DUX4 recruits p300/CBP through its C-terminus and induces global H3K27 acetylation changes.
about
Mouse Dux is myotoxic and shares partial functional homology with its human paralog DUX4.Transcriptional Inhibitors Identified in a 160,000-Compound Small-Molecule DUX4 Viability Screen.Large family cohorts of lymphoblastoid cells provide a new cellular model for investigating facioscapulohumeral muscular dystrophy.A new mode of DNA binding distinguishes Capicua from other HMG-box factors and explains its mutation patterns in cancer.DUX4 induces a transcriptome more characteristic of a less-differentiated cell state and inhibits myogenesisRet function in muscle stem cells points to tyrosine kinase inhibitor therapy for facioscapulohumeral muscular dystrophy.HIST1H1C Regulates Interferon-β and Inhibits Influenza Virus Replication by Interacting with IRF3.Antisense Oligonucleotides Used to Target the DUX4 mRNA as Therapeutic Approaches in FaciosScapuloHumeral Muscular Dystrophy (FSHD).RIP140 in monocytes/macrophages regulates osteoclast differentiation and bone homeostasis.p53-independent DUX4 pathology in cell and animal models of facioscapulohumeral muscular dystrophy.Muscle pathology from stochastic low level DUX4 expression in an FSHD mouse model.DUX-family transcription factors regulate zygotic genome activation in placental mammals.A double-edged sword: The world according to Capicua in cancer.PAX7 target genes are globally repressed in facioscapulohumeral muscular dystrophy skeletal muscle.The DUX4 homeodomains mediate inhibition of myogenesis and are functionally exchangeable with the Pax7 homeodomain.Overexpression of the double homeodomain protein DUX4c interferes with myofibrillogenesis and induces clustering of myonuclei.Starting embryonic transcription for the first time.CIC-DUX4 Induces Small Round Cell Sarcomas Distinct from Ewing Sarcoma.Facioscapulohumeral Muscular Dystrophy.Functional domains of the FSHD-associated DUX4 protein.The pioneer factor activity of c-Myb involves recruitment of p300 and induction of histone acetylation followed by acetylation-induced chromatin dissociation.
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DUX4 recruits p300/CBP through its C-terminus and induces global H3K27 acetylation changes.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 06 March 2016
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
DUX4 recruits p300/CBP through ...... bal H3K27 acetylation changes.
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DUX4 recruits p300/CBP through ...... bal H3K27 acetylation changes.
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DUX4 recruits p300/CBP through ...... bal H3K27 acetylation changes.
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DUX4 recruits p300/CBP through ...... bal H3K27 acetylation changes.
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DUX4 recruits p300/CBP through ...... bal H3K27 acetylation changes.
@en
DUX4 recruits p300/CBP through ...... bal H3K27 acetylation changes.
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P2093
P2860
P50
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DUX4 recruits p300/CBP through ...... obal H3K27 acetylation changes
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P2093
Darko Bosnakovski
Minjee Kim
Natalie Schennum
Si Ho Choi
P2860
P304
P356
10.1093/NAR/GKW141
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P577
2016-03-06T00:00:00Z