Role of tRNA amino acid-accepting end in aminoacylation and its quality control
about
Recent developments of engineered translational machineries for the incorporation of non-canonical amino acids into polypeptidesA Human Disease-causing Point Mutation in Mitochondrial Threonyl-tRNA Synthetase Induces Both Structural and Functional DefectsVibrio natriegens as a fast-growing host for molecular biologyGenomic evidence for plant-parasitic nematodes as the earliest Wolbachia hostsIdentification of lethal mutations in yeast threonyl-tRNA synthetase revealing critical residues in its human homolog.In vivo identification of essential nucleotides in tRNALeu to its functions by using a constructed yeast tRNALeu knockout strain.A minimalist mitochondrial threonyl-tRNA synthetase exhibits tRNA-isoacceptor specificity during proofreading.Next generation sequencing analysis of nine Corynebacterium ulcerans isolates reveals zoonotic transmission and a novel putative diphtheria toxin-encoding pathogenicity island.Modulation of Aminoacylation and Editing Properties of Leucyl-tRNA Synthetase by a Conserved Structural Module.Degenerate connective polypeptide 1 (CP1) domain from human mitochondrial leucyl-tRNA synthetase.C-terminal Domain of Leucyl-tRNA Synthetase from Pathogenic Candida albicans Recognizes both tRNASer and tRNALeuCrucial role of the C-terminal domain of Mycobacterium tuberculosis leucyl-tRNA synthetase in aminoacylation and editing.Translational fidelity maintenance preventing Ser mis-incorporation at Thr codon in protein from eukaryote.Leucine-specific domain modulates the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetaseThe Yin and Yang of tRNA: proper binding of acceptor end determines the catalytic balance of editing and aminoacylation.Aminoacylation and translational quality control strategy employed by leucyl-tRNA synthetase from a human pathogen with genetic code ambiguityCoexistence of bacterial leucyl-tRNA synthetases with archaeal tRNA binding domains that distinguish tRNA(Leu) in the archaeal mode.Transfer RNA: a dancer between charging and mis-charging for protein biosynthesis.Editing activity for eliminating mischarged tRNAs is essential in mammalian mitochondria.A natural non-Watson-Crick base pair in human mitochondrial tRNAThr causes structural and functional susceptibility to local mutations.An orthogonal ribosome-tRNA pair via engineering of the peptidyl transferase center.
P2860
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P2860
Role of tRNA amino acid-accepting end in aminoacylation and its quality control
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Role of tRNA amino acid-accepting end in aminoacylation and its quality control
@en
type
label
Role of tRNA amino acid-accepting end in aminoacylation and its quality control
@en
prefLabel
Role of tRNA amino acid-accepting end in aminoacylation and its quality control
@en
P2093
P2860
P356
P1476
Role of tRNA amino acid-accepting end in aminoacylation and its quality control
@en
P2093
Dao-Hai Du
En-Duo Wang
Gilbert Eriani
Hui-Yan Lei
Liang-Liang Ruan
Xiao-Long Zhou
P2860
P304
P356
10.1093/NAR/GKR595
P407
P577
2011-07-20T00:00:00Z