Binding of Fibrin Monomer and Heparin to Thrombin in a Ternary Complex Alters the Environment of the Thrombin Catalytic Site, Reduces Affinity for Hirudin, and Inhibits Cleavage of Fibrinogen-Reference-Cited by-同舟云学术

Binding of Fibrin Monomer and Heparin to Thrombin in a Ternary Complex Alters the Environment of the Thrombin Catalytic Site, Reduces Affinity for Hirudin, and Inhibits Cleavage of Fibrinogen

Published:1996-10 Issue:42 Volume:271 Page:26088-26095
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Hogg Philip J.,Jackson Craig M.,Labanowski Jan K.,Bock Paul E.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference48 articles.

1. The clot thickens: clues provided by thrombin structure

2. Thrombin Functions and Antithrombotic Intervention

3. The refined 1.9-Å X-ray crystal structure of d-Phe-Pro-Arg chloromethylketone-inhibited humanα-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships

4. A player of many parts: The spotlight falls on thrombin's structure

5. Thrombin inhibitors A new generation of antithrombotics

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