Structure of an intermediate in the unfolding of creatine kinase
Author:
Publisher
Wiley
Subject
Molecular Biology,Biochemistry,Structural Biology
Reference43 articles.
1. An equilibrium study of the dependence of secondary and tertiary structure of creatine kinase on subunit association
2. Reversible Dissociation and Unfolding of Dimeric Creatine Kinase Isoenzyme MM in Guanidine Hydrochloride and Urea
3. Multiple-state equilibrium unfolding of guanidino kinases
4. Denaturation by guanidinium chloride of dimeric MM-creatine kinase and its proteinase K-nicked form: evidence for a multiple-step process
5. Discrimination between the Four Tryptophan Residues of MM-Creatine Kinase on the Basis of the Effect ofN-Bromosuccinimide on Activity and Spectral Properties
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1. Artificial-epitope mapping for CK-MB assay;The Analyst;2011
2. Mutation of the conserved Asp122 in the linker impedes creatine kinase reactivation and refolding;International Journal of Biological Macromolecules;2009-04
3. The conserved Cys254 plays a crucial role in creatine kinase refolding under non-reduced conditions but not in its activity or stability;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2008-12
4. The Generation of the Oxidized Form of Creatine Kinase Is a Negative Regulation on Muscle Creatine Kinase;Journal of Biological Chemistry;2007-04
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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