The Arg-Gly-Asp binding domain of the vitronectin receptor. Photoaffinity cross-linking implicates amino acid residues 61-203 of the beta subunit.
Open Access
- 1 December 1988
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 263 (35) , 18726-18731
- https://doi.org/10.1016/s0021-9258(18)37343-5
Abstract
No abstract availableThis publication has 31 references indexed in Scilit:
- Investigation of the biological effects of anti-cell adhesive synthetic peptides that inhibit experimental metastasis of B16-F10 murine melanoma cells.Journal of Clinical Investigation, 1988
- New Perspectives in Cell Adhesion: RGD and IntegrinsScience, 1987
- Amino acid sequence of the human fibronectin receptor.The Journal of cell biology, 1987
- An Arg-Gly-Asp-directed receptor on the surface of human melanoma cells exists in an divalent cation-dependent functional complex with the disialoganglioside GD2.The Journal of cell biology, 1987
- Competition for related but nonidentical binding sites on the glycoprotein IIb-IIIa complex by peptides derived from platelet adhesive proteinsCell, 1987
- Cloning of the $beta; subunit of the leukocyte adhesion proteins: Homology to an extracellular matrix receptor defines a novel supergene familyCell, 1987
- Integrins: A family of cell surface receptorsCell, 1987
- Structure of integrin, a glycoprotein involved in the transmembrane linkage between fibronectin and actinCell, 1986
- Platelet Membrane Glycoprotein IIb/IIIa: Member of a Family of Arg-Gly-Asp—Specific Adhesion ReceptorsScience, 1986
- Interaction of fibronectin with its receptor on plateletsCell, 1985