Poly(A)-binding protein acts in translation termination via eukaryotic release factor 3 interaction and does not influence [PSI(+)] propagation.
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Amyloid-mediated sequestration of essential proteins contributes to mutant huntingtin toxicity in yeastAtaxin-2 interacts with the DEAD/H-box RNA helicase DDX6 and interferes with P-bodies and stress granulesStructural basis of ligand recognition by PABC, a highly specific peptide-binding domain found in poly(A)-binding protein and a HECT ubiquitin ligase.Molecular basis of eRF3 recognition by the MLLE domain of poly(A)-binding proteinInteractions between UPF1, eRFs, PABP and the exon junction complex suggest an integrated model for mammalian NMD pathwaysSMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate remodeling of the mRNA surveillance complex during nonsense-mediated mRNA decayA competition between stimulators and antagonists of Upf complex recruitment governs human nonsense-mediated mRNA decayTermination of translation: interplay of mRNA, rRNAs and release factors?3' end mRNA processing: molecular mechanisms and implications for health and diseaseMechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylasesPoly(A)-binding proteins: multifunctional scaffolds for the post-transcriptional control of gene expressionViable nonsense mutants for the essential gene SUP45 of Saccharomyces cerevisiaeYeast prions: structure, biology, and prion-handling systemsPrion Aggregates Are Recruited to the Insoluble Protein Deposit (IPOD) via Myosin 2-Based Vesicular TransportPoly(A)-binding protein is differentially required for translation mediated by viral internal ribosome entry sitesSolution structure of the C-terminal domain from poly(A)-binding protein inTrypanosoma cruzi: A vegetal PABC domainStructural and functional analysis of Nro1/Ett1: a protein involved in translation termination in S. cerevisiae and in O2-mediated gene control in S. pombeFine-tuning of translation termination efficiency in Saccharomyces cerevisiae involves two factors in close proximity to the exit tunnel of the ribosome.Tpa1p is part of an mRNP complex that influences translation termination, mRNA deadenylation, and mRNA turnover in Saccharomyces cerevisiae.Structural and functional insights into Saccharomyces cerevisiae Tpa1, a putative prolylhydroxylase influencing translation termination and transcription.The shuttling protein Npl3 promotes translation termination accuracy in Saccharomyces cerevisiae.A specific role for the C-terminal region of the Poly(A)-binding protein in mRNA decayTranslation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation.The DEAD-box protein Dhh1 promotes decapping by slowing ribosome movementNonsense-Mediated mRNA Decay: Degradation of Defective Transcripts Is Only Part of the StoryAttenuation of nonsense-mediated mRNA decay enhances in vivo nonsense suppressionQualitative and quantitative multiplexed proteomic analysis of complex yeast protein fractions that modulate the assembly of the yeast prion Sup35pThe major 5' determinant in stop codon read-through involves two adjacent adeninesN-terminal region of Saccharomyces cerevisiae eRF3 is essential for the functioning of the eRF1/eRF3 complex beyond translation termination.Inactivation 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.Mouse GSPT2, but not GSPT1, can substitute for yeast eRF3 in vivo.Genetic Codes with No Dedicated Stop Codon: Context-Dependent Translation TerminationThe [PSI+] prion exists as a dynamic cloud of variantsThe relationship of prions and translationPhylogenetic analysis reveals dynamic evolution of the poly(A)-binding protein gene family in plants.Interaction between the poly(A)-binding protein Pab1 and the eukaryotic release factor eRF3 regulates translation termination but not mRNA decay in Saccharomyces cerevisiaeMultiple transcripts from a 3'-UTR reporter vary in sensitivity to nonsense-mediated mRNA decay in Saccharomyces cerevisiaeNMD: At the crossroads between translation termination and ribosome recycling.An unbiased proteomics approach to identify human cytomegalovirus RNA-associated proteins.
