Ca binding of rat fibrinogen and fibrin(ogen) degradation products
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(78)80831-X/fullpdf
Reference10 articles.
1. Structural Aspects of the Fibrinogen to Fibrin Conversion
2. Equilibria in the fibrinogen-fibrin conversion
3. The ɛ-(γ-Glutamyl)Lysine Crosslink and the Catalytic Role of Transglutaminases
4. The binding of calcium to fibrinogen: Some structural features
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1. Kinetics of Fibrinopeptide Release by Thrombin as a Function of CaCl2 Concentration: Different Susceptibility of FPA and FPB and Evidence for a Fibrinogen Isoform-Specific Effect at Physiological Ca2+ Concentration;Biochemistry;2003-09-30
2. Conformational Changes in Fragments D and Double-D from Human Fibrin(ogen) upon Binding the Peptide Ligand Gly-His-Arg-Pro-Amide,;Biochemistry;1999-02-18
3. Crystal Structure of Fragment Double-D from Human Fibrin with Two Different Bound Ligands,;Biochemistry;1998-05-21
4. Characterization of an abnormal fibrinogen Osaka V with the replacement of gamma-arginine 375 by glycine. The lack of high affinity calcium binding to D-domains and the lack of protective effect of calcium on fibrinolysis.;Journal of Biological Chemistry;1992-02
5. Mutagenesis of human fibrinogen γ chain 259–411 synthesized in E. coli: Further characterization of the role of the disulfide bond CYS326–CYS339 in calcium binding;Biochemical and Biophysical Research Communications;1991-01
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