The GTP-binding release factor eRF3 as a key mediator coupling translation termination to mRNA decay.
about
Binding of a novel SMG-1-Upf1-eRF1-eRF3 complex (SURF) to the exon junction complex triggers Upf1 phosphorylation and nonsense-mediated mRNA decayInteractions between UPF1, eRFs, PABP and the exon junction complex suggest an integrated model for mammalian NMD pathwaysInvolvement of human release factors eRF3a and eRF3b in translation termination and regulation of the termination complex formationHuman eukaryotic release factor 3a depletion causes cell cycle arrest at G1 phase through inhibition of the mTOR pathwayMechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylasesYeast prions: structure, biology, and prion-handling systemsStructure of yeast Dom34: a protein related to translation termination factor Erf1 and involved in No-Go decayStructural insights into eRF3 and stop codon recognition by eRF1Tpa1p is part of an mRNP complex that influences translation termination, mRNA deadenylation, and mRNA turnover in Saccharomyces cerevisiae.The zinc finger protein Ynr046w is plurifunctional and a component of the eRF1 methyltransferase in yeast.Upf1 potentially serves as a RING-related E3 ubiquitin ligase via its association with Upf3 in yeastInactivation of NMD increases viability of sup45 nonsense mutants in Saccharomyces cerevisiae.Evolution of nonstop, no-go and nonsense-mediated mRNA decay and their termination factor-derived components.The [PSI+] prion exists as a dynamic cloud of variantsInteraction between the poly(A)-binding protein Pab1 and the eukaryotic release factor eRF3 regulates translation termination but not mRNA decay in Saccharomyces cerevisiaeThe evolutionary and functional diversity of classical and lesser-known cytoplasmic and organellar translational GTPases across the tree of lifeEvidence of abundant stop codon readthrough in Drosophila and other metazoaTesting the faux-UTR model for NMD: analysis of Upf1p and Pab1p competition for binding to eRF3/Sup35p.Caenorhabditis elegans SMG-2 selectively marks mRNAs containing premature translation termination codons.Modulation of efficiency of translation termination in Saccharomyces cerevisiae.Prions are affected by evolution at two levelsIdentification and functional analysis of novel phosphorylation sites in the RNA surveillance protein Upf1.NMD: a multifaceted response to premature translational termination.RNA degradation in Saccharomyces cerevisaeMechanism of the initiation of mRNA decay: role of eRF3 family G proteins.Ribosome-associated complex and Ssb are required for translational repression induced by polylysine segments within nascent chains.GTP-dependent structural rearrangement of the eRF1:eRF3 complex and eRF3 sequence motifs essential for PABP binding.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.Defining the protein complexome of translation termination factor eRF1: Identification of four novel eRF1-containing complexes that range from 20S to 57S in size.Collaboration of tRNA modifications and elongation factor eEF1A in decoding and nonsense suppression
P2860
Q24303422-BED35C19-20A1-45D7-B7DA-E44E0662BE8EQ24311680-74255C0B-714D-412B-A55B-3585465A87D5Q24531977-97F9DE20-E4C7-4EFF-B296-997C13298E58Q24675599-72165D7E-1D54-4F37-8182-2B0D0B0080DBQ24675982-EF1E5D7C-AAB7-4771-9211-775840D94455Q27007482-3B5A3EE5-7842-4215-B7F2-D7B7C4AFDEA1Q27649495-E18AE7C3-A3D9-4C46-93A2-468E46A5D4AAQ27655386-3562C507-D09B-4362-B983-3E02155CD6EEQ27934115-D5DFD633-AD55-48A2-9644-F411BCC1D36EQ27934958-A21F9F9D-5DE0-4477-857F-90455F1E3FB2Q27938201-1A4CCEEA-1686-4009-B523-45E7D38AE523Q33294485-F8D62740-6EA3-468B-B2DD-F3ED3FDD7D4CQ33378990-33D05870-0176-4702-978C-0EA72A81BF66Q34574937-9DFF2B00-23A2-4669-8E42-8EF6FBFC5768Q34761585-079D9FCC-3719-4322-841C-F97199ADF2EDQ35127797-9CFC09F7-8E37-4019-9EC6-A5B9CA6DDF65Q35581562-ACF1F0EA-D198-4C2E-B62C-11856822A129Q35942095-0AC9DEF3-C5E2-4DA2-907A-08041B2D9036Q35950217-1AF4B879-444A-4887-B49B-7A1C45169E02Q36147322-A9D3EB12-A7B7-4794-947B-1333DCD61CB8Q36604678-0F560FC6-FFC5-42A3-8EDB-3623A7B23792Q37574287-A41A2E0E-DC04-4756-9D1A-19E7BBBE9833Q37675497-8578F325-6A5E-40F4-9716-04220EA2B644Q38025564-8E04391B-7A92-4C33-95CB-AE68449C68BFQ38042403-CBD35480-E32C-4B8A-BB0A-73AE56F0B879Q41170166-ACEA31D4-973E-44D5-BD8F-2E51762501F4Q42036963-512A26E7-C117-4821-92A2-AA85C427FB21Q42116112-B4CDADF3-19A4-445A-8A0D-920ADF78F77CQ47176446-EEB74528-FF1C-46A8-A6FB-58F98E0DC0A8Q58707914-53B7FA58-E028-40E9-8F85-9065855249BA
P2860
The GTP-binding release factor eRF3 as a key mediator coupling translation termination to mRNA decay.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh-hant
name
The GTP-binding release factor ...... ion termination to mRNA decay.
@en
The GTP-binding release factor ...... ion termination to mRNA decay.
@nl
type
label
The GTP-binding release factor ...... ion termination to mRNA decay.
@en
The GTP-binding release factor ...... ion termination to mRNA decay.
@nl
prefLabel
The GTP-binding release factor ...... ion termination to mRNA decay.
@en
The GTP-binding release factor ...... ion termination to mRNA decay.
@nl
P2093
P2860
P356
P1476
The GTP-binding release factor ...... ion termination to mRNA decay.
@en
P2093
Shin-Ichi Hoshino
Tetsuo Kobayashi
Toshiaki Katada
Yuji Funakoshi
P2860
P304
45693-45700
P356
10.1074/JBC.M405163200
P407
P577
2004-08-26T00:00:00Z