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Volumn 12, Issue , 1996, Pages 697-715

RGD and other recognition sequences for integrins

Author keywords

cell adhesion; cell migration; extracellular matrix; peptides

Indexed keywords

ARGINYLGLYCYLASPARTIC ACID; BINDING PROTEIN; CELL SURFACE PROTEIN; CELL SURFACE RECEPTOR; CYCLOPEPTIDE; INTEGRIN; SYNTHETIC PEPTIDE;

EID: 0029775681     PISSN: 10810706     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.cellbio.12.1.697     Document Type: Review
Times cited : (2684)

References (102)
  • 5
    • 0027220944 scopus 로고
    • The TAT protein of HIV-1, a growth factor for AIDS-Kaposi's sarcoma and cytokine-activated vascular cells, induces adhesion of the same cell-types by using integrin receptors recognizing the RGD amino-acid sequence
    • Barillari G, Gendelman R, Gallo RC, Ensoli B. 1993. The TAT protein of HIV-1, a growth factor for AIDS-Kaposi's sarcoma and cytokine-activated vascular cells, induces adhesion of the same cell-types by using integrin receptors recognizing the RGD amino-acid sequence. Proc. Natl. Acad. Sci. USA 90:7941-45
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7941-7945
    • Barillari, G.1    Gendelman, R.2    Gallo, R.C.3    Ensoli, B.4
  • 6
    • 0024547527 scopus 로고
    • Tenascin mediates cell attachment through an RGD-dependent receptor
    • Bourdon M, Ruoslahti E. 1989. Tenascin mediates cell attachment through an RGD-dependent receptor. J. Cell Biol. 108:1149-55
    • (1989) J. Cell Biol. , vol.108 , pp. 1149-1155
    • Bourdon, M.1    Ruoslahti, E.2
  • 8
    • 0025162671 scopus 로고
    • Identification of an Arg-Gly-Asp (RGD) cell adhesion site in human immunodeficiency virus type 1 transactivation protein, tat
    • Brake DA, Debouck C, Biesecker G. 1990. Identification of an Arg-Gly-Asp (RGD) cell adhesion site in human immunodeficiency virus type 1 transactivation protein, tat. J. Cell Biol. 111:1275-81
    • (1990) J. Cell Biol. , vol.111 , pp. 1275-1281
    • Brake, D.A.1    Debouck, C.2    Biesecker, G.3
  • 11
    • 0026671979 scopus 로고
    • Drosophila PS2 integrin mediates RGD-dependent cell-matrix interactions
    • Bunch TA, Brower DL. 1992. Drosophila PS2 integrin mediates RGD-dependent cell-matrix interactions. Development 116:239-47
    • (1992) Development , vol.116 , pp. 239-247
    • Bunch, T.A.1    Brower, D.L.2
  • 12
    • 0027378219 scopus 로고
    • Glycoprotein IIb peptide-656-667 mimics the fibrinogen gamma-chain-402-411 binding-site on platelet integrin GPIIb/IIIa
    • Calvete JJ, Rivas G, Schafer W, McLane MA, Niewiarowski S. 1993. Glycoprotein IIb peptide-656-667 mimics the fibrinogen gamma-chain-402-411 binding-site on platelet integrin GPIIb/IIIa. FEBS Lett. 335:132-35
    • (1993) FEBS Lett. , vol.335 , pp. 132-135
    • Calvete, J.J.1    Rivas, G.2    Schafer, W.3    McLane, M.A.4    Niewiarowski, S.5
  • 15
    • 0028276559 scopus 로고
    • Crystals of the cell-binding module of fibronectin obtained from a series of recombinant fragments differing in length
    • Dickinson CD, Gay DA, Parello J, Ruoslahti E, Ely KR. 1994. Crystals of the cell-binding module of fibronectin obtained from a series of recombinant fragments differing in length. J. Mol. Biol. 237:123-27
    • (1994) J. Mol. Biol. , vol.237 , pp. 123-127
    • Dickinson, C.D.1    Gay, D.A.2    Parello, J.3    Ruoslahti, E.4    Ely, K.R.5
  • 16
    • 0025216612 scopus 로고
    • The ligand binding site of the platelet integrin receptor GPIIb-IIIa is proximal to the second calcium binding domain of its α-subunit
    • D' Souza SE, Ginsberg MH, Burke TA, Plow EF. 1990. The ligand binding site of the platelet integrin receptor GPIIb-IIIa is proximal to the second calcium binding domain of its α-subunit. J. Biol. Chem. 265:3440-46
