Invariant amino acids essential for decoding function of polypeptide release factor eRF1.
about
NMR solution structure and function of the C-terminal domain of eukaryotic class 1 polypeptide chain release factorDifferent modes of stop codon restriction by the Stylonychia and Paramecium eRF1 translation termination factorsTranslational readthrough potential of natural termination codons in eucaryotes--The impact of RNA sequenceTermination of protein synthesis in mammalian mitochondriaRelease Factors 2 from Escherichia coli and Thermus thermophilus: structural, spectroscopic and microcalorimetric studiesEukaryotic class 1 translation termination factor eRF1--the NMR structure and dynamics of the middle domain involved in triggering ribosome-dependent peptidyl-tRNA hydrolysisStructural insights into eRF3 and stop codon recognition by eRF1Structural basis for translation termination by archaeal RF1 and GTP-bound EF1 complexSelectivity of stop codon recognition in translation termination is modulated by multiple conformations of GTS loop in eRF1Structure and dynamics in solution of the stop codon decoding N-terminal domain of the human polypeptide chain release factor eRF1Structural characterization of eRF1 mutants indicate a complex mechanism of stop codon recognitionTranslation in giant viruses: a unique mixture of bacterial and eukaryotic termination schemes.tRNA mimicry in translation termination and beyond.Evolution of nonstop, no-go and nonsense-mediated mRNA decay and their termination factor-derived components.Molecular dissection of translation termination mechanism identifies two new critical regions in eRF1.Translation termination in pyrrolysine-utilizing archaeaThree distinct peptides from the N domain of translation termination factor eRF1 surround stop codon in the ribosome.On the Diversification of the Translation Apparatus across EukaryotesThe elongation, termination, and recycling phases of translation in eukaryotes.Connection between stop codon reassignment and frequent use of shifty stop frameshiftingAdenine and guanine recognition of stop codon is mediated by different N domain conformations of translation termination factor eRF1.Structural basis for stop codon recognition in eukaryotes.Two-step model of stop codon recognition by eukaryotic release factor eRF1New 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 eRF1Amino acid residue doublet propensity in the protein-RNA interface and its application to RNA interface prediction.Identification of eRF1 residues that play critical and complementary roles in stop codon recognition.Genetic analysis of L123 of the tRNA-mimicking eukaryote release factor eRF1, an amino acid residue critical for discrimination of stop codons.Termination of translation in eukaryotes is mediated by the quaternary eRF1*eRF3*GTP*Mg2+ complex. The biological roles of eRF3 and prokaryotic RF3 are profoundly distinct.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.Atomic mutagenesis of stop codon nucleotides reveals the chemical prerequisites for release factor-mediated peptide release.Origin of the omnipotence of eukaryotic release factor 1.Identification of amino acids responsible for stop codon recognition for polypeptide chain release factor.Reassigning stop codons via translation termination: How a few eukaryotes broke the dogma.Genetically Encoded Protein Phosphorylation in Mammalian Cells
P2860
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P2860
Invariant amino acids essential for decoding function of polypeptide release factor eRF1.
description
2005 nî lūn-bûn
@nan
2005 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Invariant amino acids essential for decoding function of polypeptide release factor eRF1
@nl
Invariant amino acids essential for decoding function of polypeptide release factor eRF1.
@ast
Invariant amino acids essential for decoding function of polypeptide release factor eRF1.
@en
Invariant amino acids essential for decoding function of polypeptide release factor eRF1.
@en-gb
type
label
Invariant amino acids essential for decoding function of polypeptide release factor eRF1
@nl
Invariant amino acids essential for decoding function of polypeptide release factor eRF1.
@ast
Invariant amino acids essential for decoding function of polypeptide release factor eRF1.
@en
Invariant amino acids essential for decoding function of polypeptide release factor eRF1.
@en-gb
prefLabel
Invariant amino acids essential for decoding function of polypeptide release factor eRF1
@nl
Invariant amino acids essential for decoding function of polypeptide release factor eRF1.
@ast
Invariant amino acids essential for decoding function of polypeptide release factor eRF1.
@en
Invariant amino acids essential for decoding function of polypeptide release factor eRF1.
@en-gb
P2093
P2860
P356
P1476
Invariant amino acids essential for decoding function of polypeptide release factor eRF1
@en
P2093
Alexandr Efimov
Artem Kononenko
Just Justesen
Lev Kisselev
Ludmila Frolova
Petr Kolosov
Vera Dubovaya
P2860
P304
P356
10.1093/NAR/GKI927
P407
P577
2005-11-10T00:00:00Z