The N-terminal fragment of Acanthamoeba polyphaga mimivirus tyrosyl-tRNA synthetase (TyrRSapm ) is a monomer in solution
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/j.febslet.2013.01.048/fullpdf
Reference56 articles.
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2. Tyrosyl-tRNA synthetases;Bedouelle,2005
3. The crystal structure of tyrosyl-transfer RNA synthetase at 2∓7 A resolution;Irwin;J. Mol. Biol.,1976
4. Demonstration of two active sites on a monomeric aminoacyl-tRNA synthetase. Possible roles of negative cooperativity and half-of-the-sites reactivity in oligomeric enzymes;Fersht;Biochemistry,1975
5. Mechanism of aminoacylation of tRNA. Proof of the aminoacyl adenylate pathway for the isoleucyl- and tyrosyl-tRNA synthetases from Escherichia coli K12;Fersht;Biochemistry,1976
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1. Spectroscopic studies of the unfolding of a multimeric protein α-crystallin;Biopolymers;2014-02-21
2. VEGF, not VEGFR2, is associated with the angiogenesis effect of mini-TyrRS/mini-TrpRS in human umbilical vein endothelial cells in hypoxia;Cytotechnology;2013-07-30
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