    • (1990) J. Biol. Chem. , vol.265 , pp. 3440-3446
    • D' Souza, S.E.1    Ginsberg, M.H.2    Burke, T.A.3    Plow, E.F.4
  • 17
    • 0024280898 scopus 로고
    • Localization of an Arg-Gly-Asp recognition site within an integrin adhesion receptor
    • D' Souza SE, Ginsberg MH, Burke TA, Lam SC-T, Plow EF. 1988. Localization of an Arg-Gly-Asp recognition site within an integrin adhesion receptor. Science 242:91-93
    • (1988) Science , vol.242 , pp. 91-93
    • D' Souza, S.E.1    Ginsberg, M.H.2    Burke, T.A.3    Lam, S.C.-T.4    Plow, E.F.5
  • 20
    • 0023920778 scopus 로고
    • 2+: A possible role for unusual binding sites for divalent cations in receptors for proteins containing Arg-Gly-Asp
    • 2+: a possible role for unusual binding sites for divalent cations in receptors for proteins containing Arg-Gly-Asp. J. Cell Sci. 89:507-13
    • (1988) J. Cell Sci. , vol.89 , pp. 507-513
    • Edwards, J.1    Hameed, H.2    Campbell, G.3
  • 21
    • 0025344596 scopus 로고
    • Tat protein of HIV-1 stimulates growth of cells derived from Kaposi's sarcoma lesions of AIDs patients
    • Ensoli B, Barillari G, Salahuddin SZ, Gallo RC, Wong-Staal F. 1990. Tat protein of HIV-1 stimulates growth of cells derived from Kaposi's sarcoma lesions of AIDs patients. Nature 345:84-86
    • (1990) Nature , vol.345 , pp. 84-86
    • Ensoli, B.1    Barillari, G.2    Salahuddin, S.Z.3    Gallo, R.C.4    Wong-Staal, F.5
  • 22
    • 0025874744 scopus 로고
    • Two integrin-binding peptides abrogate T cell-mediated immune responses in vitro
    • Ferguson TA, Mizutani H, Kupper T. 1991. Two integrin-binding peptides abrogate T cell-mediated immune responses in vitro. Proc. Natl. Acad. Sci. USA 88:8072-76
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8072-8076
    • Ferguson, T.A.1    Mizutani, H.2    Kupper, T.3
  • 23
    • 0027450510 scopus 로고
    • Inhibition of osteoclastic bone resorption in vivo by echistatin. "An Arginyl-Glycyl-Aspartyl" (RGD)-containing protein
    • Fisher JE, Caulfield MP, Sato M, Quartuccio HA, Gould RJ, et al. 1993. Inhibition of osteoclastic bone resorption in vivo by echistatin. "An Arginyl-Glycyl-Aspartyl" (RGD)-containing protein. Endocrinology 132:1411-13
    • (1993) Endocrinology , vol.132 , pp. 1411-1413
    • Fisher, J.E.1    Caulfield, M.P.2    Sato, M.3    Quartuccio, H.A.4    Gould, R.J.5
  • 25
    • 0022273672 scopus 로고
    • Interaction of fibronectin with its receptor on platelets
    • Gardner JM, Hynes RO. 1985. Interaction of fibronectin with its receptor on platelets. Cell 42:439-48
    • (1985) Cell , vol.42 , pp. 439-448
    • Gardner, J.M.1    Hynes, R.O.2
  • 26
    • 0022385454 scopus 로고
    • The tetrapeptide analog of the cell attachment site of fibronectin inhibits platelet aggregation and fibrinogen binding to activated platelets
    • Gartner TK, Bennett JS. 1985. The tetrapeptide analog of the cell attachment site of fibronectin inhibits platelet aggregation and fibrinogen binding to activated platelets. J. Biol. Chem. 260:11891-94
    • (1985) J. Biol. Chem. , vol.260 , pp. 11891-11894
    • Gartner, T.K.1    Bennett, J.S.2
  • 27
    • 0025681557 scopus 로고
    • The amino acid sequence gly-ala-pro-leu appears to be a fibrinogen binding site in the platelet integrin, glycoprotein IIb
    • Gartner TK, Taylor DB. 1990. The amino acid sequence gly-ala-pro-leu appears to be a fibrinogen binding site in the platelet integrin, glycoprotein IIb. Thromb. Res. 60:291-309
    • (1990) Thromb. Res. , vol.60 , pp. 291-309
    • Gartner, T.K.1    Taylor, D.B.2
  • 28
    • 0027082156 scopus 로고
    • A 109-amino acid C-terminal fragment of Alzheimer's-disease amyloid percursor protein contains a sequence, RHDS, that promotes cell adhesion
