Identification of two active functional domains of human adenylate kinase 5
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/j.febslet.2009.07.047/fullpdf
Reference18 articles.
1. Exchange of nucleoside monophosphate-binding domains in adenylate kinase and UMP/CMP kinase;Okajima;J. Biochem.,1998
2. Phosphorylation of deoxycytidine analog monophosphates by UMP–CMP kinase: molecular characterization of the human enzyme;Van Rompay;Mol. Pharmacol.,1999
3. Human UMP–CMP kinase 2, a novel nucleoside monophosphate kinase localized in mitochondria;Xu;J. Biol. Chem.,2008
4. Adenylate kinase 1 deficiency induces molecular and structural adaptations to support muscle energy metabolism;Janssen;J. Biol. Chem.,2003
5. Ancient divergence of long and short isoforms of adenylate kinase: molecular evolution of the nucleoside monophosphate kinase family;Fukami-Kobayashi;FEBS Lett.,1996
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