Characteristics of Fibrinogen Binding to the Domain of CD11c, an α Subunit of p150,95
- 1 November 1999
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 264 (3) , 630-634
- https://doi.org/10.1006/bbrc.1999.1564
Abstract
No abstract availableKeywords
Funding Information
- Ministry of Education, Kenya
This publication has 29 references indexed in Scilit:
- Leukocyte integrinsPublished by Elsevier ,2002
- Identification of a Novel Recognition Sequence for Integrin αMβ2 within the γ-chain of FibrinogenJournal of Biological Chemistry, 1998
- Crystal structure of the A domain from the a subunit of integrin CR3 (CD11 b/CD18)Cell, 1995
- A novel divalent cation-binding site in the a domain of the ?2 integrin CR3 (CD11b/CD18) is essential for ligand bindingCell, 1993
- The I domain is a major recognition site on the leukocyte integrin Mac-1 (CD11b/CD18) for four distinct adhesion ligands.The Journal of cell biology, 1993
- Interaction of leukocyte integrins with ligand is necessary but not sufficient for function.The Journal of cell biology, 1992
- CD11c/CD18 on neutrophils recognizes a domain at the N terminus of the A alpha chain of fibrinogen.Proceedings of the National Academy of Sciences, 1991
- Adhesion receptors of the immune systemNature, 1990
- A facile separation of fragments D and E from the fibrinogen/fibrin degradation products of three mammalian speciesBiochemical and Biophysical Research Communications, 1974
- Plasminogen: Purification from Human Plasma by Affinity ChromatographyScience, 1970