Aspartic acid 349 in the fourth epidermal growth factor-like structure of human thrombomodulin plays a role in its Ca(2+)-mediated binding to protein C.-Reference-Cited by-同舟云学术

Aspartic acid 349 in the fourth epidermal growth factor-like structure of human thrombomodulin plays a role in its Ca(2+)-mediated binding to protein C.

Published:1991-10 Issue:30 Volume:266 Page:19886-19889
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Zushi M.,Gomi K.,Honda G.,Kondo S.,Yamamoto S.,Hayashi T.,Suzuki K.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference19 articles.

1. Isolation of a membrane-bound cofactor for thrombin-catalyzed activation of protein C.

2. Structure and expression of human thrombomodulin, a thrombin receptor on endothelium acting as a cofactor for protein C activation.

3. Antithrombotic effect of recombinant human thrombomodulin on thrombin- induced thromboembolism in mice

4. The Last Three Consecutive Epidermal Growth Factor-like Structures of Human Thrombomodulin Comprise the Minimum Functional Domain for Protein C-activating Cofactor Activity and Anticoagulant Activity

5. Further localization of binding sites for thrombin and protein C in human thrombomodulin

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