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Journal Abstract Search
303 related items for PubMed ID: 8092274
1. Effects of ATP on ligand recognition of platelet fibrinogen receptor on GPIIb-IIIa. Gawaz MP, Mayinger P, Neumann FJ. Am J Physiol; 1994 Sep; 267(3 Pt 2):H1098-106. PubMed ID: 8092274 [Abstract] [Full Text] [Related]
3. Human platelet activation is inhibited by the occupancy of glycoprotein IIb/IIIa receptor. Padoin E, Alexandre A, Cavallini L, Polverino de Laureto P, Rao GH, Doni MG. Arch Biochem Biophys; 1996 Sep 15; 333(2):407-13. PubMed ID: 8809080 [Abstract] [Full Text] [Related]
4. [Conformational changes of the platelet membrane glycoprotein IIb-IIIa complex stimulated by a monoclonal antibody to the N-terminal segment of glycoprotein IIIa]. Khaspekova SG, Vyzova TV, Lukin VV, Tikhomirov OIu, Berndt M, Kouns W, Mazurov AV. Biokhimiia; 1996 Mar 15; 61(3):412-28. PubMed ID: 8724599 [Abstract] [Full Text] [Related]
8. Localization of the cross-linking sites of RGD and KQAGDV peptides to the isolated fibrinogen receptor, the human platelet integrin glycoprotein IIb/IIIa. Influence of peptide length. Calvete JJ, Schäfer W, Mann K, Henschen A, González-Rodríguez J. Eur J Biochem; 1992 Jun 15; 206(3):759-65. PubMed ID: 1376688 [Abstract] [Full Text] [Related]
9. Endogenous platelet fibrinogen surface expression on activated platelets. Gralnick HR, Williams S, McKeown L, Connaghan G, Shafer B, Hansmann K, Vail M, Fenton J. J Lab Clin Med; 1991 Dec 15; 118(6):604-13. PubMed ID: 1744509 [Abstract] [Full Text] [Related]
12. The Arg-Gly-Asp (RGD) recognition site of platelet glycoprotein IIb-IIIa on nonactivated platelets is accessible to high-affinity macromolecules. Tomiyama Y, Tsubakio T, Piotrowicz RS, Kurata Y, Loftus JC, Kunicki TJ. Blood; 1992 May 01; 79(9):2303-12. PubMed ID: 1373972 [Abstract] [Full Text] [Related]
18. Inhibition of fibrinogen binding and surface recruitment of GpIIb/IIIa as dose-dependent effects of the RGD-mimetic MK-852. Wittig K, Rothe G, Schmitz G. Thromb Haemost; 1998 Mar 15; 79(3):625-30. PubMed ID: 9531053 [Abstract] [Full Text] [Related]