STRUCTURE–FUNCTION RELATIONSHIP IN THE PLASMINOGEN ACTIVATOR ISOLATED FROM THE VENOM OFTRIMERESURUS STEJNEGERI-Reference-Cited by-同舟云学术

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STRUCTURE–FUNCTION RELATIONSHIP IN THE PLASMINOGEN ACTIVATOR ISOLATED FROM THE VENOM OFTRIMERESURUS STEJNEGERI

Published:2007-01 Issue:1 Volume:26 Page:1-24
ISSN:1556-9543
Container-title:Toxin Reviews
language:en
Short-container-title:Toxin Reviews

Author:

Le Bonniec Bernard F.

Publisher

Informa UK Limited

Subject

Toxicology

Link

http://www.tandfonline.com/doi/pdf/10.1080/15569540600567404

Reference56 articles.

1. Experimental and theoretical evidence supporting the role of Gly363 in blood coagulation factor IXa (Gly193 in chymotrypsin) for proper activation of the proenzyme.

2. Molecular defects in CRM+ factor VII deficiencies: modelling of missense mutations in the catalytic domain of FVII

3. Mapping of the Catalytic Groove Preferences of Factor Xa Reveals an Inadequate Selectivity for Its Macromolecule Substrates

4. The Contribution of Residues 192 and 193 to the Specificity of Snake Venom Serine Proteinases

5. The Stratagem Utilized by the Plasminogen Activator from the Snake Trimeresurus stejnegeri To Escape Serpins

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