Identification of Amino Acid Sequences in Fibrinogen γ-Chain and Tenascin C C-terminal Domains Critical for Binding to Integrin αvβ3
Open Access
- 1 June 2000
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 275 (22) , 16891-16898
- https://doi.org/10.1074/jbc.m000610200
Abstract
No abstract availableKeywords
This publication has 45 references indexed in Scilit:
- Identification of a Novel Recognition Sequence for Integrin αMβ2 within the γ-chain of FibrinogenJournal of Biological Chemistry, 1998
- The Role of Putative Fibrinogen Aα-, Bβ-, and γA-chain Integrin Binding Sites in Endothelial Cell-mediated Clot RetractionPublished by Elsevier ,1997
- Changing Ligand Specificities of αvβ1 and αvβ3 Integrins by Swapping a Short Diverse Sequence of the β SubunitJournal of Biological Chemistry, 1997
- Crystal structure of a 30 kDa C-terminal fragment from the γ chain of human fibrinogenStructure, 1997
- A peptide isolated from phage display libraries is a structural and functional mimic of an RGD-binding site on integrins.The Journal of cell biology, 1995
- Involvement of α6β3 Integrin in Mediating Fibrin Gel RetractionJournal of Biological Chemistry, 1995
- Requirement of Vascular Integrin α v β 3 for AngiogenesisScience, 1994
- Carboxy-terminal-extended variant of the human fibrinogen .alpha. subunit: a novel exon conferring marked homology to .beta. and .gamma. subunitsBiochemistry, 1992
- Tumors: Wounds That Do Not HealNew England Journal of Medicine, 1986
- Trinodular structure of fibrinogenJournal of Molecular Biology, 1979