    • Ghiso J, Rostagno A, Gardella JE, Liem L, Gorevic PD, Frangione BA. 1992. A 109-amino acid C-terminal fragment of Alzheimer's-disease amyloid percursor protein contains a sequence, RHDS, that promotes cell adhesion. Biochem. J. 288:1053-59
    • (1992) Biochem. J. , vol.288 , pp. 1053-1059
    • Ghiso, J.1    Rostagno, A.2    Gardella, J.E.3    Liem, L.4    Gorevic, P.D.5    Frangione, B.A.6
  • 31
    • 0027102818 scopus 로고
    • Conformation/activity studies of rationally designed potent anti-adhesive RGD peptides
    • Gurrath M, Muller G, Kessler H, Aumailley M, Timpl R. 1992. Conformation/activity studies of rationally designed potent anti-adhesive RGD peptides. Eur. J. Biochem. 270:911-21
    • (1992) Eur. J. Biochem. , vol.270 , pp. 911-921
    • Gurrath, M.1    Muller, G.2    Kessler, H.3    Aumailley, M.4    Timpl, R.5
  • 32
    • 0027135270 scopus 로고
    • Inhibition of metastatic cell colonization in murine lungs and tumor-induced morbidity by non-peptidic Arg-Gly-Asp mimetics
    • Hardan I, Weiss L, Hershkovitz R, Greenspoon N, Alon R, et al. 1993. Inhibition of metastatic cell colonization in murine lungs and tumor-induced morbidity by non-peptidic Arg-Gly-Asp mimetics. Int. J. Cancer 55:1023-28
    • (1993) Int. J. Cancer , vol.55 , pp. 1023-1028
    • Hardan, I.1    Weiss, L.2    Hershkovitz, R.3    Greenspoon, N.4    Alon, R.5
  • 34
    • 0024587422 scopus 로고
    • Effects of modifications of the RGD sequence and its context on recognition by the fibronectin receptor
    • Hautanen A, Gailit J, Mann DM, Ruoslahti E. 1989. Effects of modifications of the RGD sequence and its context on recognition by the fibronectin receptor. J. Biol. Chem. 264:1437-42
    • (1989) J. Biol. Chem. , vol.264 , pp. 1437-1442
    • Hautanen, A.1    Gailit, J.2    Mann, D.M.3    Ruoslahti, E.4
  • 36
    • 0029096892 scopus 로고
    • Protein ligands of the human adenovirus type 2 outer capsid identified by biopanning of a phage-displayed peptide library on separate domains of wild-type and mutant penton capsomers
    • Hong SS, Boulanger P. 1995. Protein ligands of the human adenovirus type 2 outer capsid identified by biopanning of a phage-displayed peptide library on separate domains of wild-type and mutant penton capsomers. EMBO J. 14:4714-27
    • (1995) EMBO J. , vol.14 , pp. 4714-4727
    • Hong, S.S.1    Boulanger, P.2
  • 37
    • 0028987384 scopus 로고
    • 5 on human monocytes and T lymphocytes facilitates adenovirus-mediated gene delivery
    • 5 on human monocytes and T lymphocytes facilitates adenovirus-mediated gene delivery. J. Virol. 69:2257-63
    • (1995) J. Virol. , vol.69 , pp. 2257-2263
    • Huang, S.1    Endo, R.I.2    Nemerow, G.R.3
  • 38
    • 0022870911 scopus 로고
    • Identification of an alternatively spliced site in human plasma fibronectin that mediates cell type-specific adhesion
    • Humphries MJ, Akiyama SK, Komoriya A, Olden K, Yamada KM. 1986. Identification of an alternatively spliced site in human plasma fibronectin that mediates cell type-specific adhesion. J. Cell Biol. 103:2637-47
    • (1986) J. Cell Biol. , vol.103 , pp. 2637-2647
    • Humphries, M.J.1    Akiyama, S.K.2    Komoriya, A.3    Olden, K.4    Yamada, K.M.5
  • 39
    • 0024844513 scopus 로고
    • Primary sequence of a motor neuron-selective adhesive site in the synaptic basal lamina protein S-laminin
    • Hunter DD, Porter BE, Bulock JW, Adams SP, Merlie JP, Sanes JR. 1989. Primary sequence of a motor neuron-selective adhesive site in the synaptic basal lamina protein S-laminin. Cell 59:905-13
    • (1989) Cell , vol.59 , pp. 905-913
    • Hunter, D.D.1    Porter, B.E.2    Bulock, J.W.3    Adams, S.P.4    Merlie, J.P.5    Sanes, J.R.6
  • 40
