Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
- 1 May 1984
- journal article
- Published by Springer Science and Business Media LLC in Nature
- Vol. 309 (5963), 30-33
- https://doi.org/10.1038/309030a0
Abstract
The ability of fibronectin to bind cells can be accounted for by the tetrapeptide L-arginyl-glycyl-L-aspartyl-L-serine, a sequence which is part of the cell attachment domain of fibronectin and present in at least five other proteins. This tetrapeptide may constitute a cellular recognition determinant common to several proteins.Keywords
This publication has 25 references indexed in Scilit:
- Fibronectin-mediated binding and phagocytosis of polystyrene latex beads by baby hamster kidney cells.The Journal of cell biology, 1983
- Synthetic peptide with cell attachment activity of fibronectin.Proceedings of the National Academy of Sciences of the United States of America, 1983
- Binding of plasma fibronectin to the surfaces of BHK cells in suspension at 4 °CExperimental Cell Research, 1982
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982
- Gene sequence of the λ receptor, an outer membrane protein of E. coli K12Cell, 1981
- Location of the cell-attachment site in fibronectin with monoclonal antibodies and proteolytic fragments of the moleculeCell, 1981
- Nucleotide sequence of the 26S mRNA of Sindbis virus and deduced sequence of the encoded virus structural proteins.Proceedings of the National Academy of Sciences of the United States of America, 1981
- Amino acid sequence studies on the .alpha. chain of human fibrinogen. Overlapping sequences providing the complete sequenceBiochemistry, 1979
- Molecular requirements for the adhesion and spreading of hamster fibroblastsExperimental Cell Research, 1979
- L. F. BatesNature, 1978