P2860
Q21134910-1028730C-0F0E-4BC3-9571-7142DAA845E7Q24301077-5F4E1D24-68DC-4F08-BD81-C70C325C8BFCQ24302239-02C465B5-2D5A-47C9-91AF-3AC408034408Q24307891-9F98D792-37A1-4460-A15D-5F5CE51BDC8FQ24311680-44AFD704-B6D5-422B-81ED-2A2EB24E55F2Q24322423-D2848820-756D-4347-9D94-5CB74E38D788Q24336651-C0CC4CE4-7DE1-4B85-BD72-0F24CA3E3D8BQ24540309-7D9B7882-D033-4095-9D85-A1BAF2E7A6F9Q24648650-200230D7-1EDC-492E-99FC-4D747F8F1961Q24675982-44ADABE6-3C2D-42E2-8C09-325AE51B17A9Q24796373-9C5412B5-8354-4A25-8B3F-92D5BDB60B08Q24802715-6EA099A0-CBF0-4055-8838-A4382F0185A4Q27007482-7D4DA472-8325-408C-9C6A-9A30FE8B5B51Q27307839-9F5425DA-4292-48F0-9800-5A5724FA15D6Q27480995-1FC768A2-219B-47CF-86A9-F8886E12E9DCQ27641883-007A6AEB-DA94-4E2A-ADA9-98E2D7D933F8Q27667987-E7BC89D9-49DC-471B-BD09-CA9EFA46165CQ27931377-215307A6-F0AA-4AF5-BD86-7DE4A118D491Q27934115-65217E45-ECA8-4305-B977-6A508A5469A0Q27935079-86EB22CB-F17F-4127-B3E8-7B9E86E6D64CQ27935914-CF45CED8-D60E-4FD0-B357-C68D80F43862Q27936791-7AED99E1-20BC-4D9A-9494-8484102BC528Q27938398-47CE1A63-C250-4FB9-B34F-7192B2D09581Q27940178-167E78D4-9212-4848-8906-BA385CE6B357Q28082699-7E5B87B8-A84B-49EE-87DB-EBB26E33B375Q28486134-B83CA855-A2E5-42F2-A43A-DF731FC323CFQ28740450-CC31824C-F83A-41F5-A656-DEF3A673C2C2Q30749007-CB87A26A-627A-49C6-904D-44347E7F7C4CQ33260080-082D6615-A36F-4339-B108-4AB8B6BF40D2Q33294485-179196D1-DCF0-4BE5-8414-72614511B6ADQ33378990-515AB4BD-24C9-4C68-B92F-073293A41EC6Q34152266-540DD0A3-DF37-4348-AB24-FBB05191A65DQ34534392-D53BFB56-45C2-4509-BBF1-5A87FD079792Q34574937-F6D411FA-8338-48EF-B0B9-CF0030E2DDB3Q34576013-AEBA8279-63AF-4F9F-B01A-8ADF30A607DBQ34617073-3D82EB21-F09B-4900-B81F-86217D6BD307Q34761585-33F6B02E-45A7-4ADB-9A85-7CC5225332A9Q35049399-04A68D85-17A0-4858-A0AA-2D2B39195182Q35602865-ABB54F43-5E2E-4634-8569-D02AF4E6D44FQ35625050-F4D5E83C-F0B8-487C-9B63-F6DD1B60A694
P2860
Poly(A)-binding protein acts in translation termination via eukaryotic release factor 3 interaction and does not influence [PSI(+)] propagation.
description
2002 nî lūn-bûn
@nan
2002 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Poly(A)-binding protein acts i ...... nfluence [PSI(+)] propagation.
@ast
Poly(A)-binding protein acts i ...... nfluence [PSI(+)] propagation.
@en
type
label
Poly(A)-binding protein acts i ...... nfluence [PSI(+)] propagation.
@ast
Poly(A)-binding protein acts i ...... nfluence [PSI(+)] propagation.
@en
prefLabel
Poly(A)-binding protein acts i ...... nfluence [PSI(+)] propagation.
@ast
Poly(A)-binding protein acts i ...... nfluence [PSI(+)] propagation.
@en
P2093
P2860
P1476
Poly(A)-binding protein acts i ...... nfluence [PSI(+)] propagation.
@en
P2093
Anne Couturier
Denis Kiktev
Michel Philippe
Sergey Inge-Vechtomov
Svetlana Chabelskaya
P2860
P304
P356
10.1128/MCB.22.10.3301-3315.2002
P407
P577
2002-05-01T00:00:00Z