Three distinct peptides from the N domain of translation termination factor eRF1 surround stop codon in the ribosome. - Wikidata - awgldk - TriplyDB

Three distinct peptides from the N domain of translation termination factor eRF1 surround stop codon in the ribosome.

Three distinct peptides from the N domain of translation termination factor eRF1 surround stop codon in the ribosome.

http://www.wikidata.org/entity/Q34135153

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Selectivity of stop codon recognition in translation termination is modulated by multiple conformations of GTS loop in eRF1 Structure and dynamics in solution of the stop codon decoding N-terminal domain of the human polypeptide chain release factor eRF1 Structural characterization of eRF1 mutants indicate a complex mechanism of stop codon recognition The mechanism of eukaryotic translation initiation: new insights and challenges Hydroxylated histidine of human ribosomal protein uL2 is involved in maintaining the local structure of 28S rRNA in the ribosomal peptidyl transferase center.The elongation, termination, and recycling phases of translation in eukaryotes.Chemical footprinting reveals conformational changes of 18S and 28S rRNAs at different steps of translation termination on the human ribosome.Adenine and guanine recognition of stop codon is mediated by different N domain conformations of translation termination factor eRF1.Hydroxylation and translational adaptation to stress: some answers lie beyond the STOP codon.Structural basis for stop codon recognition in eukaryotes.Two-step model of stop codon recognition by eukaryotic release factor eRF1 In Aspergillus nidulans the suppressors suaA and suaC code for release factors eRF1 and eRF3 and suaD codes for a glutamine tRNA.New insights into stop codon recognition by eRF1.Efficient multisite unnatural amino acid incorporation in mammalian cells via optimized pyrrolysyl tRNA synthetase/tRNA expression and engineered eRF1 Genetic analysis of L123 of the tRNA-mimicking eukaryote release factor eRF1, an amino acid residue critical for discrimination of stop codons.A central fragment of ribosomal protein S26 containing the eukaryote-specific motif YxxPKxYxK is a key component of the ribosomal binding site of mRNA region 5' of the E site codon Aminoglycoside-mediated promotion of translation readthrough occurs through a non-stochastic mechanism that competes with translation termination.Atomic mutagenesis of stop codon nucleotides reveals the chemical prerequisites for release factor-mediated peptide release.A substitution mutation in OsPELOTA confers bacterial blight resistance by activating the salicylic acid pathway.Eukaryotic translational termination efficiency is influenced by the 3' nucleotides within the ribosomal mRNA channel.Identification of amino acids responsible for stop codon recognition for polypeptide chain release factor.

P2860

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P2860

Three distinct peptides from the N domain of translation termination factor eRF1 surround stop codon in the ribosome.

http://www.wikidata.org/entity/Q34135153

description

2010 nî lūn-bûn

@nan

2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Three distinct peptides from t ...... nd stop codon in the ribosome.

@ast

Three distinct peptides from t ...... nd stop codon in the ribosome.

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Three distinct peptides from t ...... nd stop codon in the ribosome.

@nl

type

label

Three distinct peptides from t ...... nd stop codon in the ribosome.

@ast

Three distinct peptides from t ...... nd stop codon in the ribosome.

@en

Three distinct peptides from t ...... nd stop codon in the ribosome.

@nl

prefLabel

Three distinct peptides from t ...... nd stop codon in the ribosome.

@ast

Three distinct peptides from t ...... nd stop codon in the ribosome.

@en

Three distinct peptides from t ...... nd stop codon in the ribosome.

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Three distinct peptides from t ...... nd stop codon in the ribosome.

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P2093

Aliya G Ven'yaminova

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Dmitri M Graifer

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Galina G Karpova

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Konstantin N Bulygin

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

Lev L Kisselev

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Ludmila Yu Frolova

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

Petr M Kolosov

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Yulia S Khairulina

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

Yuri N Vorobjev

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

P2860

A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor

The invariant uridine of stop codons contacts the conserved NIKSR loop of human eRF1 in the ribosome

Invariant amino acids essential for decoding function of polypeptide release factor eRF1.

Termination of translation: interplay of mRNA, rRNAs and release factors?

The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis

Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1

A cryo-electron microscopic study of ribosome-bound termination factor RF2

Structure of the Escherichia coli ribosomal termination complex with release factor 2

Structure of the Mammalian 80S Ribosome at 8.7 Å Resolution

Structural basis for translation termination on the 70S ribosome

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1902-1914

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scholarly article

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10.1261/RNA.2066910

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10

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16

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2010-08-05T00:00:00Z

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20688868

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2941099

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