메뉴 건너뛰기




Volumn 50, Issue 3, 1996, Pages 529-537

Studies on α(v)β3/ligand interactions using a [3H]SK and F-107260 binding assay

Author keywords

[No Author keywords available]

Indexed keywords

PENTAPEPTIDE; SKF 107260; UNCLASSIFIED DRUG; VITRONECTIN RECEPTOR BLOCKING AGENT;

EID: 9544258252     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (27)

References (41)
  • 1
    • 0023612102 scopus 로고
    • Biosynthetic, and functional properties of an Arg-Gly-Asp-directed receptor involved in human melanoma attachment to vitronectin, fibrinogen and von-Willebrand factor
    • Cheresh, D. A., and R. C. Spiro. Biosynthetic, and functional properties of an Arg-Gly-Asp-directed receptor involved in human melanoma attachment to vitronectin, fibrinogen and von-Willebrand factor. J. Biol. Chem. 262:17703-17711 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 17703-17711
    • Cheresh, D.A.1    Spiro, R.C.2
  • 2
    • 0025035781 scopus 로고
    • Current status review: Vitronectin receptor, tissue specific expression or adaptation to culture?
    • Horton, M. Current status review: vitronectin receptor, tissue specific expression or adaptation to culture? Int. J. Exp. Pathol. 71:741-759 (1990).
    • (1990) Int. J. Exp. Pathol. , vol.71 , pp. 741-759
    • Horton, M.1
  • 3
    • 0024454316 scopus 로고
    • The osteoclast functional antigen, implicated in the regulation of bone resorption, is biochemically related to the vitronectin receptor
    • Davies, J., J. Warwick, N. Totty, R. Philp, M. Helfrich, and M. Horton. The osteoclast functional antigen, implicated in the regulation of bone resorption, is biochemically related to the vitronectin receptor. J. Cell Biol. 109:1817-1826 (1989).
    • (1989) J. Cell Biol. , vol.109 , pp. 1817-1826
    • Davies, J.1    Warwick, J.2    Totty, N.3    Philp, R.4    Helfrich, M.5    Horton, M.6
  • 6
  • 8
    • 0025787570 scopus 로고
    • Arg-Gly-Asp peptides and the anti-vitronectin receptor antibody 23C6 inhibit dentine resorption and cell spreading by osteoclast
    • Horton, M. A., M. L. Taylor, T. R. Arnett, and M. H. Helfrich. Arg-Gly-Asp peptides and the anti-vitronectin receptor antibody 23C6 inhibit dentine resorption and cell spreading by osteoclast. Exp. Cell Res. 195:368-375 (1991).
    • (1991) Exp. Cell Res. , vol.195 , pp. 368-375
    • Horton, M.A.1    Taylor, M.L.2    Arnett, T.R.3    Helfrich, M.H.4
  • 9
    • 0022502048 scopus 로고
    • Platelet membrane glycoprotein IIb/IIIa: Member of a family of Arg-Gly-Asp-specific adhesion receptors
    • Pytela, R., M. D. Pierschbacher, M. H. Ginsberg, E. F. Plow, and E. Ruoslahti. Platelet membrane glycoprotein IIb/IIIa: member of a family of Arg-Gly-Asp-specific adhesion receptors. Science (Washington D. C.) 231: 1559-1562 (1986).
    • (1986) Science (Washington D. C.) , vol.231 , pp. 1559-1562
    • Pytela, R.1    Pierschbacher, M.D.2    Ginsberg, M.H.3    Plow, E.F.4    Ruoslahti, E.5
  • 10
    • 0024848055 scopus 로고
    • Abolition of in vivo platelet thrombus formation in primates with monoclonal antibodies to the platelet GPIIb/IIIa receptor: Correlation with bleeding time, platelet aggregation, and blockage of GPIIb/IIIa
    • Coller, B. S., J. D. Folts, S. R. Smith, L. E. Scudder, and R. Jordan, Abolition of in vivo platelet thrombus formation in primates with monoclonal antibodies to the platelet GPIIb/IIIa receptor: correlation with bleeding time, platelet aggregation, and blockage of GPIIb/IIIa. Circulation 80:1766-1774 (1989).
    • (1989) Circulation , vol.80 , pp. 1766-1774
