An Allosteric Ca2+ Binding Site on the β3-Integrins That Regulates the Dissociation Rate for RGD Ligands
Open Access
- 1 September 1996
- journal article
- Published by Elsevier
- Vol. 271 (36) , 21745-21751
- https://doi.org/10.1074/jbc.271.36.21745
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Ca2+Suppresses Cell Adhesion to Osteopontin by Attenuating Binding Affinity for Integrin αvβ3Published by Elsevier ,1995
- Integrin αvβ3 antagonists promote tumor regression by inducing apoptosis of angiogenic blood vesselsCell, 1994
- Ligand and cation binding are dual functions of a discrete segment of the integrin β3 subunit: Cation displacement is involved in ligand bindingCell, 1994
- Requirement of Vascular Integrin α v β 3 for AngiogenesisScience, 1994
- Integrins: Versatility, modulation, and signaling in cell adhesionCell, 1992
- Divalent cations mimic the inhibitory effect of extracellular ionised calcium on bone resorption by isolated rat osteoclasts: Further evidence for a “calcium receptor”Journal of Cellular Physiology, 1991
- Integrins.Journal of Clinical Investigation, 1991
- Osteoclast cytosolic calcium, regulated by voltage-gated calcium channels and extracellular calcium, controls podosome assembly and bone resorption.The Journal of cell biology, 1990
- A β 3 Integrin Mutation Abolishes Ligand Binding and Alters Divalent Cation-Dependent ConformationScience, 1990
- The membrane glycoprotein Ia-IIa (VLA-2) complex mediates the Mg++-dependent adhesion of platelets to collagen.The Journal of cell biology, 1989