Many of the conserved nucleotides of tRNA(Phe) are not essential for ternary complex formation and peptide elongation.
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The role of exportin-t in selective nuclear export of mature tRNAsPost-transfer editing in vitro and in vivo by the beta subunit of phenylalanyl-tRNA synthetaseThe yeast gene YNL292w encodes a pseudouridine synthase (Pus4) catalyzing the formation of psi55 in both mitochondrial and cytoplasmic tRNAs.Transportin 3 promotes a nuclear maturation step required for efficient HIV-1 integration.Importance of the reverse Hoogsteen base pair 54-58 for tRNA function.A genetically encoded fluorescent tRNA is active in live-cell protein synthesis.Decoding the genome: a modified view.The tRNA specificity of Thermus thermophilus EF-Tu.Topological constraints are major determinants of tRNA tertiary structure and dynamics and provide basis for tertiary folding cooperativity.Recognition of the universally conserved 3'-CCA end of tRNA by elongation factor EF-Tu.Tuning the affinity of aminoacyl-tRNA to elongation factor Tu for optimal decodingAntideterminants present in minihelix(Sec) hinder its recognition by prokaryotic elongation factor Tu.RNA-dependent lipid remodeling by bacterial multiple peptide resistance factors.Posttranscriptional modification of retroviral primers is required for late stages of DNA replication.Identification of specific Rp-phosphate oxygens in the tRNA anticodon loop required for ribosomal P-site bindingLack of discrimination against non-proteinogenic amino acid norvaline by elongation factor Tu from Escherichia coli.Atypical archaeal tRNA pyrrolysine transcript behaves towards EF-Tu as a typical elongator tRNA.Perturbation of the tRNA tertiary core differentially affects specific steps of the elongation cycle.Structural variation and functional importance of a D-loop-T-loop interaction in valine-accepting tRNA-like structures of plant viral RNAs.Interaction of tRNAs with the ribosome at the A and P sites.Directed mutagenesis identifies amino acid residues involved in elongation factor Tu binding to yeast Phe-tRNAPhe.
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P2860
Many of the conserved nucleotides of tRNA(Phe) are not essential for ternary complex formation and peptide elongation.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on May 1994
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
@cs
name
Many of the conserved nucleotides of tRNA
@nl
Many of the conserved nucleoti ...... mation and peptide elongation.
@en
type
label
Many of the conserved nucleotides of tRNA
@nl
Many of the conserved nucleoti ...... mation and peptide elongation.
@en
prefLabel
Many of the conserved nucleotides of tRNA
@nl
Many of the conserved nucleoti ...... mation and peptide elongation.
@en
P2093
P2860
P1433
P1476
Many of the conserved nucleoti ...... rmation and peptide elongation
@en
P2093
I A Nazarenko
K M Harrington
O C Uhlenbeck
P2860
P304
P356
10.1002/J.1460-2075.1994.TB06531.X
P407
P577
1994-05-01T00:00:00Z