The human cap-binding complex is functionally connected to the nuclear RNA exosome. - Wikidata - awgldk - TriplyDB

The human cap-binding complex is functionally connected to the nuclear RNA exosome.

The human cap-binding complex is functionally connected to the nuclear RNA exosome.

http://www.wikidata.org/entity/Q37581812

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Rrp6: Integrated roles in nuclear RNA metabolism and transcription termination Fail-safe transcription termination: Because one is never enough The Zinc-Finger Protein SOP1 Is Required for a Subset of the Nuclear Exosome Functions in Arabidopsis mRNA capping: biological functions and applications The nuclear exosome is active and important during budding yeast meiosis.The role of TREX in gene expression and disease RNA Exosome Regulates AID DNA Mutator Activity in the B Cell Genome The RNA helicases AtMTR4 and HEN2 target specific subsets of nuclear transcripts for degradation by the nuclear exosome in Arabidopsis thaliana Post-transcriptional regulation of meiotic genes by a nuclear RNA silencing complex.Tyrosine phosphorylation of RNA polymerase II CTD is associated with antisense promoter transcription and active enhancers in mammalian cells A Sub-Element in PRE enhances nuclear export of intronless mRNAs by recruiting the TREX complex via ZC3H18 Terminate and make a loop: regulation of transcriptional directionality.CstF64: cell cycle regulation and functional role in 3' end processing of replication-dependent histone mRNAs.p38MAPK/MK2-mediated phosphorylation of RBM7 regulates the human nuclear exosome targeting complex Noncoding RNA transcription targets AID to divergently transcribed loci in B cells.RBM7 subunit of the NEXT complex binds U-rich sequences and targets 3'-end extended forms of snRNAs Rapid, optimized interactomic screening The fission yeast MTREC complex targets CUTs and unspliced pre-mRNAs to the nuclear exosome.Affinity proteomics to study endogenous protein complexes: pointers, pitfalls, preferences and perspectives.An Interaction between RRP6 and SU(VAR)3-9 Targets RRP6 to Heterochromatin and Contributes to Heterochromatin Maintenance in Drosophila melanogaster Canonical Poly(A) Polymerase Activity Promotes the Decay of a Wide Variety of Mammalian Nuclear RNAs.DIS3 shapes the RNA polymerase II transcriptome in humans by degrading a variety of unwanted transcripts.DGCR8 Acts as an Adaptor for the Exosome Complex to Degrade Double-Stranded Structured RNAs.Enhancer of Rudimentary Cooperates with Conserved RNA-Processing Factors to Promote Meiotic mRNA Decay and Facultative Heterochromatin Assembly.Relationships between PROMPT and gene expression.The Nrd1-like protein Seb1 coordinates cotranscriptional 3' end processing and polyadenylation site selection.A conserved virus-induced cytoplasmic TRAMP-like complex recruits the exosome to target viral RNA for degradation.The fission yeast MTREC and EJC orthologs ensure the maturation of meiotic transcripts during meiosis.Purification and analysis of endogenous human RNA exosome complexes.Principles for RNA metabolism and alternative transcription initiation within closely spaced promoters.Attacked from All Sides: RNA Decay in Antiviral Defense.Targeting RNA for processing or destruction by the eukaryotic RNA exosome and its cofactors.Mutually Exclusive CBC-Containing Complexes Contribute to RNA Fate.Transcription termination and the control of the transcriptome: why, where and how to stop.Divergent transcription and epigenetic directionality of human promoters.Cajal bodies and snRNPs - friends with benefits.Peculiarities of Yeasts and Human Telomerase RNAs Processing.Mutagenesis of ARS2 Domains To Assess Possible Roles in Cell Cycle Progression and MicroRNA and Replication-Dependent Histone mRNA Biogenesis.Distinctive Patterns of Transcription and RNA Processing for Human lincRNAs.Structure of the RBM7-ZCCHC8 core of the NEXT complex reveals connections to splicing factors.

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The human cap-binding complex is functionally connected to the nuclear RNA exosome.

http://www.wikidata.org/entity/Q37581812

description

2013 nî lūn-bûn

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2013年の論文

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2013年学术文章

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name

The human cap-binding complex is functionally connected to the nuclear RNA exosome.

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The human cap-binding complex is functionally connected to the nuclear RNA exosome.

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type

label

The human cap-binding complex is functionally connected to the nuclear RNA exosome.

@en

The human cap-binding complex is functionally connected to the nuclear RNA exosome.

@nl

prefLabel

The human cap-binding complex is functionally connected to the nuclear RNA exosome.

@en

The human cap-binding complex is functionally connected to the nuclear RNA exosome.

@nl

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Nature Structural & Molecular Biology

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The human cap-binding complex is functionally connected to the nuclear RNA exosome.

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Aleks Schein

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Anthony Hyman

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Celine Verheggen

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Helena Storvall

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Ina Poser

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

Jens S Andersen

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

Maiken S Kristiansen

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

Marie Hallais

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

Michal Domanski

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A new yeast poly(A) polymerase complex involved in RNA quality control

Identification of the factors that interact with NCBP, an 80 kDa nuclear cap binding protein

Ars2 links the nuclear cap-binding complex to RNA interference and cell proliferation

The human core exosome interacts with differentially localized processive RNases: hDIS3 and hDIS3L

Dis3-like 1: a novel exoribonuclease associated with the human exosome

A nuclear cap binding protein complex involved in pre-mRNA splicing

Participation of the nuclear cap binding complex in pre-mRNA 3' processing

RNA exosome depletion reveals transcription upstream of active human promoters

A nuclear cap-binding complex binds Balbiani ring pre-mRNA cotranscriptionally and accompanies the ribonucleoprotein particle during nuclear export

A cap-binding protein complex mediating U snRNA export

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1367-1376

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10.1038/NSMB.2703

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12

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20

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Rickard Sandberg

Torben Heick Jensen

Jakob Bunkenborg

Edouard Bertrand

Peter Refsing Andersen

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2013-11-24T00:00:00Z

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258854893

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24270879

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3923317

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