Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM
about
Elongation in translation as a dynamic interaction among the ribosome, tRNA, and elongation factors EF-G and EF-TuStructural insights into cognate versus near-cognate discrimination during decoding.How mutations in tRNA distant from the anticodon affect the fidelity of decodingDeducing the kinetics of protein synthesis in vivo from the transition rates measured in vitroThe natural history of transfer RNA and its interactions with the ribosomeProperties of Escherichia coli EF-Tu mutants designed for fluorescence resonance energy transfer from tRNA molecules.Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine.GTPases and the origin of the ribosome.Conformational sampling of aminoacyl-tRNA during selection on the bacterial ribosome.Structure and dynamics of a processive Brownian motor: the translating ribosomeFunctional elucidation of a key contact between tRNA and the large ribosomal subunit rRNA during decodingMutations in the intersubunit bridge regions of 16S rRNA affect decoding and subunit-subunit interactions on the 70S ribosomeHelix 69 is key for uniformity during substrate selection on the ribosome.The roles of RNA in the synthesis of protein.Phenotypic Suppression of Streptomycin Resistance by Mutations in Multiple Components of the Translation ApparatusVisualizing the protein synthesis machinery: new focus on the translational GTPase elongation factor TuA sequence element that tunes Escherichia coli tRNA(Ala)(GGC) to ensure accurate decoding.tRNA-nucleotidyltransferases: highly unusual RNA polymerases with vital functions.From DNA to proteins via the ribosome: structural insights into the workings of the translation machinery.Dynamics of the translational machineryA highly purified, fluorescently labeled in vitro translation system for single-molecule studies of protein synthesis.Structural Insights into tRNA Dynamics on the Ribosome.The mechanism of translation.The pathway to GTPase activation of elongation factor SelB on the ribosome.tRNA residues evolved to promote translational accuracy.Ribosome structural dynamics in translocation: yet another functional role for ribosomal RNA.Cryo-EM shows stages of initial codon selection on the ribosome by aa-tRNA in ternary complex with GTP and the GTPase-deficient EF-TuH84A.
P2860
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P2860
Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM
description
2008 nî lūn-bûn
@nan
2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM
@ast
Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM
@en
Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM
@nl
type
label
Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM
@ast
Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM
@en
Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM
@nl
prefLabel
Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM
@ast
Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM
@en
Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM
@nl
P2093
P2860
P50
P356
P1433
P1476
Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM
@en
P2093
Jianlin Lei
Julie L Brunelle
Lamine Bouakaz
Rachel Green
Suparna Sanyal
P2860
P304
P356
10.1038/EMBOJ.2008.243
P407
P577
2008-12-17T00:00:00Z