Site-directed mutagenesis of the cell-binding domain of human fibronectin: Separable, synergistic sites mediate adhesive function
- 1 May 1988
- Vol. 53 (4) , 649-657
- https://doi.org/10.1016/0092-8674(88)90580-6
Abstract
No abstract availableThis publication has 57 references indexed in Scilit:
- Fibroblast adhesion to RGDS shows novel features compared with fibronectin.The Journal of cell biology, 1987
- Expression of the cell‐binding domain of human fibronectin in E. coliFEBS Letters, 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
- Integrins: A family of cell surface receptorsCell, 1987
- Peptide inhibitors of fibronectin, laminin, and other adhesion molecules: Unique and shared featuresJournal of Cellular Physiology, 1987
- Identification of an alternatively spliced site in human plasma fibronectin that mediates cell type-specific adhesion.The Journal of cell biology, 1986
- Substratum contacts and cytoskeletal reorganization of BALB/c 3T3 cells on a cell-binding fragment and heparin-binding fragments of plasma fibronectinExperimental Cell Research, 1986
- Arg-Gly-Asp: A versatile cell recognition signalCell, 1986
- Collagen can modulate cell interactions with fibronectin.The Journal of cell biology, 1985
- Interaction of the 70,000-mol-wt amino-terminal fragment of fibronectin with the matrix-assembly receptor of fibroblasts.The Journal of cell biology, 1985