Hydrolytic editing by a class II aminoacyl-tRNA synthetase. - Wikidata - awgldk - TriplyDB

Hydrolytic editing by a class II aminoacyl-tRNA synthetase.

Hydrolytic editing by a class II aminoacyl-tRNA synthetase.

http://www.wikidata.org/entity/Q35190818

about

Post-transfer editing in vitro and in vivo by the beta subunit of phenylalanyl-tRNA synthetase In silico discovery of aminoacyl-tRNA synthetase inhibitors Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase The physiological target for LeuRS translational quality control is norvaline Loss of editing activity during the evolution of mitochondrial phenylalanyl-tRNA synthetase.Pre-transfer editing by class II prolyl-tRNA synthetase: role of aminoacylation active site in "selective release" of noncognate amino acids.An isolated class II aminoacyl-tRNA synthetase insertion domain is functional in amino acid editing Cell-specific differences in the requirements for translation quality control Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site.tRNA synthetase: tRNA aminoacylation and beyond Leucyl-tRNA synthetase from the ancestral bacterium Aquifex aeolicus contains relics of synthetase evolution.Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase.Resampling and editing of mischarged tRNA prior to translation elongation.Role of tRNA orthogonality in an expanded genetic code.Aminoacyl-tRNA synthetases: versatile players in the changing theater of translation.Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability Interstice mutations that block site-to-site translocation of a misactivated amino acid bound to a class I tRNA synthetase.Modular pathways for editing non-cognate amino acids by human cytoplasmic leucyl-tRNA synthetase Cysteinyl-tRNA formation and prolyl-tRNA synthetase.Fidelity escape by the unnatural amino acid β-hydroxynorvaline: an efficient substrate for Escherichia coli threonyl-tRNA synthetase with toxic effects on growth.Structural and mutational studies of the amino acid-editing domain from archaeal/eukaryal phenylalanyl-tRNA synthetase.Formation of two classes of tRNA synthetases in relation to editing functions and genetic code.Aminoacyl-tRNA synthesis: a postgenomic perspective.Substrate-mediated fidelity mechanism ensures accurate decoding of proline codons.Ancestral AlaX editing enzymes for control of genetic code fidelity are not tRNA-specific.Mechanism of tRNA-dependent editing in translational quality control Homologous trans-editing factors with broad tRNA specificity prevent mistranslation caused by serine/threonine misactivation.Substrate specificity of bacterial prolyl-tRNA synthetase editing domain is controlled by a tunable hydrophobic pocket Specificity and catalysis hardwired at the RNA-protein interface in a translational proofreading enzyme.Restoring species-specific posttransfer editing activity to a synthetase with a defunct editing domain Role of coupled dynamics in the catalytic activity of prokaryotic-like prolyl-tRNA synthetases.Phenylalanyl-tRNA synthetase editing defects result in efficient mistranslation of phenylalanine codons as tyrosine.In vitro assays for the determination of aminoacyl-tRNA synthetase editing activity.Selection of tRNA charging quality control mechanisms that increase mistranslation of the genetic code.A freestanding proofreading domain is required for protein synthesis quality control in Archaea.Aminoacyl-tRNA substrate and enzyme backbone atoms contribute to translational quality control by YbaK Exclusive use of trans-editing domains prevents proline mistranslation Transplantation of a tyrosine editing domain into a tyrosyl-tRNA synthetase variant enhances its specificity for a tyrosine analog.Quality control despite mistranslation caused by an ambiguous genetic code Multiple pathways promote dynamical coupling between catalytic domains in Escherichia coli prolyl-tRNA synthetase.

P2860

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P2860

Hydrolytic editing by a class II aminoacyl-tRNA synthetase.

http://www.wikidata.org/entity/Q35190818

description

2000 nî lūn-bûn

@nan

2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2000年の論文

@ja

2000年論文

@yue

2000年論文

@zh-hant

2000年論文

@zh-hk

2000年論文

@zh-mo

2000年論文

@zh-tw

2000年论文

@wuu

name

Hydrolytic editing by a class II aminoacyl-tRNA synthetase.

@ast

Hydrolytic editing by a class II aminoacyl-tRNA synthetase.

@en

type

label

Hydrolytic editing by a class II aminoacyl-tRNA synthetase.

@ast

Hydrolytic editing by a class II aminoacyl-tRNA synthetase.

@en

prefLabel

Hydrolytic editing by a class II aminoacyl-tRNA synthetase.

@ast

Hydrolytic editing by a class II aminoacyl-tRNA synthetase.

@en

P1433

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P356

PNAS.97.16.8916

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Hydrolytic editing by a class II aminoacyl-tRNA synthetase.

@en

P2093

K Musier-Forsyth

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

P J Beuning

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

P2860

Insights into editing from an ile-tRNA synthetase structure with tRNAile and mupirocin

Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase

Enzyme structure with two catalytic sites for double-sieve selection of substrate

Kinetic amplification of enzyme discrimination

Transfer ribonucleic acid-induced hydrolysis of valyladenylate bound to isoleucyl ribonucleic acid synthetase

tRNA(Pro) anticodon recognition by Thermus thermophilus prolyl-tRNA synthetase.

Phenylalanyl-tRNA synthetase and isoleucyl-tRNA Phe : a possible verification mechanism for aminoacyl-tRNA

Molecular recognition of tRNA(Pro) by Escherichia coli proline tRNA synthetase in vitro

Editing of errors in selection of amino acids for protein synthesis

Amino acid antagonist death in Escherichia coli.

P304

8916-8920

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scholarly article

P356

10.1073/PNAS.97.16.8916

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P433

16

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P478

97

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P577

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10922054

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16796

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