Structure of the Escherichia coli ribosomal termination complex with release factor 2
about
Crystal structure of elongation factor P from Thermus thermophilus HB8Visualization of ribosome-recycling factor on the Escherichia coli 70S ribosome: functional implicationsDifferent modes of stop codon restriction by the Stylonychia and Paramecium eRF1 translation termination factorsViable 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 implicationsCrystal structures of 70S ribosomes bound to release factors RF1, RF2 and RF3Release Factors 2 from Escherichia coli and Thermus thermophilus: structural, spectroscopic and microcalorimetric studiesStructure of a UPF0150-family protein fromThermus thermophilusHB8Eukaryotic class 1 translation termination factor eRF1--the NMR structure and dynamics of the middle domain involved in triggering ribosome-dependent peptidyl-tRNA hydrolysisInsights into Translational Termination from the Structure of RF2 Bound to the RibosomeStructure of the 70S ribosome bound to release factor 2 and a substrate analog provides insights into catalysis of peptide releaseRecognition of the amber UAG stop codon by release factor RF1A paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine residue in translation elongation factor PStructure of the no-go mRNA decay complex Dom34-Hbs1 bound to a stalled 80S ribosomeSolution structure and siRNA-mediated knockdown analysis of the mitochondrial disease-related protein C12orf65The 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 RF2Polypeptide release factors and stop codon recognition in the apicoplast and mitochondrion of Plasmodium falciparumCapturing RNA-dependent pathways for cryo-EM analysis.The process of mRNA-tRNA translocationConserved loop sequence of helix 69 in Escherichia coli 23 S rRNA is involved in A-site tRNA binding and translational fidelity.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 codonstRNA mimicry in translation termination and beyond.Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine.Three distinct peptides from the N domain of translation termination factor eRF1 surround stop codon in the ribosome.Ribosomal dynamics inferred from variations in experimental measurementsMolecular mimicry: quantitative methods to study structural similarity between protein and RNAComparison of characteristics and function of translation termination signals between and within prokaryotic and eukaryotic organismsYaeJ is a novel ribosome-associated protein in Escherichia coli that can hydrolyze peptidyl-tRNA on stalled ribosomes.Pseudouridylation of helix 69 of 23S rRNA is necessary for an effective translation termination.Introduction to 3D reconstruction of macromolecules using single particle electron microscopy.Monolayer purification: a rapid method for isolating protein complexes for single-particle electron microscopy.The Affinity Grid: a pre-fabricated EM grid for monolayer purification.Mutations in conserved helix 69 of 23S rRNA of Thermus thermophilus that affect capreomycin resistance but not posttranscriptional modificationsQuantitative studies of ribosome conformational dynamics.Modulating the activity of the peptidyl transferase center of the ribosome.Fidelity at the molecular level: lessons from protein synthesis.Nucleotide modifications in three functionally important regions of the Saccharomyces cerevisiae ribosome affect translation accuracy.A structural view on the mechanism of the ribosome-catalyzed peptide bond formation.
P2860
Q24562017-27132F0B-0C53-4DC1-A5D3-227F7DDF8273Q24562642-A0FC8472-31B8-4A78-93BC-69849B572F0EQ24682497-E93DCD15-2568-45F3-8797-CAB74F22FB40Q24802715-736BDDF7-0393-4860-B160-5783BCB0579EQ24814464-08FA41C4-1473-4181-ACB0-E631BFC2E647Q26851217-D841195A-ADC1-4066-B469-1E51F4AEEE03Q27643716-1A916AE9-6D8F-4C6B-B4F1-AB54955DE54FQ27643943-ED99B667-EF0E-4B08-9D16-21A98BB24F4FQ27646860-18CD23CA-71DF-46A2-9CFB-E3F48A70DCE5Q27652801-3E85A412-49C9-4C22-AB7E-4034683B29D9Q27660905-FB30BA1A-FFFD-43BA-B93A-B120016AC709Q27662895-2D63BF32-B39F-4DF4-8494-4AC9E682EC5EQ27664126-7643B6C8-8593-4112-9E4C-95AD276AAEFCQ27668080-6B5A4996-46D1-4919-A8BF-399C079B81E7Q27681815-06E99F4F-2DBD-4FDC-940B-7375AB474E1FQ27938301-D9DE0767-4AD6-4A06-A839-065ACB7860B2Q27939290-1F22E82E-50E6-4805-BF16-A98C5424453EQ28216346-974528FD-378F-4B5A-9902-BCF22A6D7703Q30039559-B5F59D0B-54B4-4F6D-A136-476E21C81198Q30414125-3AABD634-9F0C-4662-BB98-BEE04321C5ABQ30480890-E2760064-0683-4B10-BEC1-E834723AD4DBQ33240227-605229C2-DF90-486B-846A-693738AE5333Q33257465-605ADF5C-203F-4DC5-A092-820D4F34C9FCQ33351954-1227DA22-2323-48CA-84BE-E1EF0B869A0CQ33681451-04B7471B-A5A0-4163-8965-5B6C7022A4C5Q34135153-B45AAE31-16B8-41CF-9771-67124F208AF4Q34141707-BEF7E939-A952-44FD-88E0-5DD602670B46Q34366505-7F765251-AB15-48B1-821C-6F4DD27D402CQ34538456-310DB1BC-E01D-415D-8D91-BE282FF8AB43Q34699801-AF8EBDAD-85BD-42B1-8C16-9D815144DDC3Q34717123-E9223E6A-2388-4BC7-8302-AAB129B487A0Q36262433-C574DC4D-37CD-44EC-A621-FF14D96E2D2EQ36534257-6E4D13F2-6A05-406D-AFF9-3CC8E2183729Q36930227-13BA39B6-B587-4170-9D37-6A97746274B7Q36974601-E8D4DC3F-37B0-49AE-BFFA-8D8A1C5F7BDEQ37029425-36B62232-8D59-46B0-ACE6-51D16C33690DQ37120124-5E2057B0-0613-4EBA-8FED-151ADD1522F3Q37400330-F5AF872B-FACD-426B-8773-15E7CA3E2952Q37477549-96A27B15-B78C-48E4-BB1F-09C33917FEE5Q37549187-F4BB986A-77EB-4EDF-99B8-BEE099DB6B34
P2860
Structure of the Escherichia coli ribosomal termination complex with release factor 2
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Structure of the Escherichia coli ribosomal termination complex with release factor 2
@ast
Structure of the Escherichia coli ribosomal termination complex with release factor 2
@en
Structure of the Escherichia coli ribosomal termination complex with release factor 2
@nl
type
label
Structure of the Escherichia coli ribosomal termination complex with release factor 2
@ast
Structure of the Escherichia coli ribosomal termination complex with release factor 2
@en
Structure of the Escherichia coli ribosomal termination complex with release factor 2
@nl
prefLabel
Structure of the Escherichia coli ribosomal termination complex with release factor 2
@ast
Structure of the Escherichia coli ribosomal termination complex with release factor 2
@en
Structure of the Escherichia coli ribosomal termination complex with release factor 2
@nl
P2093
P2860
P50
P356
P1433
P1476
Structure of the Escherichia coli ribosomal termination complex with release factor 2
@en
P2093
Alexander G Myasnikov
Bruno P Klaholz
Marin van Heel
P2860
P2888
P356
10.1038/NATURE01225
P407
P577
2003-01-02T00:00:00Z
P5875
P6179
1041608257