Poly(A) nuclease interacts with the C-terminal domain of polyadenylate-binding protein domain from poly(A)-binding protein - Test2 - elhamkhani - TriplyDB

Poly(A) nuclease interacts with the C-terminal domain of polyadenylate-binding protein domain from poly(A)-binding protein

Poly(A) nuclease interacts with the C-terminal domain of polyadenylate-binding protein domain from poly(A)-binding protein

http://www.wikidata.org/entity/Q24314646

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miRNA repression involves GW182-mediated recruitment of CCR4-NOT through conserved W-containing motifs miRNA-mediated deadenylation is orchestrated by GW182 through two conserved motifs that interact with CCR4-NOT Structural basis of binding of P-body-associated proteins GW182 and ataxin-2 by the Mlle domain of poly(A)-binding protein The interactions of GW182 proteins with PABP and deadenylases are required for both translational repression and degradation of miRNA targets Molecular basis of eRF3 recognition by the MLLE domain of poly(A)-binding protein Regulation of the fructose transporter GLUT5 in health and disease Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases The panorama of miRNA-mediated mechanisms in mammalian cells The role of mammalian poly(A)-binding proteins in co-ordinating mRNA turnover Heterogeneity and complexity within the nuclease module of the Ccr4-Not complex La-Related Protein 4 Binds Poly(A), Interacts with the Poly(A)-Binding Protein MLLE Domain via a Variant PAM2w Motif, and Can Promote mRNA Stability Structural basis for Pan3 binding to Pan2 and its function in mRNA recruitment and deadenylation An asymmetric PAN3 dimer recruits a single PAN2 exonuclease to mediate mRNA deadenylation and decay The structure of the Pan2-Pan3 core complex reveals cross-talk between deadenylase and pseudokinase Deadenylation is prerequisite for P-body formation and mRNA decay in mammalian cells Poliovirus-mediated disruption of cytoplasmic processing bodies Insights into the structure and architecture of the CCR4-NOT complex Functional characterization of three leishmania poly(a) binding protein homologues with distinct binding properties to RNA and protein partners.Nuclear import of cytoplasmic poly(A) binding protein restricts gene expression via hyperadenylation and nuclear retention of mRNA.The complexity of miRNA-mediated repression Interaction between the poly(A)-binding protein Pab1 and the eukaryotic release factor eRF3 regulates translation termination but not mRNA decay in Saccharomyces cerevisiae Nuclear localization of cytoplasmic poly(A)-binding protein upon rotavirus infection involves the interaction of NSP3 with eIF4G and RoXaN.Mammalian hyperplastic discs homolog EDD regulates miRNA-mediated gene silencing Unraveling regulation and new components of human P-bodies through a protein interaction framework and experimental validation The multifunctional poly(A)-binding protein (PABP) 1 is subject to extensive dynamic post-translational modification, which molecular modelling suggests plays an important role in co-ordinating its activities.The Caenorhabditis elegans GW182 protein AIN-1 interacts with PAB-1 and subunits of the PAN2-PAN3 and CCR4-NOT deadenylase complexes.Biological role of the two overlapping poly(A)-binding protein interacting motifs 2 (PAM2) of eukaryotic releasing factor eRF3 in mRNA decay.A molecular link between miRISCs and deadenylases provides new insight into the mechanism of gene silencing by microRNAs.BTG2 bridges PABPC1 RNA-binding domains and CAF1 deadenylase to control cell proliferation Studies on human eRF3-PABP interaction reveal the influence of eRF3a N-terminal glycin repeat on eRF3-PABP binding affinity and the lower affinity of eRF3a 12-GGC allele involved in cancer susceptibility.The role of deadenylation in the degradation of unstable mRNAs in trypanosomes.Mechanism of the initiation of mRNA decay: role of eRF3 family G proteins.Poly(A)-specific ribonuclease (PARN): an allosterically regulated, processive and mRNA cap-interacting deadenylase.mRNA deadenylation by Pan2-Pan3.Analysis of mRNA deadenylation by multi-protein complexes.Deadenylation-a piece of PANcake.Mass spectrometric identification of proteins that interact through specific domains of the poly(A) binding protein.Harnessing short poly(A)-binding protein-interacting peptides for the suppression of nonsense-mediated mRNA decay.Short poly(A) tails are a conserved feature of highly expressed genes.Characterization of the multimeric structure of poly(A)-binding protein on a poly(A) tail.

P2860

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P2860

Poly(A) nuclease interacts with the C-terminal domain of polyadenylate-binding protein domain from poly(A)-binding protein

http://www.wikidata.org/entity/Q24314646

description

2007 nî lūn-bûn

@nan

2007 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

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Poly(A) nuclease interacts wit ...... n from poly(A)-binding protein

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Poly(A) nuclease interacts wit ...... n from poly(A)-binding protein

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Poly(A) nuclease interacts wit ...... n from poly(A)-binding protein

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P1433

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P1476

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P2860

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P356

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P407

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P433

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P478

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P577

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P698

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P356

P1433

Journal of Biological Chemistry

P1476

Poly(A) nuclease interacts wit ...... n from poly(A)-binding protein

@en

P2093

Ann-Bin Shyu

http://www.w3.org/2001/XMLSchema#string

David A Mangus

http://www.w3.org/2001/XMLSchema#string

Jeanne-Marie Palermino

http://www.w3.org/2001/XMLSchema#string

Nadeem Siddiqui

http://www.w3.org/2001/XMLSchema#string

Tsung-Cheng Chang

http://www.w3.org/2001/XMLSchema#string

P2860

Translational repression by a novel partner of human poly(A) binding protein, Paip2

Paip1 interacts with poly(A) binding protein through two independent binding motifs

Identification of a human cytoplasmic poly(A) nuclease complex stimulated by poly(A)-binding protein

UNR, a new partner of poly(A)-binding protein, plays a key role in translationally coupled mRNA turnover mediated by the c-fos major coding-region determinant

Structural basis of ligand recognition by PABC, a highly specific peptide-binding domain found in poly(A)-binding protein and a HECT ubiquitin ligase.

The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes.

The human poly(A)-binding protein 1 shuttles between the nucleus and the cytoplasm

An integrative approach to gain insights into the cellular function of human ataxin-2

Mammalian poly(A)-binding protein is a eukaryotic translation initiation factor, which acts via multiple mechanisms

Cap-dependent deadenylation of mRNA

P304

25067-75

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P31

scholarly article

P356

10.1074/JBC.M701256200

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P407

P433

34

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P478

282

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P50

P577

2007-08-24T00:00:00Z

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P698

17595167

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