Integrin alpha IIb beta 3 (platelet GPIIb-IIIa) recognizes multiple sites in fibronectin.

This publication has 47 references indexed in Scilit:

• Monoclonal antibody characterization of two distant sites required for function of the central cell-binding domain of fibronectin in cell adhesion, cell migration, and matrix assembly.
  The Journal of cell biology, 1991
• Receptor functions for the integrin VLA-3: fibronectin, collagen, and laminin binding are differentially influenced by Arg-Gly-Asp peptide and by divalent cations.
  The Journal of cell biology, 1991
• Ligand binding to integrins: Common and ligand specific recognition mechanisms
  Cell Differentiation and Development, 1990
• The vitronectin receptor alpha v beta 3 binds fibronectin and acts in concert with alpha 5 beta 1 in promoting cellular attachment and spreading on fibronectin.
  The Journal of cell biology, 1990
• VLA Proteins in the Integrin Family: Structures, Functions, and Their Role on Leukocytes
  Annual Review of Immunology, 1990
• Isolation and characterization of two monoclonal antibodies that recognize remote epitopes on the cell-binding domain of human fibronectin
  Experimental Cell Research, 1989
• Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein
  Gene, 1988
• Site-directed mutagenesis of the cell-binding domain of human fibronectin: Separable, synergistic sites mediate adhesive function
  Cell, 1988
• Cell surface proteoglycan binds mouse mammary epithelial cells to fibronectin and behaves as a receptor for interstitial matrix
  The Journal of cell biology, 1988
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970