    • 0027497077 scopus 로고
    • Endothelial cells adhere to the RGD domain and the fibrinogen-like terminal knob of tenascin
    • Joshi P, Chung C-Y, Aukhil I, Erickson HP. 1993. Endothelial cells adhere to the RGD domain and the fibrinogen-like terminal knob of tenascin. J. Cell Sci. 106:389-400
    • (1993) J. Cell Sci. , vol.106 , pp. 389-400
    • Joshi, P.1    Chung, C.-Y.2    Aukhil, I.3    Erickson, H.P.4
  • 43
    • 0028899525 scopus 로고
    • Phage libraries displaying cyclic peptides with different ring size: Ligand specificities of the RGD-directed integrins
    • Koivunen E, Wang B, Ruoslahti E. 1995. Phage libraries displaying cyclic peptides with different ring size: ligand specificities of the RGD-directed integrins. Biotechnology 13:265-70
    • (1995) Biotechnology , vol.13 , pp. 265-270
    • Koivunen, E.1    Wang, B.2    Ruoslahti, E.3
  • 44
    • 0021319857 scopus 로고
    • Platelet receptor recognition site on human fibrinogen. Synthesis and structure-function relationship of peptides corresponding to the carboxy-terminal segment of the gamma chain
    • Kloczewiak M, Timmons S, Lukas TJ, Hawiger J. 1984. Platelet receptor recognition site on human fibrinogen. Synthesis and structure-function relationship of peptides corresponding to the carboxy-terminal segment of the gamma chain. Biochemistry 23:1767-74
    • (1984) Biochemistry , vol.23 , pp. 1767-1774
    • Kloczewiak, M.1    Timmons, S.2    Lukas, T.J.3    Hawiger, J.4
  • 45
    • 0028929054 scopus 로고
    • Crystal structure of the OPG2 Fab. An anti-receptor antibody that mimics an RGD cell adhesion site
    • Kodandapani R, Veerapandian B, Kunicki TJ, Ely KR. 1995. Crystal structure of the OPG2 Fab. An anti-receptor antibody that mimics an RGD cell adhesion site. J. Biol. Chem. 270:2268-73
    • (1995) J. Biol. Chem. , vol.270 , pp. 2268-2273
    • Kodandapani, R.1    Veerapandian, B.2    Kunicki, T.J.3    Ely, K.R.4
  • 46
    • 0023663947 scopus 로고
    • Evidence that arginyl-glycyl-aspartate peptides and fibrinogen alpha chain peptides share a common binding site on platelets
    • Lam SC-T, Plow EF, Smith MA, Andrieux A, Ryckwaert JJ, et al. 1987. Evidence that arginyl-glycyl-aspartate peptides and fibrinogen alpha chain peptides share a common binding site on platelets. J. Biol Chem. 262: 947-56
    • (1987) J. Biol Chem. , vol.262 , pp. 947-956
    • Lam, S.C.-T.1    Plow, E.F.2    Smith, M.A.3    Andrieux, A.4    Ryckwaert, J.J.5
  • 48
    • 0026490256 scopus 로고
    • Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein
    • Leahy DJ, Hendrickson WA, Aukhil I, Erickson HP. 1992. Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Science 258:987-91
    • (1992) Science , vol.258 , pp. 987-991
    • Leahy, D.J.1    Hendrickson, W.A.2    Aukhil, I.3    Erickson, H.P.4
  • 49
    • 0028986196 scopus 로고
    • Crystal structure of the a domain from the a subunit of integrin CR3 (CD11b/CD18)
    • Lee J-O, Rieu P, Arnaout MA, Liddington R. 1995. Crystal structure of the A domain from the a subunit of integrin CR3 (CD11b/CD18). Cell 80:631-38
    • (1995) Cell , vol.80 , pp. 631-638
    • Lee, J.-O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 50
    • 0026020971 scopus 로고
    • Pertactin, an Arg-Gly-Asp-containing Bordetella pertussis surface protein that promotes adherence of mammalian cells
    • Leininger E, Roberts M, Kenimer JG, Charle IG, Fairweather N, et al. 1991. Pertactin, an Arg-Gly-Asp-containing Bordetella pertussis surface protein that promotes adherence of mammalian cells. Proc. Natl. Acad. Sci. USA 88:345-49
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 345-349
    • Leininger, E.1    Roberts, M.2    Kenimer, J.G.3    Charle, I.G.4    Fairweather, N.5
  • 51
