The NH2-terminal fibrin-binding site of fibronectin is formed by interacting fourth and fifth finger domains. Studies with recombinant finger fragments expressed in Escherichia coli
Open Access
- 1 April 1994
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 269 (13) , 9539-9546
- https://doi.org/10.1016/s0021-9258(17)36915-6
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Secondary structure of a pair of fibronectin type 1 modules by two-dimensional nuclear magnetic resonanceBiochemistry, 1993
- Ribonuclease S‐peptide as a carrier in fusion proteinsProtein Science, 1993
- Specificity of Factor Xa in the cleavage of fusion proteinsProtein Journal, 1993
- Generation of full-length cDNA recombinant vectors for the transient expression of human fibronectin in mammalian cell linesExperimental Cell Research, 1991
- Domain structure and interactions of the type I and type II modules in the gelatin-binding region of fibronectin: All six modules are independently foldedJournal of Molecular Biology, 1991
- The elastic modulus of fibrin clots and fibrinogen gels: The effect of fibronectin and dithiothreitolBiopolymers, 1990
- SPECIFICITY OF FIBRONECTIN‐FIBRIN CROSS‐LINKING*Annals of the New York Academy of Sciences, 1983
- Affinity Chromatography on Immobilized Fibrin Monomer, IV. Two Fibrin-Binding Peptides of a Chymotryptic Digest of Human Plasma FibronectinHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1983
- Shape, conformation and stability of fibronectin fragments determined by electron microscopy, circular dichroism and ultracentrifugationJournal of Molecular Biology, 1982
- Amino acid sequence of the factor XIIIa acceptor site in bovine plasma fibronectinFEBS Letters, 1981