  • 52
    • 0028984244 scopus 로고
    • Integrin receptor α6β1 is localized at specific sites of cell-cell contact in rat seminiferous epithelium
    • Salanova, M., M. Stefanini, I. De Curtis, and F. Palombi. 1995. Integrin receptor α6β1 is localized at specific sites of cell-cell contact in rat seminiferous epithelium. Biol. Reprod. 52:79-87.
    • (1995) Biol. Reprod. , vol.52 , pp. 79-87
    • Salanova, M.1    Stefanini, M.2    De Curtis, I.3    Palombi, F.4
  • 54
    • 0027332373 scopus 로고
    • Regulation of α6β1 integrin laminin receptor function by the cytoplasmic domain of the α6 subunit
    • Shaw, L.M., and A.M. Mercurio. 1993. Regulation of α6β1 integrin laminin receptor function by the cytoplasmic domain of the α6 subunit. J. Cell Biol. 123:1017-1025.
    • (1993) J. Cell Biol. , vol.123 , pp. 1017-1025
    • Shaw, L.M.1    Mercurio, A.M.2
  • 55
    • 0028356999 scopus 로고
    • Regulation of cellular interactions with laminin by integrin cytoplasmic domains: The A and B structural variants of the α6β1 integrin differentially modulate the adhesive strength, morphology, and migration of macrophages
    • Shaw, L.M., and A.M. Mercurio. 1994. Regulation of cellular interactions with laminin by integrin cytoplasmic domains: the A and B structural variants of the α6β1 integrin differentially modulate the adhesive strength, morphology, and migration of macrophages. Mol. Biol. Cell. 5:679-690.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 679-690
    • Shaw, L.M.1    Mercurio, A.M.2
  • 56
    • 0027258613 scopus 로고
    • Inside-out integrin signaling in macrophages. Analysis of the role of the α6Aβ1 and α6Bβ1 integrin variants in laminin adhesion by cDNA expression in an α6 integrin-deficient macrophage cell line
    • Shaw, L.M., M.M. Lotz, and A.M. Mercurio. 1993. Inside-out integrin signaling in macrophages. Analysis of the role of the α6Aβ1 and α6Bβ1 integrin variants in laminin adhesion by cDNA expression in an α6 integrin-deficient macrophage cell line. J. Biol. Chem. 268:11401-11408.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11401-11408
    • Shaw, L.M.1    Lotz, M.M.2    Mercurio, A.M.3
  • 57
    • 0023664709 scopus 로고
    • A complex of platelet glycoproteins Ic and IIa identified by a rat mAb
    • Sonnenberg, A., H. Janssen, F. Hogervorst, J. Calafat, and J. Hilgers. 1987. A complex of platelet glycoproteins Ic and IIa identified by a rat mAb. J. Biol. Chem. 262:10376-10383.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10376-10383
    • Sonnenberg, A.1    Janssen, H.2    Hogervorst, F.3    Calafat, J.4    Hilgers, J.5
  • 58
    • 0023812375 scopus 로고
    • Laminin receptor on platelets is the integrin VI.A-6
    • Sonnenberg, A., P.W. Modderman, and F. Hogervorst. 1988. Laminin receptor on platelets is the integrin VI.A-6. Nature. 336:487-489.
    • (1988) Nature , vol.336 , pp. 487-489
    • Sonnenberg, A.1    Modderman, P.W.2    Hogervorst, F.3
  • 59
    • 0024360298 scopus 로고
    • Latrunculins: Novel marine macrolides that disrupt microfilament organization and affect cell growth. I. Comparison with cytochalasin D
    • Spector, I., N.R. Shochet, D. Blasberger, and Y. Kashman. 1989. Latrunculins: novel marine macrolides that disrupt microfilament organization and affect cell growth. I. Comparison with cytochalasin D. Cell Motil. Cytoskeleton. 13: 127-144.
    • (1989) Cell Motil. Cytoskeleton. , vol.13 , pp. 127-144
    • Spector, I.1    Shochet, N.R.2    Blasberger, D.3    Kashman, Y.4
  • 60
    • 0019148893 scopus 로고
    • An improved culture medium for mouse blastocysts
    • Spindle, A. 1980. An improved culture medium for mouse blastocysts. In Vitro. 16:669-674.
    • (1980) In Vitro , vol.16 , pp. 669-674
    • Spindle, A.1
  • 61
    • 0027142391 scopus 로고
    • Targeted deletion of β1 integrins in F9 embryonal carcinoma cells affects morphological differentiation but not tissue-specific gene expression
    • Stephens, L.E., J.E. Sonne, M.L. Fitzgerald, and C.H. Damsky. 1993. Targeted deletion of β1 integrins in F9 embryonal carcinoma cells affects morphological differentiation but not tissue-specific gene expression. J. Cell Biol. 123: 1607-1620.
    • (1993) J. Cell Biol. , vol.123 , pp. 1607-1620
    • Stephens, L.E.1    Sonne, J.E.2    Fitzgerald, M.L.3    Damsky, C.H.4
  • 63
    • 0027505080 scopus 로고
    • Developmental regulation of integrin expression at the time of implantation in the mouse embryo
    • Sutherland, A.E., P.G. Calarco, and C.H. Damsky. 1993. Developmental regulation of integrin expression at the time of implantation in the mouse embryo. Development. 119:1175-1186.
