Autophosphorylation of creatine kinase: characterization and identification of a specifically phosphorylated peptide
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference43 articles.
1. The primary structure of chicken B-creatine kinase and evidence for heterogeneity of its mRNA
2. Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the ‘phosphocreatine circuit’ for cellular energy homeostasis
3. Occurrence of Heterogenous Forms of the Subunits of Creatine Kinase in Various Muscle and Nonmuscle Tissues and Their Behaviour during Myogenesis
4. Effect of okadaic acid on protein phosphorylation patterns of chicken myogenic cells with special reference to creatine kinase
5. A unique chicken B-creatine kinase gene gives rise to two B-creatine kinase isoproteins with distinct N termini by alternative splicing.
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4. Regulation of brain-type creatine kinase by AMP-activated protein kinase: Interaction, phosphorylation and ER localization;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2014-08
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