The fibrinogen RIBS-I epitope (γ373–385) appears proximate to the γ408–411 adhesive domain but is not involved in interaction between receptor-bound or surface-adsorbed fibrinogen and platelet GPIIbIIIa
- 8 December 1998
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1429 (1) , 217-229
- https://doi.org/10.1016/s0167-4838(98)00235-0
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- The AGDV residues on the gamma chain carboxyl terminus of platelet-bound fibrinogen are needed for platelet aggregationBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1997
- Dissecting Clot Retraction and Platelet AggregationPublished by Elsevier ,1996
- Characterization of adhesion of “resting” and stimulated platelets to fibrinogen and its fragmentsThrombosis Research, 1993
- Role of fibrinogen alpha and gamma chain sites in platelet aggregation.Proceedings of the National Academy of Sciences, 1992
- Platelet receptor recognition domain on the .gamma. chain of human fibrinogen and its synthetic peptide analoguesBiochemistry, 1989
- Platelet receptor recognition domains on the .alpha. chain of human fibrinogen: structure-function analysisBiochemistry, 1989
- Fibrinogen-independent platelet adhesion and thrombus formation on subendothelium mediated by glycoprotein IIb-IIIa complex at high shear rate.Journal of Clinical Investigation, 1989
- Platelet receptor recognition site on human fibrinogen. Synthesis and structure-function relationship of peptides corresponding to the carboxy-terminal segment of the .gamma. chainBiochemistry, 1984
- Recognition site for the platelet receptor is present on the 15-residue carboxy-terminal fragment of the γ chain of human fibrinogen and is not involved in the fibrin polymerization reactionThrombosis Research, 1983
- gamma and alpha chains of human fibrinogen possess sites reactive with human platelet receptors.Proceedings of the National Academy of Sciences, 1982