    • (1993) Development , vol.119 , pp. 1175-1186
    • Sutherland, A.E.1    Calarco, P.G.2    Damsky, C.H.3
  • 64
    • 0029150138 scopus 로고
    • Synchronous sperm penetration of zona-free mouse eggs in vitro
    • Takahashi, Y., C. Meno, E. Sato, and Y. Toyoda. 1995. Synchronous sperm penetration of zona-free mouse eggs in vitro. Biol. Reprod. 53:424-430.
    • (1995) Biol. Reprod. , vol.53 , pp. 424-430
    • Takahashi, Y.1    Meno, C.2    Sato, E.3    Toyoda, Y.4
  • 66
    • 0028176149 scopus 로고
    • 2+ modulates leukocyte function-associated antigen-1 cell surface distribution on T lymphocytes and consequently affects cell adhesion
    • 2+ modulates leukocyte function-associated antigen-1 cell surface distribution on T lymphocytes and consequently affects cell adhesion. J. Cell Biol. 124: 1061-1070.
    • (1994) J. Cell Biol. , vol.124 , pp. 1061-1070
    • Van Kooyk, Y.1    Weder, P.2    Heije, K.3    Figdor, C.G.4
  • 67
    • 0030940446 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of bovine fertilin α and β (ADAM 1 and ADAM 2): A candidate sperm-egg binding/fusion complex
    • Waters, S.I., and J.M. White. 1997. Biochemical and molecular characterization of bovine fertilin α and β (ADAM 1 and ADAM 2): a candidate sperm-egg binding/fusion complex. Biol. Reprod. 56:1245-1254.
    • (1997) Biol. Reprod. , vol.56 , pp. 1245-1254
    • Waters, S.I.1    White, J.M.2
  • 68
    • 0030902384 scopus 로고    scopus 로고
    • Integrin signaling in leukocytes: Lessons from the α6β1 integrin
    • Wei, J., L.M. Shaw, and A.M. Mercurio. 1997. Integrin signaling in leukocytes: lessons from the α6β1 integrin. J. Leukocyte Biol. 61:397-407.
    • (1997) J. Leukocyte Biol. , vol.61 , pp. 397-407
    • Wei, J.1    Shaw, L.M.2    Mercurio, A.M.3
  • 69
    • 0026935755 scopus 로고
    • Disintegrins: RGD-containing proteins which inhibit cell matrix interactions (adhesion) and cell-cell interactions (aggregation) via the integrin receptors
    • Williams, J.A. 1992. Disintegrins: RGD-containing proteins which inhibit cell matrix interactions (adhesion) and cell-cell interactions (aggregation) via the integrin receptors. Pathol. Biol. 40:813-821.
    • (1992) Pathol. Biol. , vol.40 , pp. 813-821
    • Williams, J.A.1
  • 70
    • 0030589505 scopus 로고    scopus 로고
    • ADAMs in fertilization and development
    • Wolfsberg, T.G., and J.M. White. 1996. ADAMs in fertilization and development. Dev. Biol. 180:389-401.
    • (1996) Dev. Biol. , vol.180 , pp. 389-401
    • Wolfsberg, T.G.1    White, J.M.2
  • 71
    • 0018253891 scopus 로고
    • Calcium requirement for sperm-egg fusion in mammals
    • Yanagimachi, R. 1978. Calcium requirement for sperm-egg fusion in mammals. Biol. Reprod. 19:949-958.
    • (1978) Biol. Reprod. , vol.19 , pp. 949-958
    • Yanagimachi, R.1
  • 72
    • 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, S.-K. Kraeft, L.B. Chen, M.P. Sheetz, and 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    Kraeft, S.-K.3    Chen, L.B.4    Sheetz, M.P.5    Hemler, M.E.6
  • 73
    • 0030951614 scopus 로고    scopus 로고
    • A role for the disintegrin domain of cyritestin, a sperm surface protein belonging to the ADAM family, in mouse sperm-egg plasma membrane adhesion and fusion
    • Yuan, R., P. Primakoff, and D.G. Myles. 1997. A role for the disintegrin domain of cyritestin, a sperm surface protein belonging to the ADAM family, in mouse sperm-egg plasma membrane adhesion and fusion. J. Cell Biol. 137:105-112.
    • (1997) J. Cell Biol. , vol.137 , pp. 105-112
    • Yuan, R.1    Primakoff, P.2    Myles, D.G.3
  • 74
  • 75
    • 0032571315 scopus 로고    scopus 로고
    • Specific interaction of the recombinant disintegrin-like domain of MDC-15 (Metargidin, ADAM-15) with integrin αvβ3
    • Zhang, X.-P., T. Kamata, K. Yokoyama, W. Puzon-McLaughlin, and Y. Takada. 1998. Specific interaction of the recombinant disintegrin-like domain of MDC-15 (Metargidin, ADAM-15) with integrin αvβ3. J. Biol. Chem. 273:7345-7350.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7345-7350
    • Zhang, X.-P.1    Kamata, T.2    Yokoyama, K.3    Puzon-McLaughlin, W.4    Takada, Y.5
  • 76
    • 0030840417 scopus 로고    scopus 로고
    • The laminin-binding activity of the alpha 7 integrin receptor is defined by developmentally regulated splicing in the extracellular domain
    • Ziober, B.L., Y. Chen, and R.H. Kramer. 1997. The laminin-binding activity of the alpha 7 integrin receptor is defined by developmentally regulated splicing in the extracellular domain. Mol. Biol. Cell. 8:1723-1734.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 1723-1734
    • Ziober, B.L.1    Chen, Y.2    Kramer, R.H.3


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