These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
9. An echistatin-like Arg-Gly-Asp (RGD)-containing sequence in the heavy chain CDR3 of a murine monoclonal antibody that inhibits human platelet glycoprotein IIb/IIIa function. Deckmyn H, Stanssens P, Hoet B, Declerck PJ, Lauwereys M, Gansemans Y, Tornai I, Vermylen J. Br J Haematol; 1994 Jul 05; 87(3):562-71. PubMed ID: 7993797 [Abstract] [Full Text] [Related]
10. Synthetic peptides demonstrate RGD-independent platelet glycoprotein IIb/IIIa recognition site in cell binding domain of human fibronectin. Mohri H, Tanabe J, Katoh K, Okubo T. Peptides; 1995 Jul 05; 16(2):263-8. PubMed ID: 7784256 [Abstract] [Full Text] [Related]
11. Distribution of ligand-occupied alpha IIb beta 3 in resting and activated human platelets determined by expression of a novel class of ligand-induced binding site recognized by monoclonal antibody AP6. Nurden P, Humbert M, Piotrowicz RS, Bihour C, Poujol C, Nurden AT, Kunicki TJ. Blood; 1996 Aug 01; 88(3):887-99. PubMed ID: 8704246 [Abstract] [Full Text] [Related]
12. Regulation of ligand binding to glycoprotein IIb-IIIa (integrin alpha IIb beta 3) in isolated platelet membranes. Smyth SS, Parise LV. Biochem J; 1993 Jun 15; 292 ( Pt 3)(Pt 3):749-58. PubMed ID: 7686366 [Abstract] [Full Text] [Related]
13. Tetrafibricin, a novel non-peptide fibrinogen receptor antagonist, induces conformational changes in glycoprotein IIb/IIIa. Satoh T, Kouns WC, Yamashita Y, Kamiyama T, Steiner B. Biochem J; 1994 Aug 01; 301 ( Pt 3)(Pt 3):785-91. PubMed ID: 7519850 [Abstract] [Full Text] [Related]
14. Role of platelet GpIIb/IIIa receptors in the modulation of platelet plasminogen activator inhibitors type-1 (PAI-1) release. Mousa SA, Bozarth J, Forsythe M, Tsao P, Pease L, Reilly TM. Life Sci; 1994 Aug 01; 54(16):1155-62. PubMed ID: 8152339 [Abstract] [Full Text] [Related]
16. The integrin alpha IIb beta 3 contains distinct and interacting binding sites for snake-venom RGD (Arg-Gly-Asp) proteins. Evidence that the receptor-binding characteristics of snake-venom RGD proteins are related to the amino acid environment flanking the sequence RGD. Rahman S, Lu X, Kakkar VV, Authi KS. Biochem J; 1995 Nov 15; 312 ( Pt 1)(Pt 1):223-32. PubMed ID: 7492316 [Abstract] [Full Text] [Related]