    • Coller, B.S.1    Folts, J.D.2    Smith, S.R.3    Scudder, L.E.4    Jordan, R.5
  • 11
    • 0023234083 scopus 로고
    • Arg-Gly-Asp recognition by a cell adhesion receptor requires its 130 kDa α subunit
    • Cheresh, D. A., and J. R. Harper. Arg-Gly-Asp recognition by a cell adhesion receptor requires its 130 kDa α subunit. J. Biol. Chem. 262:1434-1437 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 1434-1437
    • Cheresh, D.A.1    Harper, J.R.2
  • 12
    • 0022338260 scopus 로고
    • Monoclonal antibodies to osteoclastomas (giant cell bone tumours): Definition of osteoclast-specific antigens
    • Horton, M. A., D. Lewis, K. McNulty, J. A. S. Pringle, and T. J. Chambers. Monoclonal antibodies to osteoclastomas (giant cell bone tumours): definition of osteoclast-specific antigens. Cancer Res. 45:5663-5669 (1985).
    • (1985) Cancer Res. , vol.45 , pp. 5663-5669
    • Horton, M.A.1    Lewis, D.2    McNulty, K.3    Pringle, J.A.S.4    Chambers, T.J.5
  • 18
    • 0023189463 scopus 로고
    • Protein sequence of endothelial glycoprotein IIIa derived from a cDNA clone
    • Fitzgerald, L. A., B. Steiner, S. C. Rall, Jr., S. S. Lo, and D. R. Phillips. Protein sequence of endothelial glycoprotein IIIa derived from a cDNA clone. J. Biol. Chem. 262:3936-3939 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 3936-3939
    • Fitzgerald, L.A.1    Steiner, B.2    Rall Jr., S.C.3    Lo, S.S.4    Phillips, D.R.5
  • 19
    • 0023749491 scopus 로고
    • Cloning of glycoprotein IIIa cDNA from human erythroleukemia cells and localization of the gene to chromosome 17
    • Rosa, J.-P., P. F. Bray, O. Gayet, G. I. Johnston, R. G. Cook, K. W. Jackson, M. A. Shuman, and R. P. McEver. Cloning of glycoprotein IIIa cDNA from human erythroleukemia cells and localization of the gene to chromosome 17. Blood 72:593-600 (1988).
    • (1988) Blood , vol.72 , pp. 593-600
    • Rosa, J.-P.1    Bray, P.F.2    Gayet, O.3    Johnston, G.I.4    Cook, R.G.5    Jackson, K.W.6    Shuman, M.A.7    McEver, R.P.8
  • 20
    • 0023607232 scopus 로고
    • Comparison of cDNA-derived protein sequences of the human fibronectin and vitronectin receptor α-subunits and platelet glycoprotein IIb
    • Fitzgerald, L. A., M. Poncz, B. Steiner, S. C. Rall, J. S. Bennett, and D. R. Phillips. Comparison of cDNA-derived protein sequences of the human fibronectin and vitronectin receptor α-subunits and platelet glycoprotein IIb. Biochemistry 26:8158-8165 (1987).
    • (1987) Biochemistry , vol.26 , pp. 8158-8165
    • Fitzgerald, L.A.1    Poncz, M.2    Steiner, B.3    Rall, S.C.4    Bennett, J.S.5    Phillips, D.R.6
  • 21
    • 0023625872 scopus 로고
    • Amino acid sequence of the vitronectin receptor α subunit and comparative expression of adhesion receptor mRNAs
    • Suzuki, S., W. S. Argraves, H. Arai, L. R. Languino, M. D. Pierschbacher, and E. Ruoslahti. Amino acid sequence of the vitronectin receptor α subunit and comparative expression of adhesion receptor mRNAs. J. Biol. Chem. 262:14080-14085 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 14080-14085
    • Suzuki, S.1    Argraves, W.S.2    Arai, H.3    Languino, L.R.4    Pierschbacher, M.D.5    Ruoslahti, E.6
  • 22
    • 2042439878 scopus 로고
    • cDNA, and amino acid sequences of the cell adhesion protein receptor recognizing vitronectin reveal a transmembrane domain and homologies with other adhesion protein receptors
    • Suzuki, S., W. S. Argraves, R. Pytela, H. Arai, T. Kruisius, M. D, Pierschbacher, and E. Ruoslahti. cDNA, and amino acid sequences of the cell adhesion protein receptor recognizing vitronectin reveal a transmembrane domain and homologies with other adhesion protein receptors. Proc. Natl. Acad. Sci. USA 83:8614-8618 (1987).
