Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site.
about
Mechanistic insights into cognate substrate discrimination during proofreading in translationYeast mitochondrial threonyl-tRNA synthetase recognizes tRNA isoacceptors by distinct mechanisms and promotes CUN codon reassignmentRole of the ubiquitin-like protein Urm1 as a noncanonical lysine-directed protein modifier.Multiple Quality Control Pathways Limit Non-protein Amino Acid Use by Yeast Cytoplasmic Phenylalanyl-tRNA Synthetase.The essential iron-sulfur protein Rli1 is an important target accounting for inhibition of cell growth by reactive oxygen species.Polyphosphate is a primordial chaperoneThe dual role of ubiquitin-like protein Urm1 as a protein modifier and sulfur carrierBiological Chemistry and Functionality of Protein Sulfenic Acids and Related Thiol ModificationsTranslation system engineering in Escherichia coli enhances non-canonical amino acid incorporation into proteins.Double-sieving-defective aminoacyl-tRNA synthetase causes protein mistranslation and affects cellular physiology and developmentReduced amino acid specificity of mammalian tyrosyl-tRNA synthetase is associated with elevated mistranslation of Tyr codons.Metabolomic Profiling of Soybeans (Glycine max L.) Reveals the Importance of Sugar and Nitrogen Metabolism under Drought and Heat StressAdaptive translation as a mechanism of stress response and adaptation.A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activityRedox status affects the catalytic activity of glutamyl-tRNA synthetase.Relaxed substrate specificity leads to extensive tRNA mischarging by Streptococcus pneumoniae class I and class II aminoacyl-tRNA synthetasesDoes the central dogma still stand?Mistranslation of the genetic code.Protein aggregation caused by aminoglycoside action is prevented by a hydrogen peroxide scavenger.Deficiencies in tRNA synthetase editing activity cause cardioproteinopathy.Misacylation of specific nonmethionyl tRNAs by a bacterial methionyl-tRNA synthetase.Protein mistranslation protects bacteria against oxidative stressA comprehensive method for detecting ubiquitinated substrates using TR-TUBE.Homologous trans-editing factors with broad tRNA specificity prevent mistranslation caused by serine/threonine misactivation.Transfer RNAs Mediate the Rapid Adaptation of Escherichia coli to Oxidative Stress.Structural analyses clarify the complex control of mistranslation by tRNA synthetasesGenome-wide ribosome profiling reveals complex translational regulation in response to oxidative stress.Selection of tRNA charging quality control mechanisms that increase mistranslation of the genetic code.Translation quality control is critical for bacterial responses to amino acid stress.Escherichia coli avoids high dissolved oxygen stress by activation of SoxRS and manganese-superoxide dismutase.Inhibition of Protein Ubiquitination by Paraquat and 1-Methyl-4-Phenylpyridinium Impairs Ubiquitin-Dependent Protein Degradation Pathways.Apoptosis and DNA damage in human spermatozoa.Reduced Protein Synthesis Fidelity Inhibits Flagellar Biosynthesis and Motility.Lipid II-independent trans editing of mischarged tRNAs by the penicillin resistance factor MurMInhibition of glutathione biosynthesis alters compartmental redox status and the thiol proteome in organogenesis-stage rat conceptusesMycobacterial mistranslation is necessary and sufficient for rifampicin phenotypic resistance.Upgrading protein synthesis for synthetic biology.Discovery of a Structurally Unique Small Molecule that Inhibits Protein SynthesisHomocysteine Editing, Thioester Chemistry, Coenzyme A, and the Origin of Coded Peptide Synthesis †.Molecular targets of oxidative stress.
P2860
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P2860
Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site.
description
2010 nî lūn-bûn
@nan
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
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
@wuu
name
Severe oxidative stress induce ...... -tRNA synthetase editing site.
@ast
Severe oxidative stress induce ...... -tRNA synthetase editing site.
@en
type
label
Severe oxidative stress induce ...... -tRNA synthetase editing site.
@ast
Severe oxidative stress induce ...... -tRNA synthetase editing site.
@en
prefLabel
Severe oxidative stress induce ...... -tRNA synthetase editing site.
@ast
Severe oxidative stress induce ...... -tRNA synthetase editing site.
@en
P2860
P356
P1476
Severe oxidative stress induce ...... l-tRNA synthetase editing site
@en
P2093
Dieter Söll
P2860
P304
P356
10.1073/PNAS.1000315107
P407
P50
P577
2010-02-16T00:00:00Z