Convalent surface immobilization of Arg-Gly-Asp- and Tyr-Ile-Gly-Ser-Arg-containing peptides to obtain well-defined cell-adhesive substrates
- 1 June 1990
- journal article
- research article
- Published by Elsevier in Analytical Biochemistry
- Vol. 187 (2) , 292-301
- https://doi.org/10.1016/0003-2697(90)90459-m
Abstract
No abstract availableThis publication has 22 references indexed in Scilit:
- Covalent attachment of an Arg-Gly-Asp sequece peptide to derivatizable polyacrylamide surfaces: Support of fibroblast adhesion and long-term growthAnalytical Biochemistry, 1988
- Fibroblast adhesion to RGDS shows novel features compared with fibronectin.The Journal of cell biology, 1987
- Identification of an amino acid sequence in laminin mediating cell attachment, chemotaxis, and receptor bindingCell, 1987
- The fibronectin cell attachment sequence Arg-Gly-Asp-Ser promotes focal contact formation during early fibroblast attachment and spreading.The Journal of cell biology, 1987
- Focal adhesion sites and the removal of substratum-bound fibronectin.The Journal of cell biology, 1986
- Arg-Gly-Asp: A versatile cell recognition signalCell, 1986
- Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the moleculeNature, 1984
- Iodination of proteins, glycoproteins, and peptides using a solid-phase oxidizing agent, 1,3,4,6-tetrachloro-3α,6α-diphenyl glycoluril (Iodogen)Analytical Biochemistry, 1981
- Immobilization of enzymes and affinity ligands to various hydroxyl group carrying supports using highly reactive sulfonyl chloridesBiochemical and Biophysical Research Communications, 1981
- High performance liquid affinity chromatography (HPLAC) and its application to the separation of enzymes and antigensFEBS Letters, 1978