Structural consequences of disease-causing mutations in the ATRX-DNMT3-DNMT3L (ADD) domain of the chromatin-associated protein ATRX - Wikidata - wikimedia - TriplyDB

Structural consequences of disease-causing mutations in the ATRX-DNMT3-DNMT3L (ADD) domain of the chromatin-associated protein ATRX

Structural consequences of disease-causing mutations in the ATRX-DNMT3-DNMT3L (ADD) domain of the chromatin-associated protein ATRX

http://www.wikidata.org/entity/Q27646539

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The ATRX-ADD domain binds to H3 tail peptides and reads the combined methylation state of K4 and K9 Structural basis for recognition of H3K4 methylation status by the DNA methyltransferase 3A ATRX-DNMT3-DNMT3L domain Histone regulation in the CNS: basic principles of epigenetic plasticity Active DNA demethylation of the vertebrate genomes by DNA methyltransferases: deaminase, dehydroxymethylase or demethylase?Pediatric solid tumor genomics and developmental pliancy Combinatorial readout of histone H3 modifications specifies localization of ATRX to heterochromatin ATRX ADD domain links an atypical histone methylation recognition mechanism to human mental-retardation syndrome The Role of ATRX in the Alternative Lengthening of Telomeres (ALT) Phenotype ATRX interacts with H3.3 in maintaining telomere structural integrity in pluripotent embryonic stem cells PML bodies provide an important platform for the maintenance of telomeric chromatin integrity in embryonic stem cells Comparative analysis of the ATRX promoter and 5' regulatory region reveals conserved regulatory elements which are linked to roles in neurodevelopment, alpha-globin regulation and testicular function How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers ATRX tolerates activity-dependent histone H3 methyl/phos switching to maintain repetitive element silencing in neurons Prioritizing genes for X-linked diseases using population exome data.Decreased expression of GRAF1/OPHN-1-L in the X-linked alpha thalassemia mental retardation syndrome.Analysis of neonatal brain lacking ATRX or MeCP2 reveals changes in nucleosome density, CTCF binding and chromatin looping The PML-associated protein DEK regulates the balance of H3.3 loading on chromatin and is important for telomere integrity Loss of wild-type ATRX expression in somatic cell hybrids segregates with activation of Alternative Lengthening of Telomeres.The role of genetics in the establishment and maintenance of the epigenome.A phylogenetic study of SPBP and RAI1: evolutionary conservation of chromatin binding modules.Regulating the chromatin landscape: structural and mechanistic perspectives.Role of ATRX in chromatin structure and function: implications for chromosome instability and human disease α-Thalassemia, mental retardation, and myelodysplastic syndrome.Nucleosome-depleted chromatin gaps recruit assembly factors for the H3.3 histone variant.Family-wide Characterization of Histone Binding Abilities of Human CW Domain-containing Proteins Mutations in DNMT3B Modify Epigenetic Repression of the D4Z4 Repeat and the Penetrance of Facioscapulohumeral Dystrophy.PHD fingers in human diseases: disorders arising from misinterpreting epigenetic marks.Molecular coupling of DNA methylation and histone methylation.ATRX: the case of a peculiar chromatin remodeler.Genetic syndromes caused by mutations in epigenetic genes.Readout of epigenetic modifications.Regulation of human cytomegalovirus transcription in latency: beyond the major immediate-early promoter Emerging roles of ATRX in cancer.A Structural Perspective on Readout of Epigenetic Histone and DNA Methylation Marks.Conservation and diversification of polycomb repressive complex 2 (PRC2) proteins in the green lineage.Allosteric control of mammalian DNA methyltransferases - a new regulatory paradigm.Domain Structure of the Dnmt1, Dnmt3a, and Dnmt3b DNA Methyltransferases.Regulation of ICP0-null mutant herpes simplex virus type 1 infection by ND10 components ATRX and hDaxx.Human cytomegalovirus protein pp71 displaces the chromatin-associated factor ATRX from nuclear domain 10 at early stages of infection.XNP/dATRX interacts with DREF in the chromatin to regulate gene expression.

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Structural consequences of disease-causing mutations in the ATRX-DNMT3-DNMT3L (ADD) domain of the chromatin-associated protein ATRX

http://www.wikidata.org/entity/Q27646539

description

2007 nî lūn-bûn

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2007 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2007年の論文

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Structural consequences of dis ...... omatin-associated protein ATRX

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Structural consequences of dis ...... omatin-associated protein ATRX

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Structural consequences of dis ...... omatin-associated protein ATRX

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Structural consequences of dis ...... omatin-associated protein ATRX

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Structural consequences of dis ...... omatin-associated protein ATRX

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Proceedings of the National Academy of Sciences of the United States of America

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Structural consequences of dis ...... omatin-associated protein ATRX

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Anthony Argentaro

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Daniela Rhodes

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David Neuhaus

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Ji-Chun Yang

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Lynda Chapman

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Monika S Kowalczyk

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Richard J Gibbons

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P2860

Cloning, expression and chromosome locations of the human DNMT3 gene family

Localization of a putative transcriptional regulator (ATRX) at pericentromeric heterochromatin and the short arms of acrocentric chromosomes

Mutations in ATRX, encoding a SWI/SNF-like protein, cause diverse changes in the pattern of DNA methylation

Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor

Solution structure of the PHD domain from the KAP-1 corepressor: structural determinants for PHD, RING and LIM zinc-binding domains.

Mutations in a putative global transcriptional regulator cause X-linked mental retardation with alpha-thalassemia (ATR-X syndrome)

The ATRX syndrome protein forms a chromatin-remodeling complex with Daxx and localizes in promyelocytic leukemia nuclear bodies

How the human telomeric proteins TRF1 and TRF2 recognize telomeric DNA: a view from high-resolution crystal structures

Zinc fingers as protein recognition motifs: structural basis for the GATA-1/friend of GATA interaction

The solution structure of the N-terminal zinc finger of GATA-1 reveals a specific binding face for the transcriptional co-factor FOG

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