FUS binds the CTD of RNA polymerase II and regulates its phosphorylation at Ser2. - Wikidata - awgldk - TriplyDB

FUS binds the CTD of RNA polymerase II and regulates its phosphorylation at Ser2.

FUS binds the CTD of RNA polymerase II and regulates its phosphorylation at Ser2.

http://www.wikidata.org/entity/Q30456334

about

Altered ribostasis: RNA-protein granules in degenerative disorders Mechanisms of FUS mutations in familial amyotrophic lateral sclerosis FUS-mediated regulation of alternative RNA processing in neurons: insights from global transcriptome analysis RNA-binding proteins in neurodegeneration: Seq and you shall receive Cytoplasmic sequestration of FUS/TLS associated with ALS alters histone marks through loss of nuclear protein arginine methyltransferase 1.Early lethality and neuronal proteinopathy in mice expressing cytoplasm-targeted FUS that lacks the RNA recognition motif.Legal but lethal: functional protein aggregation at the verge of toxicity FUS Interacts with HSP60 to Promote Mitochondrial Damage Determinants of Amyloid Formation for the Yeast Termination Factor Nab3 EWS and FUS bind a subset of transcribed genes encoding proteins enriched in RNA regulatory functions RNA Polymerase II C-Terminal Domain: Tethering Transcription to Transcript and Template Promiscuous RNA binding by Polycomb repressive complex 2.RNA seeds higher-order assembly of FUS protein.FUS is sequestered in nuclear aggregates in ALS patient fibroblasts.Nucleic acid-binding specificity of human FUS protein.Mutation of the TERT promoter, switch to active chromatin, and monoallelic TERT expression in multiple cancers Phosphorylation-regulated binding of RNA polymerase II to fibrous polymers of low-complexity domains.On the computational ability of the RNA polymerase II carboxy terminal domain.Alternative polyadenylation of mRNA precursors.The RNA-binding protein ELAV regulates Hox RNA processing, expression and function within the Drosophila nervous system Multistep process of FUS aggregation in the cell cytoplasm involves RNA-dependent and RNA-independent mechanisms.Functions of FUS/TLS from DNA repair to stress response: implications for ALS.Activity-dependent FUS dysregulation disrupts synaptic homeostasis Self-assembled FUS binds active chromatin and regulates gene transcription.The RNA-binding protein fused in sarcoma (FUS) functions downstream of poly(ADP-ribose) polymerase (PARP) in response to DNA damage PARP-1 dependent recruitment of the amyotrophic lateral sclerosis-associated protein FUS/TLS to sites of oxidative DNA damage.Coupling mRNA processing with transcription in time and space.Compromised paraspeckle formation as a pathogenic factor in FUSopathies.A network of RNA and protein interactions in Fronto Temporal Dementia.Linking RNA Dysfunction and Neurodegeneration in Amyotrophic Lateral Sclerosis.FUS/TLS contributes to replication-dependent histone gene expression by interaction with U7 snRNPs and histone-specific transcription factors FUS functions in coupling transcription to splicing by mediating an interaction between RNAP II and U1 snRNP ALS mutations in TLS/FUS disrupt target gene expression.Residue-by-Residue View of In Vitro FUS Granules that Bind the C-Terminal Domain of RNA Polymerase II TDP-43 and FUS en route from the nucleus to the cytoplasm.RNA polymerase II pausing as a context-dependent reader of the genome.Chromatin deregulation in disease.Stress granules as crucibles of ALS pathogenesis.Toxic gain of function from mutant FUS protein is crucial to trigger cell autonomous motor neuron loss.Distinct and shared functions of ALS-associated proteins TDP-43, FUS and TAF15 revealed by multisystem analyses.

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P2860

FUS binds the CTD of RNA polymerase II and regulates its phosphorylation at Ser2.

http://www.wikidata.org/entity/Q30456334

description

2012 nî lūn-bûn

@nan

2012 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

FUS binds the CTD of RNA polymerase II and regulates its phosphorylation at Ser2.

@ast

FUS binds the CTD of RNA polymerase II and regulates its phosphorylation at Ser2.

@en

type

label

FUS binds the CTD of RNA polymerase II and regulates its phosphorylation at Ser2.

@ast

FUS binds the CTD of RNA polymerase II and regulates its phosphorylation at Ser2.

@en

prefLabel

FUS binds the CTD of RNA polymerase II and regulates its phosphorylation at Ser2.

@ast

FUS binds the CTD of RNA polymerase II and regulates its phosphorylation at Ser2.

@en

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P1433

Genes & Development

P1476

FUS binds the CTD of RNA polymerase II and regulates its phosphorylation at Ser2.

@en

P2093

Christopher C Ebmeier

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

Dylan J Taatjes

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

Jacob C Schwartz

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

P2860

The Cyclin K/Cdk12 complex maintains genomic stability via regulation of expression of DNA damage response genes

CDK12 is a transcription elongation-associated CTD kinase, the metazoan ortholog of yeast Ctk1

c-Myc regulates transcriptional pause release

Induced ncRNAs allosterically modify RNA-binding proteins in cis to inhibit transcription

NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation

Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis

Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6

TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia

Phosphorylation of serine 2 within the RNA polymerase II C-terminal domain couples transcription and 3' end processing

TLS/FUS (translocated in liposarcoma/fused in sarcoma) regulates target gene transcription via single-stranded DNA response elements

P304

2690-2695

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

P31

scholarly article

P356

10.1101/GAD.204602.112

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

P433

24

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

P478

26

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

P50

Joseph Heimiller

Elaine R Podell

P577

2012-12-01T00:00:00Z

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P5875

233948464

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P698

23249733

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

P921

phosphorylation

P932

3533074

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