Cell biology: Nondisjunction, aneuploidy and tetraploidy (Reply)
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Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylasesCorepressor protein CDYL functions as a molecular bridge between polycomb repressor complex 2 and repressive chromatin mark trimethylated histone lysine 27Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylationMethylation of the retinoblastoma tumor suppressor by SMYD2A phospho/methyl switch at histone H3 regulates TFIID association with mitotic chromosomes.Lysine methylation of the NF-κB subunit RelA by SETD6 couples activity of the histone methyltransferase GLP at chromatin to tonic repression of NF-κB signalingING2 controls the progression of DNA replication forks to maintain genome stabilityThe autoimmune regulator PHD finger binds to non-methylated histone H3K4 to activate gene expressionRecognition of unmodified histone H3 by the first PHD finger of bromodomain-PHD finger protein 2 provides insights into the regulation of histone acetyltransferases monocytic leukemic zinc-finger protein (MOZ) and MOZ-related factor (MORF)On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complexMOZ and MORF, two large MYSTic HATs in normal and cancer stem cellsStructural insights into a dual-specificity histone demethylase ceKDM7A from Caenorhabditis elegansThe MBT Repeats of L3MBTL1 Link SET8-mediated p53 Methylation at Lysine 382 to Target Gene RepressionPlant Homeodomain (PHD) Fingers of CHD4 Are Histone H3-binding Modules with Preference for Unmodified H3K4 and Methylated H3K9ATRX ADD domain links an atypical histone methylation recognition mechanism to human mental-retardation syndromeStructure of the 30-kDa Sin3-associated Protein (SAP30) in Complex with the Mammalian Sin3A Corepressor and Its Role in Nucleic Acid BindingStructural basis for site-specific reading of unmodified R2 of histone H3 tail by UHRF1 PHD fingerStructure of Human SMYD2 Protein Reveals the Basis of p53 Tumor Suppressor MethylationLysine-specific demethylase 1 as a potential therapeutic targetHow chromatin-binding modules interpret histone modifications: lessons from professional pocket pickersThrombospondin-1 is a transcriptional repression target of PRMT6.ROW1 maintains quiescent centre identity by confining WOX5 expression to specific cells.Histone variant H2A.Z regulates centromere silencing and chromosome segregation in fission yeastThe fission yeast inhibitor of growth (ING) protein Png1p functions in response to DNA damageDrosophila SIN3 isoforms interact with distinct proteins and have unique biological functions.Activity of a C-terminal plant homeodomain (PHD) of Msc1 is essential for function.Identification and characterization of two novel JARID1C mutations: suggestion of an emerging genotype-phenotype correlationThe novel function of JADE1S in cytokinesis of epithelial cells.Analytical tools and current challenges in the modern era of neuroepigenomicsEpigenetic regulation of Atrophin1 by lysine-specific demethylase 1 is required for cortical progenitor maintenanceEpigenetic basis of opiate suppression of Bdnf gene expression in the ventral tegmental areaLincRNA-p21 acts as a mediator of ING1b-induced apoptosis.Histone tails regulate DNA methylation by allosterically activating de novo methyltransferase.PHRF1 promotes genome integrity by modulating non-homologous end-joining.R loops regulate promoter-proximal chromatin architecture and cellular differentiation.The vitamin D receptor as a therapeutic target.The MYST family of histone acetyltransferases and their intimate links to cancer.Structure and acetyl-lysine recognition of the bromodomain.Nuclear phosphatidylinositol-5-phosphate regulates ING2 stability at discrete chromatin targets in response to DNA damage.The vitamin D receptor in cancer.
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Cell biology: Nondisjunction, aneuploidy and tetraploidy (Reply)
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article publié dans la revue scientifique Nature
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scientific article published in Nature
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wetenschappelijk artikel
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наукова стаття, опублікована в Nature в серпні 2006
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name
Cell biology: Nondisjunction, aneuploidy and tetraploidy (Reply)
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Cell biology: Nondisjunction, aneuploidy and tetraploidy (Reply)
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Cell biology: Nondisjunction, aneuploidy and tetraploidy (Reply)
@en
Cell biology: Nondisjunction, aneuploidy and tetraploidy (Reply)
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Cell biology: Nondisjunction, aneuploidy and tetraploidy (Reply)
@en
Cell biology: Nondisjunction, aneuploidy and tetraploidy (Reply)
@nl
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Cell biology: Nondisjunction, aneuploidy and tetraploidy (Reply)
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Qinghua Shi
Randall W. King
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10.1038/NATURE05140
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2006-08-16T00:00:00Z
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1019775905