    • 0027372386 scopus 로고
    • A leukocyte integrin binding peptide from intercellular adhesion molecule-2 stimulates T cell adhesion and natural killer cell activity
    • Li R, Nortamo P, Kantor C, Kovanen P, Timonen T, Gahmberg CG. 1993. A leukocyte integrin binding peptide from intercellular adhesion molecule-2 stimulates T cell adhesion and natural killer cell activity. J. Biol. Chem. 268:21474-77
    • (1993) J. Biol. Chem. , vol.268 , pp. 21474-21477
    • Li, R.1    Nortamo, P.2    Kantor, C.3    Kovanen, P.4    Timonen, T.5    Gahmberg, C.G.6
  • 52
    • 0026496886 scopus 로고
    • The three-dimensional structure of the tenth type III module of fibronectin: An insight into RGD-mediated interactions
    • Main AL, Harvey TS, Baron M, Boyd J, Campbell ID. 1992. The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions. Cell 71:671-78
    • (1992) Cell , vol.71 , pp. 671-678
    • Main, A.L.1    Harvey, T.S.2    Baron, M.3    Boyd, J.4    Campbell, I.D.5
  • 53
    • 0027483226 scopus 로고
    • 2 integrin CR3 (CD11b/CD18) is essential for ligand binding
    • 2 integrin CR3 (CD11b/CD18) is essential for ligand binding. Cell 72:857-67
    • (1993) Cell , vol.72 , pp. 857-867
    • Michiashita, M.1    Videm, V.2    Arnaot, M.A.3
  • 54
    • 0025932687 scopus 로고
    • 1 in the COOH-terminal heparin-binding domain of fibronectin
    • 1 in the COOH-terminal heparin-binding domain of fibronectin. EMBO J. 10:4089-95
    • (1991) EMBO J. , vol.10 , pp. 4089-4095
    • Mould, A.P.1    Humphries, M.J.2
  • 56
    • 0028325475 scopus 로고
    • Identification of a binding site in the distintegrin domain of fertilin required for sperm-egg fusion
    • Myles DG, Kimmel LH, Blobel CP, White JM, Primakoff P. 1994. Identification of a binding site in the distintegrin domain of fertilin required for sperm-egg fusion. Proc. Natl. Acad. Sci. USA 91:4195-98
    • (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
  • 57
    • 0023506887 scopus 로고
    • Alternative splicing of chicken fibronectin in embryos and in normal and transformed cells
    • Norton PA, Hynes RO. 1987. Alternative splicing of chicken fibronectin in embryos and in normal and transformed cells. Mol. Cell. Biol. 7:4297-307
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 4297-4307
    • Norton, P.A.1    Hynes, R.O.2
  • 59
    • 0024292679 scopus 로고
    • Site-directed mutagenesis of the cell-binding domain of human fibronectin: Separable, synergistic sites mediate adhesive function
    • Obara M, Kang M, Yamada KM. 1988. Site-directed mutagenesis of the cell-binding domain of human fibronectin: Separable, synergistic sites mediate adhesive function. Cell 53:649-57
    • (1988) Cell , vol.53 , pp. 649-657
    • Obara, M.1    Kang, M.2    Yamada, K.M.3
  • 60
    • 0028950139 scopus 로고
    • 1 integrin with the synergistic region of the central cell-binding domain of fibronectin in cells to fibronectin binding
    • 1 integrin with the synergistic region of the central cell-binding domain of fibronectin in cells to fibronectin binding. Exp. Cell Res. 216:273-76
    • (1995) Exp. Cell Res. , vol.216 , pp. 273-276
    • Obara, M.1    Yoshizato, K.2
  • 62
    • 0029120428 scopus 로고
    • A peptide isolated from phage display libraries is a structural and functional mimic of an RGD-binding site on integrins
    • Pasqualini R, Koivunen E, Ruoslahti E. 1995. A peptide isolated from phage display libraries is a structural and functional mimic of an RGD-binding site on integrins. J Cell Biol. 130:1189-96
    • (1995) J Cell Biol. , vol.130 , pp. 1189-1196
    • Pasqualini, R.1    Koivunen, E.2    Ruoslahti, E.3
  • 63
    • 0026185250 scopus 로고
    • Synthesis, NMR and function of an 0-phosphorylated peptide, comprising the RGD-adhesion sequence of osteopontin
