The Effect of a Reducing-end Extension on Pentasaccharide Binding by Antithrombin
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference31 articles.
1. Binding of high affinity heparin to antithrombin III. Stopped flow kinetic studies of the binding interaction.
2. Heparin-dependent Modification of the Reactive Center Arginine of Antithrombin and Consequent Increase in Heparin Binding Affinity
3. Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithrombin-thrombin reaction. Elucidation from salt concentration effects.
4. Role of Protein Conformational Changes, Surface Approximation and Protein Cofactors in Heparin-Accelerated Antithrombin-Proteinase Reactions
5. A mechanism for heparin-induced potentiation of antithrombin III
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1. Inactive mutants of human pyridoxine 5′‐phosphate oxidase: a possible role for a noncatalytic pyridoxal 5′‐phosphate tight binding site;FEBS Open Bio;2016-03-22
2. Re-visiting the structure of heparin;Carbohydrate Research;2015-02
3. Antithrombin-binding oligosaccharides: structural diversities in a unique function?;GLYCOCONJUGATE J;2014
4. Toward a robust computational screening strategy for identifying glycosaminoglycan sequences that display high specificity for target proteins;Glycobiology;2014-07-21
5. Effect of metal ions (Li+, Na+, K+, Mg2+ and Ca2+) and water on the conformational changes of glycosidic bonds in heparin oligosaccharides;RSC Advances;2013
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