Identification of a Novel Recognition Sequence for Integrin αMβ2 within the γ-chain of Fibrinogen
Open Access
- 1 August 1998
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 273 (35) , 22519-22527
- https://doi.org/10.1074/jbc.273.35.22519
Abstract
No abstract availableKeywords
This publication has 40 references indexed in Scilit:
- Identification and Reconstruction of the Binding Site within αMβ2 for a Specific and High Affinity Ligand, NIFPublished by Elsevier ,1997
- Domain Structure and Functional Activity of the Recombinant Human Fibrinogen γ-Module (γ148−411)Biochemistry, 1997
- Crystal structure of a 30 kDa C-terminal fragment from the γ chain of human fibrinogenStructure, 1997
- Overlapping, but Not Identical, Sites Are Involved in the Recognition of C3bi, Neutrophil Inhibitory Factor, and Adhesive Ligands by the αMβ2 IntegrinJournal of Biological Chemistry, 1996
- Molecular determinants of acute inflammatory responses to biomaterials.Journal of Clinical Investigation, 1996
- Coordinate role for cell surface chondroitin sulfate proteoglycan and alpha 4 beta 1 integrin in mediating melanoma cell adhesion to fibronectin.The Journal of cell biology, 1992
- High molecular weight kininogen inhibits fibrinogen binding to cytoadhesins of neutrophils and platelets.The Journal of cell biology, 1989
- A novel member of the integrin receptor family mediates Arg-Gly-Asp-stimulated neutrophil phagocytosis.The Journal of cell biology, 1989
- Identification and distribution of fibrinogen, fibrin, and fibrin(ogen) degradation products in atherosclerosis. Use of monoclonal antibodies.Arteriosclerosis: An Official Journal of the American Heart Association, Inc., 1989
- Oligospecificity of the cellular adhesion receptor Mac-1 encompasses an inducible recognition specificity for fibrinogen.The Journal of cell biology, 1988