Regulation of Estrogen Receptor α by the SET7 Lysine Methyltransferase - Wikidata - wikimedia - TriplyDB

Regulation of Estrogen Receptor α by the SET7 Lysine Methyltransferase

Regulation of Estrogen Receptor α by the SET7 Lysine Methyltransferase

http://www.wikidata.org/entity/Q27650581

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ncRNA- and Pc2 methylation-dependent gene relocation between nuclear structures mediates gene activation programs Methylation of the retinoblastoma tumor suppressor by SMYD2 Lysine methylation of FOXO3 regulates oxidative stress-induced neuronal cell death Negative regulation of NF-kappaB action by Set9-mediated lysine methylation of the RelA subunit SET8 promotes epithelial-mesenchymal transition and confers TWIST dual transcriptional activities Nuclear receptors and epigenetic regulation: opportunities for nutritional targeting and disease prevention The functional diversity of protein lysine methylation Transcriptional regulation by the Set7 lysine methyltransferase Structural origins for the product specificity of SET domain protein methyltransferases Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294 The ankyrin repeat domain of Huntingtin interacting protein 14 contains a surface aromatic cage, a potential site for methyl-lysine binding SET7/9 Catalytic Mutants Reveal the Role of Active Site Water Molecules in Lysine Multiple Methylation A methylation and phosphorylation switch between an adjacent lysine and serine determines human DNMT1 stability Structural Insights for MPP8 Chromodomain Interaction with Histone H3 Lysine 9: Potential Effect of Phosphorylation on Methyl-Lysine Binding Structures of histone methyltransferase SET7/9 in complexes with adenosylmethionine derivatives Direct methylation of FXR by Set7/9, a lysine methyltransferase, regulates the expression of FXR target genes Set7 mediated Gli3 methylation plays a positive role in the activation of Sonic Hedgehog pathway in mammals Methyltransferase Set7/9 maintains transcription and euchromatin structure at islet-enriched genes Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives Systematic mapping of posttranslational modifications in human estrogen receptor-alpha with emphasis on novel phosphorylation sites New stably transfected bioluminescent cells expressing FLAG epitope-tagged estrogen receptors to study their chromatin recruitment.Protein arginine methyltransferase 6 regulates multiple aspects of gene expression.Palmitoylation: a protein S-acylation with implications for breast cancer.Estrogen receptor (ER) α mutations in breast cancer: hidden in plain sight Fluorescence-based methods for screening writers and readers of histone methyl marks.Phosphorylation of the mutant K303R estrogen receptor alpha at serine 305 affects aromatase inhibitor sensitivity Estrogen receptor mutations and changes in downstream gene expression and signaling (R)-PFI-2 is a potent and selective inhibitor of SETD7 methyltransferase activity in cells.Substrate and product specificities of SET domain methyltransferases A core chromatin remodeling factor instructs global chromatin signaling through multivalent reading of nucleosome codes.The transcriptional control of female puberty.Lysine methylation and functional modulation of androgen receptor by Set9 methyltransferase Dynamics of histone lysine methylation: structures of methyl writers and erasers SET7/9 methylation of the pluripotency factor LIN28A is a nucleolar localization mechanism that blocks let-7 biogenesis in human ESCs Selective mutations in estrogen receptor alpha D-domain alters nuclear translocation and non-estrogen response element gene regulatory mechanisms.Direct evidence for methyl group coordination by carbon-oxygen hydrogen bonds in the lysine methyltransferase SET7/9 SET7/9-dependent methylation of ARTD1 at K508 stimulates poly-ADP-ribose formation after oxidative stress.Liganded and unliganded activation of estrogen receptor and hormone replacement therapies.Regulation of p53 function by lysine methylation.Kinase consensus sequences: a breeding ground for crosstalk.

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P2860

Regulation of Estrogen Receptor α by the SET7 Lysine Methyltransferase

http://www.wikidata.org/entity/Q27650581

description

2008 nî lūn-bûn

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2008 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2008 թվականի մայիսին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Regulation of Estrogen Receptor α by the SET7 Lysine Methyltransferase

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Regulation of Estrogen Receptor α by the SET7 Lysine Methyltransferase

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Regulation of Estrogen Receptor α by the SET7 Lysine Methyltransferase

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type

label

Regulation of Estrogen Receptor α by the SET7 Lysine Methyltransferase

@ast

Regulation of Estrogen Receptor α by the SET7 Lysine Methyltransferase

@en

Regulation of Estrogen Receptor α by the SET7 Lysine Methyltransferase

@nl

prefLabel

Regulation of Estrogen Receptor α by the SET7 Lysine Methyltransferase

@ast

Regulation of Estrogen Receptor α by the SET7 Lysine Methyltransferase

@en

Regulation of Estrogen Receptor α by the SET7 Lysine Methyltransferase

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J.MOLCEL.2008.03.022

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Regulation of Estrogen Receptor α by the SET7 Lysine Methyltransferase

@en

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Da Jia

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Dipali Sharma

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Doris R Powell

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Junmin Peng

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Krithika Subramanian

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Paula M Vertino

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Priya Kapoor-Vazirani

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Robert E Collins

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Xiaodong Cheng

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P2860

Regulation of chromatin structure by site-specific histone H3 methyltransferases

p53 is regulated by the lysine demethylase LSD1

Structural basis for the methylation site specificity of SET7/9

Regulation of p53 activity through lysine methylation

LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription

Repression of p53 activity by Smyd2-mediated methylation

Identification of the MLL2 complex as a coactivator for estrogen receptor alpha

Gene-specific modulation of TAF10 function by SET9-mediated methylation

Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination

In vitro and in vivo analyses of a Phe/Tyr switch controlling product specificity of histone lysine methyltransferases

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10.1016/J.MOLCEL.2008.03.022

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30

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