α2-Macroglobulin bait region integrity
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(93)81086-F/fullpdf
Reference12 articles.
1. α-Macroglobulins: structure, shape, and mechanism of proteinase complex formation
2. Physical properties of human α2-macroglobulin following reaction with methylamine and trypsin
3. Evidence for similar conformational changes in α2-macroglobulin on reaction with primary amines or proteolytic enzymes
4. Inhibitors of Lysosomal Proteinases
5. Three-dimensional structures of the human α2-macroglobulin-methylamine and chymotrypsin complexes
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1. Cryo-EM structures reveal the dynamic transformation of human alpha-2-macroglobulin working as a protease inhibitor;Science China Life Sciences;2022-06-28
2. Cryo-EM structures reveal a dynamic transformation process of human alpha-2-macroglobulin working as a protease inhibitor;2022-05-10
3. Alpha-2-macroglobulin: A physiological guardian;Journal of Cellular Physiology;2013-04-18
4. Comparison ofLimulusα-Macroglobulin with Human α2-Macroglobulin: Thiol Ester Characterization, Subunit Organization, and Conformational Change;Archives of Biochemistry and Biophysics;1997-01
5. Low Resolution X-ray Structure of Human Methylamine-treated α2-Macroglobulin;Journal of Biological Chemistry;1995-10
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