Misacylation of tRNA with methionine in Saccharomyces cerevisiae. - Test2 - elhamkhani - TriplyDB

Misacylation of tRNA with methionine in Saccharomyces cerevisiae.

Misacylation of tRNA with methionine in Saccharomyces cerevisiae.

http://www.wikidata.org/entity/Q36368822

about

Codon-biased translation can be regulated by wobble-base tRNA modification systems during cellular stress responses Regulation of translation dynamic and neoplastic conversion by tRNA and their pieces Evolutionary Gain of Alanine Mischarging to Noncognate tRNAs with a G4:U69 Base Pair Adaptive translation as a mechanism of stress response and adaptation.Promiscuous methionyl-tRNA synthetase mediates adaptive mistranslation to protect cells against oxidative stress.Mistranslation of the genetic code.Reversible, Specific, Active Aggregates of Endogenous Proteins Assemble upon Heat Stress A minimalist mitochondrial threonyl-tRNA synthetase exhibits tRNA-isoacceptor specificity during proofreading.Analysis of genetic code ambiguity arising from nematode-specific misacylated tRNAs.Ancestral AlaX editing enzymes for control of genetic code fidelity are not tRNA-specific.Methionine Mistranslation Bypasses the Restraint of the Genetic Code to Generate Mutant Proteins with Distinct Activities.A dual fluorescent reporter for the investigation of methionine mistranslation in live cells.Architecture and metamorphosis.Transfer RNA: a dancer between charging and mis-charging for protein biosynthesis.Exploring the evolutionary diversity and assembly modes of multi-aminoacyl-tRNA synthetase complexes: lessons from unicellular organisms.Emerging roles of tRNA in adaptive translation, signalling dynamics and disease.The ribosome challenge to the RNA world.Stress Response and Adaptation Mediated by Amino Acid Misincorporation during Protein Synthesis.Function and origin of mistranslation in distinct cellular contexts.Mechanism of oxidant-induced mistranslation by threonyl-tRNA synthetase.Evolving Mistranslating tRNAs Through a Phenotypically Ambivalent Intermediate in Saccharomyces cerevisiae.Temperature dependent mistranslation in a hyperthermophile adapts proteins to lower temperatures.Global tRNA misacylation induced by anaerobiosis and antibiotic exposure broadly increases stress resistance in Escherichia coli.Birth of the eukaryotes by a set of reactive innovations: New insights force us to relinquish gradual models.Translational fidelity and mistranslation in the cellular response to stress.tRNA Misacylation with Methionine in the Mouse Gut Microbiome in Situ.Determining the fidelity of tRNA aminoacylation via microarrays.

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P2860

Misacylation of tRNA with methionine in Saccharomyces cerevisiae.

http://www.wikidata.org/entity/Q36368822

description

2012 nî lūn-bûn

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2012年の論文

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2012年学术文章

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2012年学术文章

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2012年学术文章

@zh-hans

2012年学术文章

@zh-my

2012年学术文章

@zh-sg

2012年學術文章

@yue

2012年學術文章

@zh

2012年學術文章

@zh-hant

name

Misacylation of tRNA with methionine in Saccharomyces cerevisiae.

@ast

Misacylation of tRNA with methionine in Saccharomyces cerevisiae.

@en

type

label

Misacylation of tRNA with methionine in Saccharomyces cerevisiae.

@ast

Misacylation of tRNA with methionine in Saccharomyces cerevisiae.

@en

prefLabel

Misacylation of tRNA with methionine in Saccharomyces cerevisiae.

@ast

Misacylation of tRNA with methionine in Saccharomyces cerevisiae.

@en

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P1433

Nucleic Acids Research

P1476

Misacylation of tRNA with methionine in Saccharomyces cerevisiae.

@en

P2093

Elizabeth Wiltrout

http://www.w3.org/2001/XMLSchema#string

Jeffrey M Goodenbour

http://www.w3.org/2001/XMLSchema#string

Mathieu Fréchin

http://www.w3.org/2001/XMLSchema#string

Tao Pan

http://www.w3.org/2001/XMLSchema#string

P2860

Transformation of isolated mammalian mitochondria by bacterial conjugation

Genome-wide analysis of tRNA charging and activation of the eIF2 kinase Gcn2p

Methionine residues as endogenous antioxidants in proteins

Compilation of tRNA sequences and sequences of tRNA genes

A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases.

Arc1p organizes the yeast aminoacyl-tRNA synthetase complex and stabilizes its interaction with the cognate tRNAs.

Oxidants, oxidative stress and the biology of ageing

Uniform binding of aminoacyl-tRNAs to elongation factor Tu by thermodynamic compensation

Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration

MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification

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10494-10506

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scholarly article

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10.1093/NAR/GKS805

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20

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40

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2012-08-31T00:00:00Z

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Saccharomyces cerevisiae

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3488245

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