Allostery in Coagulation Factor VIIa Revealed by Ensemble Refinement of Crystallographic Structures-Reference-Cited by-同舟云学术

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Allostery in Coagulation Factor VIIa Revealed by Ensemble Refinement of Crystallographic Structures

Published:2019-05 Issue:10 Volume:116 Page:1823-1835
ISSN:0006-3495
Container-title:Biophysical Journal
language:en
Short-container-title:Biophysical Journal

Author:

Sorensen Anders B.,Madsen Jesper J.,Frimurer Thomas M.,Overgaard Michael T.,Gandhi Prafull S.,Persson Egon,Olsen Ole H.

Funder

Danish Agency for Science, Technology and Innovation

Novo Nordisk R&D Science Talent Attraction and Recruitment

Carlsberg Foundation

Publisher

Elsevier BV

Subject

Biophysics

Reference41 articles.

1. Trypsin and trypsin-like proteases in the brain: proteolysis and cellular functions;Wang;Cell. Mol. Life Sci,2008

2. Crystal structure of bovine trypsinogen at 1-8 A resolution. II. Crystallographic refinement, refined crystal structure and comparison with bovine trypsin;Fehlhammer;J. Mol. Biol,1977

3. Structural basis of the activation and action of trypsin;Huber;Acc. Chem. Res,1978

4. The coagulation cascade: initiation, maintenance, and regulation;Davie;Biochemistry,1991

5. The length of the linker between the epidermal growth factor-like domains in factor VIIa is critical for a productive interaction with tissue factor;Persson;Protein Sci,2014

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3. Elucidating the complex membrane binding of a protein with multiple anchoring domains;2023-08-14

4. Structural and functional characterization of novel F7 mutations identified in Chinese factor VII‐deficient patients;British Journal of Haematology;2023-03-23

5. Mechanistic basis of GPCR activation explored by ensemble refinement of crystallographic structures;Protein Science;2022-10-26

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