Site-directed mutagenesis of the arginine-glycine-aspartic acid in vitronectin abolishes cell adhesion
Open Access
- 1 May 1993
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 268 (13) , 9725-9729
- https://doi.org/10.1016/s0021-9258(18)98408-5
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- Integrins: Versatility, modulation, and signaling in cell adhesionCell, 1992
- Diversities in animal vitronectins. Differences in molecular weight, immunoreactivity and carbohydrate chainsBiochimica et Biophysica Acta (BBA) - General Subjects, 1990
- Site-directed mutagenesis of the cell-binding domain of human fibronectin: Separable, synergistic sites mediate adhesive functionCell, 1988
- A simple and rapid method for the selection of oligodeoxynucleotide-directed mutantsGene, 1988
- New Perspectives in Cell Adhesion: RGD and IntegrinsScience, 1987
- Expression of the cell‐binding domain of human fibronectin in E. coliFEBS Letters, 1987
- Platelet Membrane Glycoprotein IIb/IIIa: Member of a Family of Arg-Gly-Asp—Specific Adhesion ReceptorsScience, 1986
- Arg-Gly-Asp: A versatile cell recognition signalCell, 1986
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- PREPARATION FROM HUMAN SERUM OF AN ALPHA-ONE PROTEIN WHICH INDUCES THE IMMEDIATE GROWTH OF UNADAPTED CELLS IN VITROThe Journal of cell biology, 1967