Structural basis for substrate recognition by the editing domain of isoleucyl-tRNA synthetase.
about
Evolutionary Limitation and Opportunities for Developing tRNA Synthetase Inhibitors with 5-Binding-Mode ClassificationMechanistic insights into cognate substrate discrimination during proofreading in translationThe Mechanism of Pre-transfer Editing in Yeast Mitochondrial Threonyl-tRNA SynthetaseMechanism of chiral proofreading during translation of the genetic codePre-transfer editing by class II prolyl-tRNA synthetase: role of aminoacylation active site in "selective release" of noncognate amino acids.Discovery and Investigation of Natural Editing Function against Artificial Amino Acids in Protein TranslationLigand co-crystallization of aminoacyl-tRNA synthetases from infectious disease organismsThe balance between pre- and post-transfer editing in tRNA synthetases.Partitioning of tRNA-dependent editing between pre- and post-transfer pathways in class I aminoacyl-tRNA synthetases.Coordination of tRNA synthetase active sites for chemical fidelityUneven spread of cis- and trans-editing aminoacyl-tRNA synthetase domains within translational compartments of P. falciparum.Specificity and catalysis hardwired at the RNA-protein interface in a translational proofreading enzyme.Amino acid toxicities of Escherichia coli that are prevented by leucyl-tRNA synthetase amino acid editingDNA polymerases and aminoacyl-tRNA synthetases: shared mechanisms for ensuring the fidelity of gene expressionTransfer RNA: a dancer between charging and mis-charging for protein biosynthesis.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.Synthesis and biological evaluation of non-isomerizable analogues of Ala-tRNA(Ala).Synthesis of 2'-([1,2,3]triazol-1-yl)-2'-deoxyadenosines.Identification of the nucleophilic factors and the productive complex for the editing reaction by leucyl-tRNA synthetase.
P2860
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P2860
Structural basis for substrate recognition by the editing domain of isoleucyl-tRNA synthetase.
description
2006 nî lūn-bûn
@nan
2006 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Structural basis for substrate ...... of isoleucyl-tRNA synthetase.
@ast
Structural basis for substrate ...... of isoleucyl-tRNA synthetase.
@en
Structural basis for substrate ...... of isoleucyl-tRNA synthetase.
@nl
type
label
Structural basis for substrate ...... of isoleucyl-tRNA synthetase.
@ast
Structural basis for substrate ...... of isoleucyl-tRNA synthetase.
@en
Structural basis for substrate ...... of isoleucyl-tRNA synthetase.
@nl
prefLabel
Structural basis for substrate ...... of isoleucyl-tRNA synthetase.
@ast
Structural basis for substrate ...... of isoleucyl-tRNA synthetase.
@en
Structural basis for substrate ...... of isoleucyl-tRNA synthetase.
@nl
P1476
Structural basis for substrate ...... of isoleucyl-tRNA synthetase.
@en
P304
P356
10.1016/J.JMB.2006.04.025
P407
P577
2006-04-25T00:00:00Z