Equilibrium Intermediates in the Unfolding Pathway of Creatine Kinase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference13 articles.
1. Further evidence for nonsymmetric subunit association and intersubunit cooperativity in creatine kinase. Subunit-selective modifications by 2,4-dinitrophenylthiocyanate.
2. Comparison of the rates of inactivation and conformational changes of creatine kinase during urea denaturation
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1. Folding studies on muscle type of creatine kinase from Pelodiscus sinensis;International Journal of Biological Macromolecules;2012-05
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3. Effect of Cysteine Modification on Creatine Kinase Aggregation;Applied Biochemistry and Biotechnology;2008-06-12
4. Towards creatine kinase aggregation due to the cysteine modification at the flexible active site and refolding pathway;International Journal of Biological Macromolecules;2007-10
5. Despite its high similarity with monomeric arginine kinase, muscle creatine kinase is only enzymatically active as a dimer;Archives of Biochemistry and Biophysics;2007-02
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