Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase.
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The Mechanism of Pre-transfer Editing in Yeast Mitochondrial Threonyl-tRNA SynthetaseYeast mitochondrial threonyl-tRNA synthetase recognizes tRNA isoacceptors by distinct mechanisms and promotes CUN codon reassignmentThe physiological target for LeuRS translational quality control is norvalineA Human Disease-causing Point Mutation in Mitochondrial Threonyl-tRNA Synthetase Induces Both Structural and Functional DefectstRNA synthetase: tRNA aminoacylation and beyondPartitioning of tRNA-dependent editing between pre- and post-transfer pathways in class I aminoacyl-tRNA synthetases.Amino-acid-dependent shift in tRNA synthetase editing mechanisms.Modular pathways for editing non-cognate amino acids by human cytoplasmic leucyl-tRNA synthetaseFidelity escape by the unnatural amino acid β-hydroxynorvaline: an efficient substrate for Escherichia coli threonyl-tRNA synthetase with toxic effects on growth.Substrate-mediated fidelity mechanism ensures accurate decoding of proline codons.Kinetic partitioning between synthetic and editing pathways in class I aminoacyl-tRNA synthetases occurs at both pre-transfer and post-transfer hydrolytic stepsRational design and directed evolution of a bacterial-type glutaminyl-tRNA synthetase precursorTranslational fidelity maintenance preventing Ser mis-incorporation at Thr codon in protein from eukaryote.Role of tRNA amino acid-accepting end in aminoacylation and its quality controlAminoacyl-tRNA synthetases.The tRNA A76 Hydroxyl Groups Control Partitioning of the tRNA-dependent Pre- and Post-transfer Editing Pathways in Class I tRNA Synthetase.Naturally Occurring Isoleucyl-tRNA Synthetase without tRNA-dependent Pre-transfer Editing.Determinants for tRNA-dependent pretransfer editing in the synthetic site of isoleucyl-tRNA synthetase.The α-amino group of the threonine substrate as the general base during tRNA aminoacylation: a new version of substrate-assisted catalysis predicted by hybrid DFT.The pimeloyl-CoA synthetase BioW defines a new fold for adenylate-forming enzymes.11th IUBMB Focused Meeting on the Aminoacyl-tRNA Synthetases: Sailing a New Sea of Complex Functions in Human Biology and Disease.
P2860
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P2860
Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase.
description
2010 nî lūn-bûn
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2010 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2010年の論文
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2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
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name
Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase.
@ast
Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase.
@en
Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase.
@nl
type
label
Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase.
@ast
Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase.
@en
Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase.
@nl
prefLabel
Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase.
@ast
Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase.
@en
Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase.
@nl
P2860
P356
P1476
Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase.
@en
P2093
Anand Minajigi
Christopher S Francklyn
P2860
P304
23810-23817
P356
10.1074/JBC.M110.105320
P407
P577
2010-05-26T00:00:00Z