    • Pettersson E, Lüning B, Mickos H, Heinegård D. 1991. Synthesis, NMR and function of an 0-phosphorylated peptide, comprising the RGD-adhesion sequence of osteopontin. Acta Chem. Scand. 45:604-8
    • (1991) Acta Chem. Scand. , vol.45 , pp. 604-608
    • Pettersson, E.1    Lüning, B.2    Mickos, H.3    Heinegård, D.4
  • 66
    • 0021271957 scopus 로고
    • The cell attachment activity of fibronectin can be duplicated by small fragments of the molecule
    • Pierschbacher MD, Ruoslahti E. 1984a. The cell attachment activity of fibronectin can be duplicated by small fragments of the molecule. Nature 309:30-33
    • (1984) Nature , vol.309 , pp. 30-33
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 67
    • 0001511468 scopus 로고
    • Variants of the cell recognition site of fibronectin that retain attachment-promoting activity
    • Pierschbacher MD, Ruoslahti E. 1984b. Variants of the cell recognition site of fibronectin that retain attachment-promoting activity. Proc. Natl. Acad. Sci. USA 81:5985-88
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 5985-5988
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 68
    • 0023609864 scopus 로고
    • Influence of stereochemistry of the sequence Arg-Gly-Asp-Xxx on binding specificity in cell adhesion
    • Pierschbacher MD, Ruoslahti E. 1987. Influence of stereochemistry of the sequence Arg-Gly-Asp-Xxx on binding specificity in cell adhesion. J. Biol. Chem. 262:17294-98
    • (1987) J. Biol. Chem. , vol.262 , pp. 17294-17298
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 70
    • 0027364324 scopus 로고
    • Multiple integrins mediate cell attachment to cytotactin/tenascin
    • Prieto AL, Edelman GM, Crossin KL. 1994. Multiple integrins mediate cell attachment to cytotactin/tenascin. Proc. Natl. Acad. Sci. USA 90:10154-58
    • (1994) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10154-10158
    • Prieto, A.L.1    Edelman, G.M.2    Crossin, K.L.3
  • 71
    • 0022000778 scopus 로고
    • Identification and isolation of a 140 kilodalton cell surface glycoprotein with properties of a fibronectin receptor
    • Pytela R, Pierschbacher MD, Ruoslahti E. 1985a. Identification and isolation of a 140 kilodalton cell surface glycoprotein with properties of a fibronectin receptor. Cell 40:191-98
    • (1985) Cell , vol.40 , pp. 191-198
    • Pytela, R.1    Pierschbacher, M.D.2    Ruoslahti, E.3
  • 72
    • 0001023374 scopus 로고
    • A 125/115 kd cell surface receptor specific for vitronectin interacts with the Arg-Gly-Asp adhesion sequence derived from fibronectin
    • Pytela R, Pierschbacher MD, Ruoslahti E. 1985b. A 125/115 kd cell surface receptor specific for vitronectin interacts with the Arg-Gly-Asp adhesion sequence derived from fibronectin. Proc. Natl. Acad. Sci. USA 82:5766-70
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 5766-5770
    • Pytela, R.1    Pierschbacher, M.D.2    Ruoslahti, E.3
  • 73
    • 0028962092 scopus 로고
    • Polymerase chain reaction cloning with degenerate primers: Homology-based identification of adhesion molecules
    • Pytela R, Suzuki S, Breuss J, Erie DJ, Sheppard D. 1994. Polymerase chain reaction cloning with degenerate primers: homology-based identification of adhesion molecules. Methods Enzymol. 245:420-51
    • (1994) Methods Enzymol. , vol.245 , pp. 420-451
    • Pytela, R.1    Suzuki, S.2    Breuss, J.3    Erie, D.J.4    Sheppard, D.5
  • 77
    • 0023637601 scopus 로고
    • New perspectives in cell adhesion: RGD and integrins
    • Ruoslahti E, Pierschbacher MD. 1987. New perspectives in cell adhesion: RGD and integrins. Science 238:491-97
    • (1987) Science , vol.238 , pp. 491-497
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 79
