The two proteins Pat1p (Mrt1p) and Spb8p interact in vivo, are required for mRNA decay, and are functionally linked to Pab1p.
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The C-terminal alpha-alpha superhelix of Pat is required for mRNA decapping in metazoaHuman Pat1b connects deadenylation with mRNA decapping and controls the assembly of processing bodiesMRM2 encodes a novel yeast mitochondrial 21S rRNA methyltransferase.A novel mRNA-decapping activity in HeLa cytoplasmic extracts is regulated by AU-rich elementsThe structural basis of Edc3- and Scd6-mediated activation of the Dcp1:Dcp2 mRNA decapping complexStructural analysis of the yeast Dhh1-Pat1 complex reveals how Dhh1 engages Pat1, Edc3 and RNA in mutually exclusive interactionsThe C-Terminal Domain from S. cerevisiae Pat1 Displays Two Conserved Regions Involved in Decapping Factor RecruitmentDecapping and decay of messenger RNA occur in cytoplasmic processing bodiesDecapping activators in Saccharomyces cerevisiae act by multiple mechanisms.Localization to, and effects of Pbp1, Pbp4, Lsm12, Dhh1, and Pab1 on stress granules in Saccharomyces cerevisiaeThe DEAD box protein Dhh1 stimulates the decapping enzyme Dcp1The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts with both the decapping and deadenylase complexes.Identification of Edc3p as an enhancer of mRNA decapping in Saccharomyces cerevisiae.The RNA polymerase II subunit Rpb4p mediates decay of a specific class of mRNAs.Yeast poly(A)-binding protein, Pab1, and PAN, a poly(A) nuclease complex recruited by Pab1, connect mRNA biogenesis to exportThe yeast POP2 gene encodes a nuclease involved in mRNA deadenylation.Sbp1p affects translational repression and decapping in Saccharomyces cerevisiae.The yeast EDC1 mRNA undergoes deadenylation-independent decapping stimulated by Not2p, Not4p, and Not5pIdentification of the Rps28 binding motif from yeast Edc3 involved in the autoregulatory feedback loop controlling RPS28B mRNA decayNovel G-protein complex whose requirement is linked to the translational status of the cell.The Rpb7p subunit of yeast RNA polymerase II plays roles in the two major cytoplasmic mRNA decay mechanisms.The enhancer of decapping proteins, Edc1p and Edc2p, bind RNA and stimulate the activity of the decapping enzyme.S. cerevisiae Vts1p induces deadenylation-dependent transcript degradation and interacts with the Ccr4p-Pop2p-Not deadenylase complex.Pat1 contributes to the RNA binding activity of the Lsm1-7-Pat1 complex.ATPase activity of the DEAD-box protein Dhh1 controls processing body formationLsm Proteins are required for normal processing and stability of ribosomal RNAsMovement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodiesMessenger RNA turnover in eukaryotes: pathways and enzymesPoly(A)-binding proteins regulate both mRNA deadenylation and decapping in yeast cytoplasmic extracts.General translational repression by activators of mRNA decappingGenomewide screen reveals a wide regulatory network for di/tripeptide utilization in Saccharomyces cerevisiae.Novel low abundance and transient RNAs in yeast revealed by tiling microarrays and ultra high-throughput sequencing are not conserved across closely related yeast speciesFission yeast Hsk1 (Cdc7) kinase is required after replication initiation for induced mutagenesis and proper response to DNA alkylation damage.mRNA decapping in yeast requires dissociation of the cap binding protein, eukaryotic translation initiation factor 4E.Analysis of recombinant yeast decapping enzyme.Crystal structure and functional analysis of DEAD-box protein Dhh1pMutations in the Saccharomyces cerevisiae LSM1 gene that affect mRNA decapping and 3' end protection.The yeast cytoplasmic LsmI/Pat1p complex protects mRNA 3' termini from partial degradation.Genetic interactions of yeast eukaryotic translation initiation factor 5A (eIF5A) reveal connections to poly(A)-binding protein and protein kinase C signalingHPat a decapping activator interacting with the miRNA effector complex.
P2860
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P2860
The two proteins Pat1p (Mrt1p) and Spb8p interact in vivo, are required for mRNA decay, and are functionally linked to Pab1p.
description
2000 nî lūn-bûn
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2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
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2000 թվականի օգոստոսին հրատարակված գիտական հոդված
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2000年の論文
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2000年学术文章
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The two proteins Pat1p (Mrt1p) ...... functionally linked to Pab1p.
@ast
The two proteins Pat1p (Mrt1p) ...... functionally linked to Pab1p.
@en
The two proteins Pat1p (Mrt1p) ...... functionally linked to Pab1p.
@nl
type
label
The two proteins Pat1p (Mrt1p) ...... functionally linked to Pab1p.
@ast
The two proteins Pat1p (Mrt1p) ...... functionally linked to Pab1p.
@en
The two proteins Pat1p (Mrt1p) ...... functionally linked to Pab1p.
@nl
prefLabel
The two proteins Pat1p (Mrt1p) ...... functionally linked to Pab1p.
@ast
The two proteins Pat1p (Mrt1p) ...... functionally linked to Pab1p.
@en
The two proteins Pat1p (Mrt1p) ...... functionally linked to Pab1p.
@nl
P2093
P2860
P3181
P1476
The two proteins Pat1p (Mrt1p) ...... functionally linked to Pab1p.
@en
P2093
P2860
P304
P3181
P356
10.1128/MCB.20.16.5939-5946.2000
P407
P577
2000-08-01T00:00:00Z