Conformational change at the active center of serine-proteases upon their binding to α2-macroglobulin
Author:
Publisher
Elsevier BV
Subject
General Medicine,Biochemistry
Reference22 articles.
1. Human α2-macroglobulin: structure and function
2. HUMAN PLASMA PROTEINASE INHIBITORS
3. The interaction of α2-macroglobulin with proteinases. Characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanism
4. In support of the trap hypothesis. Chymotrypsin is not rigidly held in its complex with human .alpha.2-macroglobulin
5. The two α2-Macroglobulin-bound trypsin molecules have different affinities for the basic pancreatic trypsin inhibitor
Cited by 5 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. The Binding of Receptor-recognized α2-Macroglobulin to the Low Density Lipoprotein Receptor-related Protein and the α2M Signaling Receptor Is Decoupled by Oxidation;Journal of Biological Chemistry;1997-08
2. Comparison ofLimulusα-Macroglobulin with Human α2-Macroglobulin: Thiol Ester Characterization, Subunit Organization, and Conformational Change;Archives of Biochemistry and Biophysics;1997-01
3. Differences in the proteinase inhibition mechanism of human alpha2-macroglobulin and pregnancy zone protein;European Journal of Biochemistry;1992-12
4. Ultrastructure of alpha 2-macroglobulins;Electron Microscopy Reviews;1992-01
5. Localization of the proteinases in the human ?2-macroglobulin-chymotrypsin complex by image processing of electron micrographs;Journal of Structural Biology;1991-02
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