Bait Region Involvement in the Dimer-Dimer Interface of Human α2-Macroglobulin and in Mediating Gross Conformational Change
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference29 articles.
1. Three-dimensional structures of the human α2-macroglobulin-methylamine and chymotrypsin complexes
2. Structure-Function Relationships of Human ?2-Macroglobulin.
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4. The α-Macroglobulin Bait Region
5. Kinetics of the conformational alterations associated with nucleophilic modification of .alpha.2-macrobglobulin
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1. Development of selective protease inhibitors via engineering of the bait region of human α2-macroglobulin;Journal of Biological Chemistry;2021-07
2. Insight into the human pathodegradome of the V8 protease from Staphylococcus aureus;Cell Reports;2021-04
3. Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism;Molecular & Cellular Proteomics;2021
4. α2-Macroglobulins: Structure and Function;Subcellular Biochemistry;2017
5. Hypochlorite-induced structural modifications enhance the chaperone activity of human 2-macroglobulin;Proceedings of the National Academy of Sciences;2014-05-05
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