The 99 and 170 Loop-modified Factor VIIa Mutants Show Enhanced Catalytic Activity without Tissue Factor-Reference-Cited by-同舟云学术

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The 99 and 170 Loop-modified Factor VIIa Mutants Show Enhanced Catalytic Activity without Tissue Factor

Published:2002-12 Issue:50 Volume:277 Page:49027-49035
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Soejima Kenji,Yuguchi Masato,Mizuguchi Jun,Tomokiyo Kazuhiko,Nakashima Toshihiro,Nakagaki Tomohiro,Iwanaga Sadaaki

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference44 articles.

1. The coagulation cascade: initiation, maintenance, and regulation

2. Phospholipid-independent and -dependent interactions required for tissue factor receptor and cofactor function

3. Tissue factor potentiates the factor VIIa-catalyzed hydrolysis of an ester substrate.

4. The evaluation of complex-dependent alterations in human factor VIIa.

5. Identification of regions of bovine factor VII essential for binding to tissue factor.

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1. Dynamic Nature ofStaphylococcus aureusType I Signal Peptidases;2024-01-23

2. A systematic approach for evaluating the role of surface-exposed loops in trypsin-like serine proteases applied to the 170 loop in coagulation factor VIIa;Scientific Reports;2022-03-08

3. Conformational Plasticity-Rigidity Axis of the Coagulation Factor VII Zymogen Elucidated by Atomistic Simulations of the N-Terminally Truncated Factor VIIa Protease Domain;Biomolecules;2021-04-08

4. Beating tissue factor at its own game: Design and properties of a soluble tissue factor–independent coagulation factor VIIa;Journal of Biological Chemistry;2020-01

5. Different Roles of Some Key Residues in the S4 Pocket of Coagulation Factor Xa for Rivaroxaban Binding;CHEM J CHINESE U;2019

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