Phenylalanyl-tRNA synthetase editing defects result in efficient mistranslation of phenylalanine codons as tyrosine.
about
Eukaryotic cytosolic and mitochondrial phenylalanyl-tRNA synthetases catalyze the charging of tRNA with the meta-tyrosineElongation Factor Tu Prevents Misediting of Gly-tRNA(Gly) Caused by the Design Behind the Chiral Proofreading Site of D-Aminoacyl-tRNA DeacylaseEditing of misaminoacylated tRNA controls the sensitivity of amino acid stress responses in Saccharomyces cerevisiaeCell-specific differences in the requirements for translation quality controlSevere oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site.Oxidation of cellular amino acid pools leads to cytotoxic mistranslation of the genetic codeAminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase.Missense suppressor mutations in 16S rRNA reveal the importance of helices h8 and h14 in aminoacyl-tRNA selection.Resampling and editing of mischarged tRNA prior to translation elongation.Misacylation of specific nonmethionyl tRNAs by a bacterial methionyl-tRNA synthetase.(R)-β-lysine-modified elongation factor P functions in translation elongation.Exclusive use of trans-editing domains prevents proline mistranslationTransplantation of a tyrosine editing domain into a tyrosyl-tRNA synthetase variant enhances its specificity for a tyrosine analog.Lack of discrimination against non-proteinogenic amino acid norvaline by elongation factor Tu from Escherichia coli.Quality control despite mistranslation caused by an ambiguous genetic codeLipid II-independent trans editing of mischarged tRNAs by the penicillin resistance factor MurMDifferent aa-tRNAs are selected uniformly on the ribosome.Transfer RNA: a dancer between charging and mis-charging for protein biosynthesis.Isoacceptor specific characterization of tRNA aminoacylation and misacylation in vivo.Game-changing restraint of Ros-damaged phenylalanine, upon tumor metastasis.mRNA Translation Gone Awry: Translation Fidelity and Neurological Disease.Aminoacyl-tRNA quality control is required for efficient activation of the TOR pathway regulator Gln3p.Errors during Gene Expression: Single-Cell Heterogeneity, Stress Resistance, and Microbe-Host Interactions.
P2860
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P2860
Phenylalanyl-tRNA synthetase editing defects result in efficient mistranslation of phenylalanine codons as tyrosine.
description
2007 nî lūn-bûn
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2007年の論文
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2007年論文
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2007年論文
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2007年論文
@zh-hk
2007年論文
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2007年論文
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2007年论文
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2007年论文
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name
Phenylalanyl-tRNA synthetase e ...... nylalanine codons as tyrosine.
@ast
Phenylalanyl-tRNA synthetase e ...... nylalanine codons as tyrosine.
@en
type
label
Phenylalanyl-tRNA synthetase e ...... nylalanine codons as tyrosine.
@ast
Phenylalanyl-tRNA synthetase e ...... nylalanine codons as tyrosine.
@en
prefLabel
Phenylalanyl-tRNA synthetase e ...... nylalanine codons as tyrosine.
@ast
Phenylalanyl-tRNA synthetase e ...... nylalanine codons as tyrosine.
@en
P2860
P356
P1433
P1476
Phenylalanyl-tRNA synthetase e ...... enylalanine codons as tyrosine
@en
P2093
Michael Ibba
Srujana S Yadavalli
P2860
P304
P356
10.1261/RNA.684107
P407
P50
P577
2007-09-05T00:00:00Z