The Conformational State of Human α2-Macroglobulin Influences Its Dissociation into Half-Molecules by Sodium Thiocyanate
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
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. α2-Macroglobulins: Structure and Function;Subcellular Biochemistry;2017
2. The Three-dimensional Structure of the Human α2-Macroglobulin Dimer Reveals Its Structural Organization in the Tetrameric Native and Chymotrypsin α2-Macroglobulin Complexes;Journal of Biological Chemistry;2002-08
3. Conformational state and receptor recognition of the C-terminal domain of human α2-macroglobulin after dissociation into half-molecules;Clinica Chimica Acta;2001-08
4. The Structure of the C949S Mutant Human α2-Macroglobulin Demonstrates the Critical Role of the Internal Thiol Esters in Its Proteinase-Entrapping Structural Transformation;Journal of Structural Biology;2000-07
5. The Contact Zones in Human alpha2-Macroglobulin. Functional Domains Important for the Regulation of the Trapping Mechanism;European Journal of Biochemistry;1997-03-15
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