    • 0024352415 scopus 로고
    • Inhibition of the metastasis of murine malignant melanoma by synthetic polymeric peptides containing core sequences of cell-adhesive molecules
    • Saiki I, Iida J, Murata J, Ogawa R, Nishi N, et al. 1989. Inhibition of the metastasis of murine malignant melanoma by synthetic polymeric peptides containing core sequences of cell-adhesive molecules. Cancer Res. 49:3815-22
    • (1989) Cancer Res. , vol.49 , pp. 3815-3822
    • Saiki, I.1    Iida, J.2    Murata, J.3    Ogawa, R.4    Nishi, N.5
  • 80
    • 0025989573 scopus 로고
    • Development of a small RGD peptide fibrinogen receptor antagonist with potent anti-aggregatory activity in vitro
    • Samanen J, Ali F, Romoff T, Calvo R, Sorenson E, et al. 1991. Development of a small RGD peptide fibrinogen receptor antagonist with potent anti-aggregatory activity in vitro. J. Med. Chem. 34:3114-25
    • (1991) J. Med. Chem. , vol.34 , pp. 3114-3125
    • Samanen, J.1    Ali, F.2    Romoff, T.3    Calvo, R.4    Sorenson, E.5
  • 81
    • 0023652380 scopus 로고
    • Competition for related but nonidentical binding sites on the glycoprotein IIb-IIIa complex by peptides derived from platelet adhesive proteins
    • Santoro SA, Lawing WJ Jr. 1987. Competition for related but nonidentical binding sites on the glycoprotein IIb-IIIa complex by peptides derived from platelet adhesive proteins. Cell 48:867-73
    • (1987) Cell , vol.48 , pp. 867-873
    • Santoro, S.A.1    Lawing Jr., W.J.2
  • 82
    • 0028799897 scopus 로고
    • Coagulation factor XI cleaves the RHDS sequence and abolishes the cell adhesive properties of the amyloid b-protein
    • Saporito-Irwin SM, Van Nostrand WE. 1995. Coagulation factor XI cleaves the RHDS sequence and abolishes the cell adhesive properties of the amyloid b-protein. J. Biol. Chem. 270:26265-69
    • (1995) J. Biol. Chem. , vol.270 , pp. 26265-26269
    • Saporito-Irwin, S.M.1    Van Nostrand, W.E.2
  • 83
    • 0027393671 scopus 로고
    • Design of potent and specific integrin antagonists with high specificity for glycoprotein IIb-IIIa
    • Scarborough RM, Naughton MA, Teng W, Rose JW, Phillips DR, et al. 1993. Design of potent and specific integrin antagonists with high specificity for glycoprotein IIb-IIIa. J. Biol. Chem. 268:1066-73
    • (1993) J. Biol. Chem. , vol.268 , pp. 1066-1073
    • Scarborough, R.M.1    Naughton, M.A.2    Teng, W.3    Rose, J.W.4    Phillips, D.R.5
  • 84
    • 0024669648 scopus 로고
    • RGD-dependent linkage between plant cell wall and plasma membrane: Consequences for growth
    • Schindler M, Meiners S, Cheresh DA. 1989. RGD-dependent linkage between plant cell wall and plasma membrane: consequences for growth. J. Cell Biol. 108:1955-65
    • (1989) J. Cell Biol. , vol.108 , pp. 1955-1965
    • Schindler, M.1    Meiners, S.2    Cheresh, D.A.3
  • 86
    • 0027165368 scopus 로고
    • The nuclear magnetic resonance solution structure of Flavoridin, an antagonist of the platelet GPIIb-IIIa receptor
    • Senn H, Klaus W. 1993. The nuclear magnetic resonance solution structure of Flavoridin, an antagonist of the platelet GPIIb-IIIa receptor. J. Mol. Biol. 232:907-25
    • (1993) J. Mol. Biol. , vol.232 , pp. 907-925
    • Senn, H.1    Klaus, W.2
  • 87
    • 0024230916 scopus 로고
    • The arg-gly-asp binding domain of the vitronectin receptor: Photoaffinity crosslinking implicates amino acid residues 61-203 of the β subunit
    • Smith JW, Cheresh DA. 1988. The arg-gly-asp binding domain of the vitronectin receptor: photoaffinity crosslinking implicates amino acid residues 61-203 of the β subunit. J. Biol. Chem. 263:18726-31
    • (1988) J. Biol. Chem. , vol.263 , pp. 18726-18731
    • Smith, J.W.1    Cheresh, D.A.2
  • 90
