Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/38947.pdf
Reference50 articles.
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2. Hall, C. E. & Slayter, H. S. The fibrinogen molecule: its size, shape and mode of polymerization. J. Biophys. Biochem. Cytol. 5, 11–15 (1959).
3. Cohen, C. Invited discussion at 1960 Symposium on Protein Structure. J. Polymer Sci. 49, 144–145 (1961).
4. Doolittle, R. F., Cassman, K. G., Cottrell, B. A., Friezner, S. J. & Takagi, T. Amino acid sequence studies on the α-chain of human fibrinogen. The covalent structure of the α-chain portion of fragment D. Biochemistry 16, 1710–1710 (1977).
5. Laudano, A. P. & Doolittle, R. F. Studies on synthetic peptides that bind to fibrinogen and prevent fibrin polymerization. Structural requirements, numbers of binding sites and species differences. Biochemistry 19, 1013–1019 (1980).
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