A tripeptide 'anticodon' deciphers stop codons in messenger RNA.
about
Structure based hypothesis of a mitochondrial ribosome rescue mechanismA functional peptidyl-tRNA hydrolase, ICT1, has been recruited into the human mitochondrial ribosomeThe invariant uridine of stop codons contacts the conserved NIKSR loop of human eRF1 in the ribosomeInvariant amino acids essential for decoding function of polypeptide release factor eRF1.Termination of translation: interplay of mRNA, rRNAs and release factors?Bioinformatic, structural, and functional analyses support release factor-like MTRF1 as a protein able to decode nonstandard stop codons beginning with adenine in vertebrate mitochondriamtRF1a is a human mitochondrial translation release factor decoding the major termination codons UAA and UAGViable nonsense mutants for the essential gene SUP45 of Saccharomyces cerevisiaeCommon and specific amino acid residues in the prokaryotic polypeptide release factors RF1 and RF2: possible functional implicationsOrigins and Early Evolution of the tRNA MoleculeRibosome evolution: emergence of peptide synthesis machineryCrystal structures of 70S ribosomes bound to release factors RF1, RF2 and RF3Crystal structure combined with genetic analysis of the Thermus thermophilus ribosome recycling factor shows that a flexible hinge may act as a functional switchA cryo-electron microscopic study of ribosome-bound termination factor RF2Structure of the Escherichia coli ribosomal termination complex with release factor 2Release Factors 2 from Escherichia coli and Thermus thermophilus: structural, spectroscopic and microcalorimetric studiesInsights into Translational Termination from the Structure of RF2 Bound to the RibosomeCrystal structure of a translation termination complex formed with release factor RF2Structural insights into eRF3 and stop codon recognition by eRF1Omnipotent role of archaeal elongation factor 1 alpha (EF1 ) in translational elongation and termination, and quality control of protein synthesisStructural 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 eRF1Structural Basis for the Rescue of Stalled Ribosomes: Structure of YaeJ Bound to the RibosomeCrystal Structure of the 70S Ribosome Bound with the Q253P Mutant Form of Release Factor RF2Structure and dynamics in solution of the stop codon decoding N-terminal domain of the human polypeptide chain release factor eRF1Functional characterization of yeast mitochondrial release factor 1.Differential regulation and substrate preferences in two peptide transporters of Saccharomyces cerevisiae.The glutamine residue of the conserved GGQ motif in Saccharomyces cerevisiae release factor eRF1 is methylated by the product of the YDR140w gene.Mutations in the yeast mrf1 gene encoding mitochondrial release factor inhibit translation on mitochondrial ribosomes.Mapping functionally important motifs SPF and GGQ of the decoding release factor RF2 to the Escherichia coli ribosome by hydroxyl radical footprinting. Implications for macromolecular mimicry and structural changes in RF2Stop codon recognition in ciliates: Euplotes release factor does not respond to reassigned UGA codonA mechanism for stop codon recognition by the ribosome: a bioinformatic approach.Decoding apparatus for eukaryotic selenocysteine insertion.Human Cells Require Non-stop Ribosome Rescue Activity in MitochondriaThe evolution of genomic instability in the obligate endosymbionts of whitefliesRNA plasticity and selectivity applicable to therapeutics and novel biosensor developmentTerminating eukaryote translation: domain 1 of release factor eRF1 functions in stop codon recognition.A post-translational modification in the GGQ motif of RF2 from Escherichia coli stimulates termination of translation.Thermodynamic and kinetic insights into stop codon recognition by release factor 1.Diverse bacterial genomes encode an operon of two genes, one of which is an unusual class-I release factor that potentially recognizes atypical mRNA signals other than normal stop codons
P2860
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P2860
A tripeptide 'anticodon' deciphers stop codons in messenger RNA.
description
2000 nî lūn-bûn
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name
A tripeptide 'anticodon' deciphers stop codons in messenger RNA.
@en
A tripeptide 'anticodon' deciphers stop codons in messenger RNA.
@nl
type
label
A tripeptide 'anticodon' deciphers stop codons in messenger RNA.
@en
A tripeptide 'anticodon' deciphers stop codons in messenger RNA.
@nl
prefLabel
A tripeptide 'anticodon' deciphers stop codons in messenger RNA.
@en
A tripeptide 'anticodon' deciphers stop codons in messenger RNA.
@nl
P2093
P2860
P356
P1433
P1476
A tripeptide 'anticodon' deciphers stop codons in messenger RNA.
@en
P2093
P2860
P2888
P304
P356
10.1038/35001115
P407
P577
2000-02-01T00:00:00Z
P6179
1012623546