Distinct eRF3 requirements suggest alternate eRF1 conformations mediate peptide release during eukaryotic translation termination. - Wikidata - wikimedia - TriplyDB

Distinct eRF3 requirements suggest alternate eRF1 conformations mediate peptide release during eukaryotic translation termination.

Distinct eRF3 requirements suggest alternate eRF1 conformations mediate peptide release during eukaryotic translation termination.

http://www.wikidata.org/entity/Q42037791

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Therapeutic suppression of premature termination codons: mechanisms and clinical considerations (review)Structural insights into eRF3 and stop codon recognition by eRF1 Structural basis for translation termination by archaeal RF1 and GTP-bound EF1 complex Structure of the mammalian ribosomal pre-termination complex associated with eRF1*eRF3*GDPNP Structural characterization of eRF1 mutants indicate a complex mechanism of stop codon recognition Translation in giant viruses: a unique mixture of bacterial and eukaryotic termination schemes.Molecular dissection of translation termination mechanism identifies two new critical regions in eRF1.Autoregulatory systems controlling translation factor expression: thermostat-like control of translational accuracy.Preparation of a highly active cell-free translation system from immature Xenopus laevis oocytes.Three distinct peptides from the N domain of translation termination factor eRF1 surround stop codon in the ribosome.Translational control from head to tail.The elongation, termination, and recycling phases of translation in eukaryotes.Suppression of premature termination codons as a therapeutic approach.Cryo-EM structure of the mammalian eukaryotic release factor eRF1-eRF3-associated termination complex.Connection between stop codon reassignment and frequent use of shifty stop frameshifting Therapeutics based on stop codon readthrough.Optimal translational termination requires C4 lysyl hydroxylation of eRF1.Mechanism of the initiation of mRNA decay: role of eRF3 family G proteins.Adenine and guanine recognition of stop codon is mediated by different N domain conformations of translation termination factor eRF1.Modifying the maker: Oxygenases target ribosome biology.SUP35 expression is enhanced in yeast containing [ISP+], a prion form of the transcriptional regulator Sfp1.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.Eukaryotic release factor 3 is required for multiple turnovers of peptide release catalysis by eukaryotic release factor 1.The role of ABCE1 in eukaryotic posttermination ribosomal recycling.Identification of eRF1 residues that play critical and complementary roles in stop codon recognition.GTP-dependent structural rearrangement of the eRF1:eRF3 complex and eRF3 sequence motifs essential for PABP binding.Genetic analysis of L123 of the tRNA-mimicking eukaryote release factor eRF1, an amino acid residue critical for discrimination of stop codons.Dual function of UPF3B in early and late translation termination.Decoding accuracy in eRF1 mutants and its correlation with pleiotropic quantitative traits in yeast.A single amino acid change of translation termination factor eRF1 switches between bipotent and omnipotent stop-codon specificity.The binding sites of class I release factor (eRF1) toward class II release factor (eRF3) in Euplotes octocarinatus.Origin of the omnipotence of eukaryotic release factor 1.An RNA decay factor wears a new coat: UPF3B modulates translation termination.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.

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P2860

Distinct eRF3 requirements suggest alternate eRF1 conformations mediate peptide release during eukaryotic translation termination.

http://www.wikidata.org/entity/Q42037791

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2008 nî lūn-bûn

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2008年の論文

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Distinct eRF3 requirements sug ...... yotic translation termination.

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Distinct eRF3 requirements sug ...... yotic translation termination.

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Distinct eRF3 requirements sug ...... yotic translation termination.

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J.MOLCEL.2008.03.020

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Distinct eRF3 requirements sug ...... yotic translation termination.

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Adam K Kallmeyer

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Andrey V Pisarev

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David M Bedwell

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

Hua Fan-Minogue

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

Joe Salas-Marco

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

Kim M Keeling

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

Ming Du

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

Sunnie R Thompson

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Tatyana V Pestova

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P2860

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

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

Terminating eukaryote translation: domain 1 of release factor eRF1 functions in stop codon recognition.

A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3.

Molecular mechanism of stop codon recognition by eRF1: a wobble hypothesis for peptide anticodons.

The molecular basis of nuclear genetic code change in ciliates.

Mimicry grasps reality in translation termination.

The early evolution of the genetic code.

Leaky termination at premature stop codons antagonizes nonsense-mediated mRNA decay in S. cerevisiae

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