The importance of tRNA backbone-mediated interactions with synthetase for aminoacylation.
about
A single residue in leucyl-tRNA synthetase affecting amino acid specificity and tRNA aminoacylationLoss of editing activity during the evolution of mitochondrial phenylalanyl-tRNA synthetase.Computational analysis of tRNA identity.Recognition of acceptor-stem structure of tRNA(Asp) by Escherichia coli aspartyl-tRNA synthetase.Improved amber and opal suppressor tRNAs for incorporation of unnatural amino acids in vivo. Part 2: evaluating suppression efficiency.Improved amber and opal suppressor tRNAs for incorporation of unnatural amino acids in vivo. Part 1: minimizing misacylationRecurrent RNA motifs as probes for studying RNA-protein interactions in the ribosomeRevisiting the operational RNA code for amino acids: Ensemble attributes and their implications.A new assay for tRNA aminoacylation kineticsAlternative designs for construction of the class II transfer RNA tertiary core.Structural insights into translational recoding by frameshift suppressor tRNASufJ.Surprising contribution to aminoacylation and translation of non-Watson-Crick pairs in tRNA.Correlation of deformability at a tRNA recognition site and aminoacylation specificity.In silico detection of tRNA sequence features characteristic to aminoacyl-tRNA synthetase class membershipGrowth-regulating Mycobacterium tuberculosis VapC-mt4 toxin is an isoacceptor-specific tRNase.Different aa-tRNAs are selected uniformly on the ribosome.A sequence element that tunes Escherichia coli tRNA(Ala)(GGC) to ensure accurate decoding.Long-range intramolecular signaling in a tRNA synthetase complex revealed by pre-steady-state kinetics.Universal rules and idiosyncratic features in tRNA identity.Functional analysis of human tRNA isodecoders.Determination of 2'-hydroxyl and phosphate groups important for aminoacylation of Escherichia coli tRNAAsp: a nucleotide analogue interference study.
P2860
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P2860
The importance of tRNA backbone-mediated interactions with synthetase for aminoacylation.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
The importance of tRNA backbone-mediated interactions with synthetase for aminoacylation.
@ast
The importance of tRNA backbone-mediated interactions with synthetase for aminoacylation.
@en
type
label
The importance of tRNA backbone-mediated interactions with synthetase for aminoacylation.
@ast
The importance of tRNA backbone-mediated interactions with synthetase for aminoacylation.
@en
prefLabel
The importance of tRNA backbone-mediated interactions with synthetase for aminoacylation.
@ast
The importance of tRNA backbone-mediated interactions with synthetase for aminoacylation.
@en
P2093
P2860
P356
P1476
The importance of tRNA backbone-mediated interactions with synthetase for aminoacylation.
@en
P2093
J Schneider
S Bhattacharya
W H McClain
P2860
P304
P356
10.1073/PNAS.95.2.460
P407
P577
1998-01-01T00:00:00Z