    • (1987) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8614-8618
    • Suzuki, S.1    Argraves, W.S.2    Pytela, R.3    Arai, H.4    Kruisius, T.5    Pierschbacher, M.D.6    Ruoslahti, E.7
  • 23
    • 0025075383 scopus 로고
    • Chick integrin α subunit molecular analysis reveals high conservation of structural domains and association with multiple β subunits in embryo fibroblasts
    • Bossy, B., and L. F. Reichardt. Chick integrin α subunit molecular analysis reveals high conservation of structural domains and association with multiple β subunits in embryo fibroblasts. Biochemistry 29:10191-10198 (1990).
    • (1990) Biochemistry , vol.29 , pp. 10191-10198
    • Bossy, B.1    Reichardt, L.F.2
  • 24
    • 0019061918 scopus 로고
    • LIGAND: A versatile computerized approach for characterization of ligand-binding systems
    • Munson, P. J., and D. Rodbard. LIGAND: a versatile computerized approach for characterization of ligand-binding systems. Anal. Biochem. 107:220-239 (1980).
    • (1980) Anal. Biochem. , vol.107 , pp. 220-239
    • Munson, P.J.1    Rodbard, D.2
  • 35
    • 0024324937 scopus 로고
    • Immunohistochemical distribution of extracellular receptors in human osteoclasts: α integrin colocalized with vinculin and talin in the podosomes of osteoclastoma giant cells
    • Zambonin-Zallone, A., A. Teti, M. Grano, A. Rubianacci, M. Abbadini, M. Gaboli, and P. C. Marchisio. Immunohistochemical distribution of extracellular receptors in human osteoclasts: α integrin colocalized with vinculin and talin in the podosomes of osteoclastoma giant cells. Exp. Cell Res. 182:645-652 (1989).
    • (1989) Exp. Cell Res. , vol.182 , pp. 645-652
    • Zambonin-Zallone, A.1    Teti, A.2    Grano, M.3    Rubianacci, A.4    Abbadini, M.5    Gaboli, M.6    Marchisio, P.C.7
  • 37
    • 0022558418 scopus 로고
    • Disialoganglioside GD2 distributes preferentially into substrate-associated microprocesses on human melanoma cells during their attachment to fibronectin
    • Cheresh, D. A., and F. G. Klier. Disialoganglioside GD2 distributes preferentially into substrate-associated microprocesses on human melanoma cells during their attachment to fibronectin. J. Cell Biol. 102:1887-1897 (1986).
    • (1986) J. Cell Biol. , vol.102 , pp. 1887-1897
    • Cheresh, D.A.1    Klier, F.G.2
  • 38
    • 0023819301 scopus 로고
    • Synergism between membrane gangliosides and Arg-Gly-Asp-directed glycoprotein receptors in attachment to matrix proteins by melanoma cells
    • Burns, G. F., C. M. Lucas, G. W. Krissansen, J. A. Werkmeister, D. B. Scanlon, R. J. Simpson, and M. A. Vadas. Synergism between membrane gangliosides and Arg-Gly-Asp-directed glycoprotein receptors in attachment to matrix proteins by melanoma cells. J. Cell Biol. 107:1225-1230 (1988).
    • (1988) J. Cell Biol. , vol.107 , pp. 1225-1230
    • Burns, G.F.1    Lucas, C.M.2    Krissansen, G.W.3    Werkmeister, J.A.4    Scanlon, D.B.5    Simpson, R.J.6    Vadas, M.A.7
  • 41
    • 0026639262 scopus 로고
    • Ligand binding specificity of the leukocyte response integrin expressed by human neutrophils
    • Gresham, H. D., S. P. Adams, and E. J. Brown. Ligand binding specificity of the leukocyte response integrin expressed by human neutrophils. J. Biol. Chem. 267:13895-13902 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 13895-13902
    • Gresham, H.D.1    Adams, S.P.2    Brown, E.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.