Determinant nucleotides of yeast tRNA(Asp) interact directly with aspartyl-tRNA synthetase.
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Apicomplexa-specific tRip facilitates import of exogenous tRNAs into malaria parasitesFe.bleomycin as a probe of RNA conformation.RNA recognition by the DNA end-binding Ku heterodimer.Additive, cooperative and anti-cooperative effects between identity nucleotides of a tRNAThe peculiar architectural framework of tRNASec is fully recognized by yeast AspRS.Mirror image alternative interaction patterns of the same tRNA with either class I arginyl-tRNA synthetase or class II aspartyl-tRNA synthetaseFootprinting of tRNA(Phe) transcripts from Thermus thermophilus HB8 with the homologous phenylalanyl-tRNA synthetase reveals a novel mode of interaction.Influence of tRNA tertiary structure and stability on aminoacylation by yeast aspartyl-tRNA synthetase.Interaction of translation factor SELB with the formate dehydrogenase H selenopolypeptide mRNA.Evolution of acceptor stem tRNA recognition by class II prolyl-tRNA synthetase.A domain in the N-terminal extension of class IIb eukaryotic aminoacyl-tRNA synthetases is important for tRNA binding.Efficient aminoacylation of resected RNA helices by class II aspartyl-tRNA synthetase dependent on a single nucleotide.Cytosine methylation of tRNA-Asp by DNMT2 has a role in translation of proteins containing poly-Asp sequences.Interaction of mRNA with the Escherichia coli ribosome: accessibility of phosphorothioate-containing mRNA bound to ribosomes for iodine cleavage.Universal rules and idiosyncratic features in tRNA identity.A short fragment of 23S rRNA containing the binding sites for two ribosomal proteins, L24 and L4, is a key element for rRNA folding during early assembly.Determination of 2'-hydroxyl and phosphate groups important for aminoacylation of Escherichia coli tRNAAsp: a nucleotide analogue interference study.Structure of 5S rRNA within the Escherichia coli ribosome: iodine-induced cleavage patterns of phosphorothioate derivativesYeast tRNA(Asp) charging accuracy is threatened by the N-terminal extension of aspartyl-tRNA synthetase.Protection patterns of tRNAs do not change during ribosomal translocation.
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P2860
Determinant nucleotides of yeast tRNA(Asp) interact directly with aspartyl-tRNA synthetase.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on July 1992
@en
vedecký článok
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vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
Determinant nucleotides of yeast tRNA
@nl
Determinant nucleotides of yea ...... with aspartyl-tRNA synthetase.
@en
type
label
Determinant nucleotides of yeast tRNA
@nl
Determinant nucleotides of yea ...... with aspartyl-tRNA synthetase.
@en
prefLabel
Determinant nucleotides of yeast tRNA
@nl
Determinant nucleotides of yea ...... with aspartyl-tRNA synthetase.
@en
P2093
P2860
P356
P1476
Determinant nucleotides of yea ...... with aspartyl-tRNA synthetase.
@en
P2093
Eckstein F
Florentz C
Puglisi JD
Rudinger J
P2860
P304
P356
10.1073/PNAS.89.13.5882
P407
P577
1992-07-01T00:00:00Z