The Anticoagulant Thrombin Mutant W215A/E217A Has a Collapsed Primary Specificity Pocket-Reference-Cited by-同舟云学术

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The Anticoagulant Thrombin Mutant W215A/E217A Has a Collapsed Primary Specificity Pocket

Published:2004-09 Issue:38 Volume:279 Page:39824-39828
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Pineda Agustin O.,Chen Zhi-Wei,Caccia Sonia,Cantwell Angelene M.,Savvides Savvas N.,Waksman Gabriel,Mathews F. Scott,Di Cera Enrico

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference26 articles.

1. The thrombin paradox

2. Thrombin Interactions

3. The Protein C Pathway

4. Single amino acid substitutions dissociate fibrinogen-clotting and thrombomodulin-binding activities of human thrombin.

5. Glu-192----Gln substitution in thrombin mimics the catalytic switch induced by thrombomodulin.

Cited by 53 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Allosteric Modulation of Thrombin by Thrombomodulin: Insights from Logistic Regression and Statistical Analysis of Molecular Dynamics Simulations;ACS Omega;2024-05-17

2. Unraveling the Impact of W215A/E217A Mutations on Thrombin’s Dynamics and Thrombomodulin Binding through Molecular Dynamics Simulations;2023-12-21

3. Thrombin - A Molecular Dynamics Perspective;Mini-Reviews in Medicinal Chemistry;2023-08-21

4. Simulations suggest double sodium binding induces unexpected conformational changes in thrombin;Journal of Molecular Modeling;2022-04-13

5. How Thrombomodulin Enables W215A/E217A Thrombin to Cleave Protein C but Not Fibrinogen;Biochemistry;2022-01-03

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