Significance of tryptophan residues in the d-domain of the fibrin molecule in fibrin polymer formation
Author:
Publisher
Elsevier BV
Subject
Biochemistry, Genetics and Molecular Biology (miscellaneous)
Reference14 articles.
1. Evidence for Localization of Polymerization Sites in Fibrinogen
2. Characterisation of a soluble D dimer-E complex in crosslinked fibrin digests
3. Amino acid sequence studies on the .alpha. chain of human fibrinogen. Overlapping sequences providing the complete sequence
4. Amino acid sequence of the .beta. chain of human fibrinogen
5. Primary Structure of Fibrinogen
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1. Photosensitized Cross-Linking of Tryptophan and Tyrosine Derivatives by Rose Bengal in Aqueous Solutions;The Journal of Organic Chemistry;2018-08-07
2. The oxidation produced by hydrogen peroxide on Ca‐ATP‐G‐actin;Protein Science;2000-01
3. The tert-Butyl Hydroperoxide-Induced Oxidation of Actin Cys-374 Is Coupled with Structural Changes in Distant Regions of the Protein;Biochemistry;1999-09-01
4. Trytophan residue in polymerization site of the carboxyl terminal domain of fibrinogen;International Journal of Biological Macromolecules;1986-10
5. Chapter 7 Fibrinogen, fibrin and factor XIII;Blood Coagulation;1986
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