Structural basis for stop codon recognition in eukaryotes.
about
Ribosome-based quality control of mRNA and nascent peptidesRibosome-associated protein quality controlRibosomal frameshifting and transcriptional slippage: From genetic steganography and cryptography to adventitious use2.8-Å Cryo-EM Structure of the Large Ribosomal Subunit from the Eukaryotic Parasite LeishmaniaStructure of the ribosome post-recycling complex probed by chemical cross-linking and mass spectrometryStructural insights into ribosomal rescue by Dom34 and Hbs1 at near-atomic resolution.Computational Methodologies for Real-Space Structural Refinement of Large Macromolecular Complexes.Nuclear genetic codes with a different meaning of the UAG and the UAA codon.Case study on the evolution of hetero-oligomer interfaces based on the differences in paralogous proteins.Rules of UGA-N decoding by near-cognate tRNAs and analysis of readthrough on short uORFs in yeastHuman nonsense-mediated mRNA decay factor UPF2 interacts directly with eRF3 and the SURF complexAdvances in the molecular dynamics flexible fitting method for cryo-EM modeling.ABCE1 is essential for S phase progression in human cellsMolecular dynamics-based refinement and validation for sub-5 Å cryo-electron microscopy mapsRibosomal 18S rRNA base pairs with mRNA during eukaryotic translation initiationStructural Basis for Translation Termination on a Pseudouridylated Stop Codon.Decoding Mammalian Ribosome-mRNA States by Translational GTPase ComplexesEvolution of Nucleotide Punctuation Marks: From Structural to Linear Signals.Nonsense Suppression as an Approach to Treat Lysosomal Storage Diseases.Trm112, a Protein Activator of Methyltransferases Modifying Actors of the Eukaryotic Translational Apparatus.Gentamicin B1 is a minor gentamicin component with major nonsense mutation suppression activitySynonymous codon bias as a basis for novel antibiotic design: from nucleotide wobble constraint to ribosomal garrotte.Hydroxylation and translational adaptation to stress: some answers lie beyond the STOP codon.Rapid in vitro screening for the location-dependent effects of unnatural amino acids on protein expression and activity.eIF5A Functions Globally in Translation Elongation and Termination.Structures of ribosome-bound initiation factor 2 reveal the mechanism of subunit association.Flexible fitting to cryo-EM density map using ensemble molecular dynamics simulations.PABP enhances release factor recruitment and stop codon recognition during translation termination.Gctf: Real-time CTF determination and correctionRNA helicase DDX19 stabilizes ribosomal elongation and termination complexes.Dual function of UPF3B in early and late translation termination.ABCE1: A special factor that orchestrates translation at the crossroad between recycling and initiation.Nonsense mRNA suppression via nonstop decay.Atomic mutagenesis of stop codon nucleotides reveals the chemical prerequisites for release factor-mediated peptide release.Embraced by eIF3: structural and functional insights into the roles of eIF3 across the translation cycle.Directed hydroxyl radical probing reveals Upf1 binding to the 80S ribosomal E site rRNA at the L1 stalk.Aminoglycoside interactions and impacts on the eukaryotic ribosome.Structural rearrangements in mRNA upon its binding to human 80S ribosomes revealed by EPR spectroscopy.Origin of the omnipotence of eukaryotic release factor 1.Stop codon readthrough generates a C-terminally extended variant of the human vitamin D receptor with reduced calcitriol response.
P2860
Q26748589-EE134984-8A15-4D2A-8BB1-E02EC18EF78BQ26770828-AC4550A4-AA13-49E9-8563-7F517116511AQ26970809-757F5C56-0C3E-4E2A-9750-6181FF0722E8Q27715930-C12A21BE-4538-462A-8863-83A851017384Q28821599-E4AA29BF-494A-4106-98D2-BB052F4CCDC3Q30833083-A848AE2E-D850-4F04-9439-9C4D1A72E5F2Q33926329-47FDD499-AD85-4B12-B6D4-1E5981673932Q36279250-187503B4-621F-47BC-A9EC-21A0996A0BD4Q36531711-BA45A78E-F3FD-4C52-B8EA-54DBA4CA0D4BQ36566617-83D33DEA-0E47-46E0-A07E-E0F1089FBF83Q36627960-676F2B8A-5876-494C-A681-43C78A35FA45Q36844818-75AAEE24-C1D6-4527-9A2A-23690E4719BAQ36956965-AB24E9CC-15E0-40FD-8DCA-5FC06E2242ACQ37187814-ED4AB58A-0817-49BA-8EFB-F1872EF73DBFQ37208276-335D05F4-2BDA-4B6E-9D74-2E174FE4610DQ37243984-7263E8E1-DEA7-4476-A9DD-07F4FEBBF5E4Q37430049-10238583-239B-473C-94C0-7490F5920162Q37721277-2641D26D-2CC0-42CF-BC02-19861BA8768BQ37726532-2234A3BF-71A4-4F1B-A0F8-8D56B95486FBQ37729408-ECC47145-BAF7-47D5-B094-2904F9DAA11FQ37737097-7F5775E5-9373-4D4D-BAE5-AB5CEB15E7B9Q38647697-99CEA0A2-5B3D-451A-A280-F86AE01C2DC4Q38732490-E32E7E05-999C-415C-A47A-6F9C90084A16Q38842563-66804FA5-47DD-46FB-8BEA-F35EFFF5CCF9Q38845545-75C79890-F072-4990-8D46-888C676CCA91Q38847520-AC3CCCAC-844E-4BD3-97C8-302FA1E87169Q38859660-D78CA3EC-3774-44BE-BB25-FEF69A6CC7A2Q41117409-7224582D-5DE5-4958-B34F-088D1A9390F3Q41603517-61B98126-4315-4148-9580-5E9C932A6779Q41694030-639B8469-3D28-4796-A288-446685ED38B4Q42378065-26BE59CB-F782-45B9-94CC-91E4DD3545D9Q47118029-643B1B47-0E9F-4DFA-A504-D9B621574297Q47198829-334987F9-B489-45F2-B9EC-D5F5A52D6F80Q47234258-C462B41A-06CC-42FB-9590-260784E3A9BDQ47234689-F0AA3273-8B70-4200-8EC5-6F659E67D040Q47281253-6B50FC72-41A8-4E68-B1C7-E03E6E39CA08Q47326437-ABBCE0F3-9CF9-4AA3-A05E-E1FD50DD4D7CQ47384205-BB2A2476-E85F-4536-B7CF-72784DB567BFQ47408878-B7976E27-0312-4352-B92A-BC53ED457044Q47547464-91C81F14-70BD-428B-8DF6-A3427C4C397D
P2860
Structural basis for stop codon recognition in eukaryotes.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年学术文章
@wuu
2015年学术文章
@zh-cn
2015年学术文章
@zh-hans
2015年学术文章
@zh-my
2015年学术文章
@zh-sg
2015年學術文章
@yue
2015年學術文章
@zh
2015年學術文章
@zh-hant
name
Structural basis for stop codon recognition in eukaryotes.
@en
type
label
Structural basis for stop codon recognition in eukaryotes.
@en
prefLabel
Structural basis for stop codon recognition in eukaryotes.
@en
P2860
P50
P356
P1433
P1476
Structural basis for stop codon recognition in eukaryotes.
@en
P2093
Jason Murray
P2860
P2888
P304
P356
10.1038/NATURE14896
P407
P577
2015-08-05T00:00:00Z
P6179
1043322399