Initiation factor IF2, thiostrepton and micrococcin prevent the binding of elongation factor G to the Escherichia coli ribosome.
about
Ribosomal protection proteins and their mechanism of tetracycline resistanceStructural insights into ribosome translocationCommon and distinctive features of GNRA tetraloops based on a GUAA tetraloop structure at 1.4 A resolution.L11 domain rearrangement upon binding to RNA and thiostrepton studied by NMR spectroscopyRecognition of ribosomal protein L11 by the protein trimethyltransferase PrmAThe common and the distinctive features of the bulged-G motif based on a 1.04 A resolution RNA structureMultiple-Site Trimethylation of Ribosomal Protein L11 by the PrmA MethyltransferaseThe Structure of the Ribosome with Elongation Factor G Trapped in the Posttranslocational StateSubstrate recognition and modification by the nosiheptide resistance methyltransferaseAntimicrobial evaluation of nocathiacins, a thiazole peptide class of antibiotics.Phylogenetic distribution of translational GTPases in bacteriaManipulation of thiocillin variants by prepeptide gene replacement: structure, conformation, and activity of heterocycle substitution mutants.Cleavage of the sarcin-ricin loop of 23S rRNA differentially affects EF-G and EF-Tu bindingThiazolyl peptide antibiotic biosynthesis: a cascade of post-translational modifications on ribosomal nascent proteins.Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.EF-G-independent reactivity of a pre-translocation-state ribosome complex with the aminoacyl tRNA substrate puromycin supports an intermediate (hybrid) state of tRNA bindingInitiation of protein synthesis in bacteria.Mechanism of Tet(O)-mediated tetracycline resistance.Differential effects of thiopeptide and orthosomycin antibiotics on translational GTPases.After the ribosome structure: how does translocation work?Thiostrepton-resistant mutants of Thermus thermophilus.Thiopeptide antibiotics stimulate biofilm formation in Bacillus subtilis.Ribosomal proteins in the spotlight.Fungal ribotoxins: molecular dissection of a family of natural killers.The posttranslational modification cascade to the thiopeptide berninamycin generates linear forms and altered macrocyclic scaffoldsMutations in conserved helix 69 of 23S rRNA of Thermus thermophilus that affect capreomycin resistance but not posttranscriptional modificationsGeneration of thiocillin variants by prepeptide gene replacement and in vivo processing by Bacillus cereus.YcaO-Dependent Posttranslational Amide Activation: Biosynthesis, Structure, and Function.A dedicated translation factor controls the synthesis of the global regulator Fis.Thiostrepton inhibits stable 70S ribosome binding and ribosome-dependent GTPase activation of elongation factor G and elongation factor 4A quantitative kinetic scheme for 70 S translation initiation complex formation.Ribosomal localization of translation initiation factor IF2Posttranslational Modifications of Ribosomal Proteins in Escherichia coli.Elongation factor G stabilizes the hybrid-state conformation of the 70S ribosome.Dissociation of intact Escherichia coli ribosomes in a mass spectrometer. Evidence for conformational change in a ribosome elongation factor G complex.Release of ribosome-bound ribosome recycling factor by elongation factor G.Interaction of thiostrepton and elongation factor-G with the ribosomal protein L11-binding domain.Interactions of the N-terminal domain of ribosomal protein L11 with thiostrepton and rRNA.
P2860
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P2860
Initiation factor IF2, thiostrepton and micrococcin prevent the binding of elongation factor G to the Escherichia coli ribosome.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh-hant
name
Initiation factor IF2, thiostr ...... the Escherichia coli ribosome.
@en
Initiation factor IF2, thiostr ...... the Escherichia coli ribosome.
@nl
type
label
Initiation factor IF2, thiostr ...... the Escherichia coli ribosome.
@en
Initiation factor IF2, thiostr ...... the Escherichia coli ribosome.
@nl
prefLabel
Initiation factor IF2, thiostr ...... the Escherichia coli ribosome.
@en
Initiation factor IF2, thiostr ...... the Escherichia coli ribosome.
@nl
P2093
P1476
Initiation factor IF2, thiostr ...... the Escherichia coli ribosome.
@en
P2093
Albert E Dahlberg
Dale M Cameron
Jill Thompson
Paul E March
P356
10.1016/S0022-2836(02)00235-8
P407
P577
2002-05-01T00:00:00Z