The Allosteric Mechanism of Activation of Antithrombin as an Inhibitor of Factor IXa and Factor Xa
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference36 articles.
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3. Binding of high affinity heparin to antithrombin III. Characterization of the protein fluorescence enhancement;Olson;J. Biol. Chem,1981
4. Deconvolution of the fluorescence emission spectrum of human antithrombin and identification of the tryptophan residues that are responsive to heparin binding;Meagher;J. Biol. Chem,1998
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1. Positive Allosteric Modulation of Antithrombin's Inhibitory Activity by RNA Aptamers;Nucleic Acid Therapeutics;2023-08-01
2. Paramount Importance of Core Conformational Changes for Heparin Allosteric Activation of Antithrombin;Biochemistry;2021-04-06
3. Cooperative Interactions of Three Hotspot Heparin Binding Residues Are Critical for Allosteric Activation of Antithrombin by Heparin;Biochemistry;2018-03-21
4. Antithrombin conformational modulation by D-myo-inositol 3,4,5,6-tetrakisphosphate (TMI), a novel scaffold for the development of antithrombotic agents;Journal of Biomolecular Structure and Dynamics;2017-12-11
5. Serpins in arthropod biology;Seminars in Cell & Developmental Biology;2017-02
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