Thiostrepton inhibits the turnover but not the GTPase of elongation factor G on the ribosome. - Wikidata - awgldk - TriplyDB

Thiostrepton inhibits the turnover but not the GTPase of elongation factor G on the ribosome.

Thiostrepton inhibits the turnover but not the GTPase of elongation factor G on the ribosome.

http://www.wikidata.org/entity/Q36426304

about

Purine bases at position 37 of tRNA stabilize codon-anticodon interaction in the ribosomal A site by stacking and Mg2+-dependent interactions.L11 domain rearrangement upon binding to RNA and thiostrepton studied by NMR spectroscopy Structures of modified eEF2 80S ribosome complexes reveal the role of GTP hydrolysis in translocation.The Structure of the Ribosome with Elongation Factor G Trapped in the Posttranslocational State NMR structures of thiostrepton derivatives for characterization of the ribosomal binding site Ribosome clearance by FusB-type proteins mediates resistance to the antibiotic fusidic acid Structure of the E. coli ribosome-EF-Tu complex at <3 Å resolution by Cs-corrected cryo-EM The bacterial ribosome as a target for antibiotics Elongation factor G-induced structural change in helix 34 of 16S rRNA related to translocation on the ribosome.Substrate recognition and modification by the nosiheptide resistance methyltransferase A covariant change of the two highly conserved bases in the GTPase-associated center of 28 S rRNA in silkworms and other moths.The ribosome as an entropy trap Antimicrobial evaluation of nocathiacins, a thiazole peptide class of antibiotics.Identification of distinct thiopeptide-antibiotic precursor lead compounds using translation machinery assays Ribosome rearrangements at the onset of translational bypassing Cleavage of the sarcin-ricin loop of 23S rRNA differentially affects EF-G and EF-Tu binding GTPases mechanisms and functions of translation factors on the ribosome.Probing translation with small-molecule inhibitors Mutations at the accommodation gate of the ribosome impair RF2-dependent translation termination.Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor.Correlated conformational events in EF-G and the ribosome regulate translocation.Colicin E3 cleavage of 16S rRNA impairs decoding and accelerates tRNA translocation on Escherichia coli ribosomes.Conformational changes of elongation factor G on the ribosome during tRNA translocation Differential effects of thiopeptide and orthosomycin antibiotics on translational GTPases.Role and timing of GTP binding and hydrolysis during EF-G-dependent tRNA translocation on the ribosome After the ribosome structure: how does translocation work?Mechanism of elongation factor G function in tRNA translocation on the ribosome.The fourth step of protein synthesis: disassembly of the posttermination complex is catalyzed by elongation factor G and ribosome recycling factor, a near-perfect mimic of tRNA.Thiostrepton interacts covalently with Rpt subunits of the 19S proteasome and proteasome substrates.Thiostrepton inhibition of tRNA delivery to the ribosome Importance of tRNA interactions with 23S rRNA for peptide bond formation on the ribosome: studies with substrate analogs.Rapid peptide bond formation on isolated 50S ribosomal subunits.YcaO-Dependent Posttranslational Amide Activation: Biosynthesis, Structure, and Function.A brief history of antibiotics and select advances in their synthesis.Post-termination complex disassembly by ribosome recycling factor, a functional tRNA mimic An uncharged amine in the transition state of the ribosomal peptidyl transfer reaction.Thiostrepton inhibits stable 70S ribosome binding and ribosome-dependent GTPase activation of elongation factor G and elongation factor 4 Inhibition of mitochondrial protein translation sensitizes melanoma cells to arsenic trioxide cytotoxicity via a reactive oxygen species dependent mechanism.A quantitative kinetic scheme for 70 S translation initiation complex formation.

P2860

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P2860

Thiostrepton inhibits the turnover but not the GTPase of elongation factor G on the ribosome.

http://www.wikidata.org/entity/Q36426304

description

1999 nî lūn-bûn

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1999年の論文

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1999年学术文章

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1999年学术文章

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1999年學術文章

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1999年學術文章

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1999年學術文章

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name

Thiostrepton inhibits the turn ...... tion factor G on the ribosome.

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Thiostrepton inhibits the turn ...... tion factor G on the ribosome.

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type

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Thiostrepton inhibits the turn ...... tion factor G on the ribosome.

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Thiostrepton inhibits the turn ...... tion factor G on the ribosome.

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Thiostrepton inhibits the turn ...... tion factor G on the ribosome.

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Thiostrepton inhibits the turn ...... tion factor G on the ribosome.

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Proceedings of the National Academy of Sciences of the United States of America

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Thiostrepton inhibits the turn ...... ation factor G on the ribosome

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P2093

A Savelsbergh

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N B Matassova

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V I Katunin

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W Wintermeyer

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Y P Semenkov

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P2860

Crystal structure of a conserved ribosomal protein-RNA complex

A detailed view of a ribosomal active site: the structure of the L11-RNA complex

Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome

Selection of the mRNA translation initiation region by Escherichia coli ribosomes

Interaction of elongation factors EF-G and EF-Tu with a conserved loop in 23S RNA.

Replacement of the L11 binding region within E.coli 23S ribosomal RNA with its homologue from yeast: in vivo and in vitro analysis of hybrid ribosomes altered in the GTPase centre.

GTP consumption of elongation factor Tu during translation of heteropolymeric mRNAs.

Alpha-sarcin cleavage of ribosomal RNA is inhibited by the binding of elongation factor G or thiostrepton to the ribosome.

Truncated elongation factor G lacking the G domain promotes translocation of the 3' end but not of the anticodon domain of peptidyl-tRNA.

Stabilization of a ribosomal RNA tertiary structure by ribosomal protein L11.

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22252

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