Role for 53BP1 Tudor domain recognition of p53 dimethylated at lysine 382 in DNA damage signaling. - Wikidata - awgldk - TriplyDB

Role for 53BP1 Tudor domain recognition of p53 dimethylated at lysine 382 in DNA damage signaling.

Role for 53BP1 Tudor domain recognition of p53 dimethylated at lysine 382 in DNA damage signaling.

http://www.wikidata.org/entity/Q37000240

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G9a and Glp methylate lysine 373 in the tumor suppressor p53 PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53 The functional diversity of protein lysine methylation An unexpected journey: lysine methylation across the proteome Structural Insight into p53 Recognition by the 53BP1 Tandem Tudor Domain The MBT Repeats of L3MBTL1 Link SET8-mediated p53 Methylation at Lysine 382 to Target Gene Repression Lysine methylation-dependent binding of 53BP1 to the pRb tumor suppressor p53 transactivation and the impact of mutations, cofactors and small molecules using a simplified yeast-based screening system Histone demethylase Jumonji D3 (JMJD3) as a tumor suppressor by regulating p53 protein nuclear stabilization Epigenome microarray platform for proteome-wide dissection of chromatin-signaling networks Preparation of recombinant peptides with site- and degree-specific lysine (13)C-methylation.Mutant TP53 posttranslational modifications: challenges and opportunities.Tracing the protectors path from the germ line to the genome.The TIP60 Complex Regulates Bivalent Chromatin Recognition by 53BP1 through Direct H4K20me Binding and H2AK15 Acetylation.An acetyl-methyl switch drives a conformational change in p53.Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1 Regulation of p53 function by lysine methylation.Identification of a fragment-like small molecule ligand for the methyl-lysine binding protein, 53BP1.Surf the post-translational modification network of p53 regulation G9a-mediated methylation of ERα links the PHF20/MOF histone acetyltransferase complex to hormonal gene expression.Proteomic analysis of murine Piwi proteins reveals a role for arginine methylation in specifying interaction with Tudor family members.A role for the p53 tumour suppressor in regulating the balance between homologous recombination and non-homologous end joining.Epigenetic regulation: methylation of histone and non-histone proteins.Regulation of p53--insights into a complex process.Systems-wide proteomic characterization of combinatorial post-translational modification patterns.Lysine methylation: beyond histones.Lysine methylation and the regulation of p53.Context-specific regulation of cancer epigenomes by histone and transcription factor methylation.On your histone mark, SET, methylate!Tudor: a versatile family of histone methylation 'readers'.PATZ1 Is a DNA Damage-Responsive Transcription Factor That Inhibits p53 Function.Post-translational control of transcription factors: methylation ranks highly.Structural aspects of small-molecule inhibition of methyllysine reader proteins.Biological function and regulation of histone and non-histone lysine methylation in response to DNA damage.Quantitation of DNA double-strand break resection intermediates in human cells.Beyond histones - the expanding roles of protein lysine methylation.53BP1 Integrates DNA Repair and p53-Dependent Cell Fate Decisions via Distinct Mechanisms.c-Fos-dependent miR-22 targets MDC1 and regulates DNA repair in terminally differentiated cells.Tudor-domain protein PHF20L1 reads lysine methylated retinoblastoma tumour suppressor protein.Reading chromatin signatures after DNA double-strand breaks.

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Role for 53BP1 Tudor domain recognition of p53 dimethylated at lysine 382 in DNA damage signaling.

http://www.wikidata.org/entity/Q37000240

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article científic

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articolo scientifico

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bilimsel makale

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scientific article published on 07 October 2008

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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

Role for 53BP1 Tudor domain re ...... e 382 in DNA damage signaling.

@en

Role for 53BP1 Tudor domain re ...... e 382 in DNA damage signaling.

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type

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Role for 53BP1 Tudor domain re ...... e 382 in DNA damage signaling.

@en

Role for 53BP1 Tudor domain re ...... e 382 in DNA damage signaling.

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prefLabel

Role for 53BP1 Tudor domain re ...... e 382 in DNA damage signaling.

@en

Role for 53BP1 Tudor domain re ...... e 382 in DNA damage signaling.

@nl

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Journal of Biological Chemistry

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Role for 53BP1 Tudor domain re ...... e 382 in DNA damage signaling.

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Ettore Appella

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Evelyn W Wang

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Hiroshi Yamaguchi

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Hong Wen

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Ioulia Kachirskaia

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Kan Tanoue

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Or Gozani

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Xiaobing Shi

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P2860

p53 is regulated by the lysine demethylase LSD1

Regulation of p53 activity through lysine methylation

Repression of p53 activity by Smyd2-mediated methylation

Modulation of p53 function by SET8-mediated methylation at lysine 382

ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression

Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase

Two cellular proteins that bind to wild-type but not mutant p53

Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair

Mitotic-specific methylation of histone H4 Lys 20 follows increased PR-Set7 expression and its localization to mitotic chromosomes.

Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks

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34660-34666

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scholarly article

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10.1074/JBC.M806020200

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50

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283

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2008-10-07T00:00:00Z

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