GTP consumption of elongation factor Tu during translation of heteropolymeric mRNAs. - Wikidata - awgldk - TriplyDB

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

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

http://www.wikidata.org/entity/Q34554084

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Purine bases at position 37 of tRNA stabilize codon-anticodon interaction in the ribosomal A site by stacking and Mg2+-dependent interactions.Ribosome formation from subunits studied by stopped-flow and rayleigh light scattering Mapping the interaction of SmpB with ribosomes by footprinting of ribosomal RNA Reorganization of an intersubunit bridge induced by disparate 16S ribosomal ambiguity mutations mimics an EF-Tu-bound state Structure of the E. coli ribosome-EF-Tu complex at <3 Å resolution by Cs-corrected cryo-EM Elongation factor G-induced structural change in helix 34 of 16S rRNA related to translocation on the ribosome.Protein folding activity of ribosomal RNA is a selective target of two unrelated antiprion drugs FRET-based identification of mRNAs undergoing translation Structural insights into the assembly of the 30S ribosomal subunit in vivo: functional role of S5 and location of the 17S rRNA precursor sequence.The roles of initiation factor 2 and guanosine triphosphate in initiation of protein synthesis Ribosome rearrangements at the onset of translational bypassing Mutations at the accommodation gate of the ribosome impair RF2-dependent translation termination.Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor.Colicin E3 cleavage of 16S rRNA impairs decoding and accelerates tRNA translocation on Escherichia coli ribosomes.Role and timing of GTP binding and hydrolysis during EF-G-dependent tRNA translocation on the ribosome Reconstitution of the human U snRNP assembly machinery reveals stepwise Sm protein organization Real-time assay for testing components of protein synthesis.Impact of methylations of m2G966/m5C967 in 16S rRNA on bacterial fitness and translation initiation.Thiostrepton inhibits the turnover but not the GTPase of elongation factor G on the ribosome.tRNA-ribosome interactions.Dynamics of translation by single ribosomes through mRNA secondary structures.Importance of tRNA interactions with 23S rRNA for peptide bond formation on the ribosome: studies with substrate analogs.Structure of ratcheted ribosomes with tRNAs in hybrid states Elongation factor G initiates translocation through a power stroke The "allosteric three-site model" of elongation cannot be confirmed in a well-defined ribosome system from Escherichia coli Low modularity of aminoacyl-tRNA substrates in polymerization by the ribosome.Solid phase synthesis and binding affinity of peptidyl transferase transition state mimics containing 2'-OH at P-site position A76.Truncated elongation factor G lacking the G domain promotes translocation of the 3' end but not of the anticodon domain of peptidyl-tRNA.Synonymous Codons Direct Cotranslational Folding toward Different Protein Conformations.Rapid peptide bond formation on isolated 50S ribosomal subunits.An uncharged amine in the transition state of the ribosomal peptidyl transfer reaction.The ribosome-bound initiation factor 2 recruits initiator tRNA to the 30S initiation complex.Dual use of GTP hydrolysis by elongation factor G on the ribosome.A quantitative kinetic scheme for 70 S translation initiation complex formation.Arginines 29 and 59 of elongation factor G are important for GTP hydrolysis or translocation on the ribosome.Codon-dependent conformational change of elongation factor Tu preceding GTP hydrolysis on the ribosome.Elongation factor Tu, a GTPase triggered by codon recognition on the ribosome: mechanism and GTP consumption.The G222D mutation in elongation factor Tu inhibits the codon-induced conformational changes leading to GTPase activation on the ribosome Exploration of the conserved A+C wobble pair within the ribosomal peptidyl transferase center using affinity purified mutant ribosomes.Fluctuations between multiple EF-G-induced chimeric tRNA states during translocation on the ribosome.

P2860

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P2860

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

http://www.wikidata.org/entity/Q34554084

description

1995 nî lūn-bûn

@nan

1995 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

1995 թվականի մարտին հրատարակված գիտական հոդված

@hy

1995年の論文

@ja

1995年論文

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1995年論文

@zh-hant

1995年論文

@zh-hk

1995年論文

@zh-mo

1995年論文

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1995年论文

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name

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

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

@en

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

@nl

type

label

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

@ast

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

@en

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

@nl

prefLabel

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

@ast

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

@en

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

@nl

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P1433

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

P1476

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

@en

P2093

Rodnina MV

http://www.w3.org/2001/XMLSchema#string

Wintermeyer W

http://www.w3.org/2001/XMLSchema#string

P2860

The role of guanosine 5'-triphosphate in polypeptide chain elongation

Selection of the mRNA translation initiation region by Escherichia coli ribosomes

Mutants of elongation factor Tu promote ribosomal frameshifting and nonsense readthrough.

How many EF-Tu molecules participate in aminoacyl-tRNA binding and peptide bond formation in Escherichia coli translation?

Towards a genetic dissection of the basis of triplet decoding, and its natural subversion: programmed reading frame shifts and hops.

Proofreading of the codon-anticodon interaction on ribosomes.

Mechanism of action of kirromycin-like antibiotics.

Properties and regulation of the GTPase activities of elongation factors Tu and G, and of initiation factor 2.

Why do two EF-Tu molecules act in the elongation cycle of protein biosynthesis?

Is there proofreading during polypeptide synthesis?

P304

1945-1949

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scholarly article

P356

10.1073/PNAS.92.6.1945

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P433

6

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P478

92

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1995-03-01T00:00:00Z

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15307434

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P698

7892205

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P932

42399

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