Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP.
about
Substrate discrimination in RNase P RNA-mediated cleavage: importance of the structural environment of the RNase P cleavage siteTranslation elongation factor-1 alpha interacts with the 3' stem-loop region of West Nile virus genomic RNAReview: Translational GTPasesA genetically encoded fluorescent tRNA is active in live-cell protein synthesis.Direct evaluation of tRNA aminoacylation status by the T-box riboswitch using tRNA-mRNA stacking and steric readout.The determination of tRNALeu recognition nucleotides for Escherichia coli L/F transferaseMutants of elongation factor Tu promote ribosomal frameshifting and nonsense readthrough.The tRNA specificity of Thermus thermophilus EF-Tu.Aminoacyl-tRNA-charged eukaryotic elongation factor 1A is the bona fide substrate for Legionella pneumophila effector glucosyltransferasesDirect evidence of an elongation factor-Tu/Ts·GTP·Aminoacyl-tRNA quaternary complex.Role of tRNA orthogonality in an expanded genetic code.Binding of misacylated tRNAs to the ribosomal A site.Mutants of Escherichia coli formylmethionine tRNA: a single base change enables initiator tRNA to act as an elongator in vitroTuning the affinity of aminoacyl-tRNA to elongation factor Tu for optimal decodingIs the sequence-specific binding of aminoacyl-tRNAs by EF-Tu universal among bacteria?Protein synthesis elongation factor EF-1 alpha is essential for ubiquitin-dependent degradation of certain N alpha-acetylated proteins and may be substituted for by the bacterial elongation factor EF-TuHistidine 66 in Escherichia coli elongation factor tu selectively stabilizes aminoacyl-tRNAs.Structure and mechanism of the T-box riboswitches.The 51-63 base pair of tRNA confers specificity for binding by EF-TuA minor arginine tRNA mutant limits translation preferentially of a protein dependent on the cognate codon.The RNA binding protein Hfq interacts specifically with tRNAs.Lack of discrimination against non-proteinogenic amino acid norvaline by elongation factor Tu from Escherichia coli.Cloning and characterization of EF-Tu and EF-Ts from Pseudomonas aeruginosa.Different aa-tRNAs are selected uniformly on the ribosome.A sequence element that tunes Escherichia coli tRNA(Ala)(GGC) to ensure accurate decoding.Understanding the sequence specificity of tRNA binding to elongation factor Tu using tRNA mutagenesis.The Escherichia coli argU10(Ts) phenotype is caused by a reduction in the cellular level of the argU tRNA for the rare codons AGA and AGG.Many of the conserved nucleotides of tRNA(Phe) are not essential for ternary complex formation and peptide elongation.Probing the importance of tRNA anticodon: human immunodeficiency virus type 1 (HIV-1) RNA genome complementarity with an HIV-1 that selects tRNA(Glu) for replication.Crosslinking of elongation factor Tu to tRNA(Phe) by trans-diamminedichloroplatinum (II). Characterization of two crosslinking sites in the tRNA.Ser-tRNAs from bovine mitochondrion form ternary complexes with bacterial elongation factor Tu and GTP.The role of modified purine 64 in initiator/elongator discrimination of tRNA(iMet) from yeast and wheat germ.Crosslinking of tRNA containing a long extra arm to elongation factor Tu by trans-diamminedichloroplatinum(II).Interaction of the isolated domain II/III of Thermus thermophilus elongation factor Tu with the nucleotide exchange factor EF-Ts.Outwitting EF-Tu and the ribosome: translation with d-amino acids.A disease-causing point mutation in human mitochondrial tRNAMet results in tRNA misfolding leading to defects in translational initiation and elongation.An ancient P-loop GTPase in rice is regulated by a higher plant-specific regulatory protein.The interface between Escherichia coli elongation factor Tu and aminoacyl-tRNA.Directed mutagenesis identifies amino acid residues involved in elongation factor Tu binding to yeast Phe-tRNAPhe.tRNAPyl: Structure, function, and applications.
P2860
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P2860
Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP.
description
1984 nî lūn-bûn
@nan
1984 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1984 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1984年の論文
@ja
1984年論文
@yue
1984年論文
@zh-hant
1984年論文
@zh-hk
1984年論文
@zh-mo
1984年論文
@zh-tw
1984年论文
@wuu
name
Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP.
@ast
Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP.
@en
Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP.
@nl
type
label
Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP.
@ast
Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP.
@en
Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP.
@nl
prefLabel
Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP.
@ast
Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP.
@en
Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP.
@nl
P2093
P1476
Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP
@en
P2093
P304
P407
P577
1984-04-01T00:00:00Z