    • 0022133419 scopus 로고
    • Complete amino acid sequence of human vitronectin deduced from cDNA. Similarity of cell attachment sites in vitronectin and fibronectin
    • Suzuki S, Oldberg A, Hayman EG, Pierschbacher MD, Ruoslahti E. 1985. Complete amino acid sequence of human vitronectin deduced from cDNA. Similarity of cell attachment sites in vitronectin and fibronectin. EMBO J. 4:2519-24
    • (1985) EMBO J. , vol.4 , pp. 2519-2524
    • Suzuki, S.1    Oldberg, A.2    Hayman, E.G.3    Pierschbacher, M.D.4    Ruoslahti, E.5
  • 95
    • 0028208244 scopus 로고
    • Residues within a conserved amino acid motif of domains 1 and 4 of VCAM-1 are required for binding to VLA-4
    • Vonderheide RH, Tedder TF, Springer TA, Staunton DE. 1994. Residues within a conserved amino acid motif of domains 1 and 4 of VCAM-1 are required for binding to VLA-4. J. Cell Biol. 125:215-22
    • (1994) J. Cell Biol. , vol.125 , pp. 215-222
    • Vonderheide, R.H.1    Tedder, T.F.2    Springer, T.A.3    Staunton, D.E.4
  • 96
    • 0026519307 scopus 로고
    • The contribution of the extracellular matrix gravisensing in characean cells
    • Wayne R, Staves MP, Leopold AC. 1992. The contribution of the extracellular matrix gravisensing in characean cells. J. Cell Sci. 101:611-23
    • (1992) J. Cell Sci. , vol.101 , pp. 611-623
    • Wayne, R.1    Staves, M.P.2    Leopold, A.C.3
  • 97
    • 0027480082 scopus 로고
    • Identification of a novel cell attachment domain in the HIV-1 Tat protein and its 90-kDa cell surface binding protein
    • Weeks BS, Desal K, Lowenstein PM, Klotman ME, Klotman PE, et al. 1993. Identification of a novel cell attachment domain in the HIV-1 Tat protein and its 90-kDa cell surface binding protein. J. Biol. Chem. 268:5279-84
    • (1993) J. Biol. Chem. , vol.268 , pp. 5279-5284
    • Weeks, B.S.1    Desal, K.2    Lowenstein, P.M.3    Klotman, M.E.4    Klotman, P.E.5
  • 98
    • 0029586317 scopus 로고
    • Targeting of adenovirus penton base to new receptors through replacement of its RGD motif with other receptor-specific peptide motifs
    • Wickham TJ, Carrion ME, Kovesdt I. 1995. Targeting of adenovirus penton base to new receptors through replacement of its RGD motif with other receptor-specific peptide motifs. Gene Ther. 2:750-56
    • (1995) Gene Ther. , vol.2 , pp. 750-756
    • Wickham, T.J.1    Carrion, M.E.2    Kovesdt, I.3
  • 99
    • 0029045064 scopus 로고
    • A widely distribued and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain
    • Wolfsberg TG, Straight PD, Gerena RL, Huovila A-PJ, Primakoff P, et al. 1995. A widely distribued and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain. Dev. Biol. 169:378-83
    • (1995) Dev. Biol. , vol.169 , pp. 378-383
    • Wolfsberg, T.G.1    Straight, P.D.2    Gerena, R.L.3    Huovila, A.-P.J.4    Primakoff, P.5
  • 100
    • 0021267179 scopus 로고
    • Dualistic nature of adhesive protein function: Fibronectin and its biologically active peptide fragments can autoinhibit fibronectin function
    • Yamada KM, Kennedy DW. 1984. Dualistic nature of adhesive protein function: Fibronectin and its biologically active peptide fragments can autoinhibit fibronectin function. J. Cell Biol. 99:29-36
    • (1984) J. Cell Biol. , vol.99 , pp. 29-36
    • Yamada, K.M.1    Kennedy, D.W.2
  • 101
    • 0023141833 scopus 로고
    • Peptide inhibitors of fibronectin, laminin, and other adhesion molecules: Unique and shared features
    • Yamada KM, Kennedy DW. 1987. Peptide inhibitors of fibronectin, laminin, and other adhesion molecules: unique and shared features. J. Cell Physiol. 130:21-28
    • (1987) J. Cell Physiol. , vol.130 , pp. 21-28
    • Yamada, K.M.1    Kennedy, D.W.2


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