PARP1 ADP-ribosylates lysine residues of the core histone tails. - Wikidata - wikimedia - TriplyDB

PARP1 ADP-ribosylates lysine residues of the core histone tails.

PARP1 ADP-ribosylates lysine residues of the core histone tails.

http://www.wikidata.org/entity/Q34246667

about

Radiation-induced alterations in histone modification patterns and their potential impact on short-term radiation effects 2,3,7,8-Tetrachlorodibenzo-p-dioxin poly(ADP-ribose) polymerase (TiPARP, ARTD14) is a mono-ADP-ribosyltransferase and repressor of aryl hydrocarbon receptor transactivation A family of macrodomain proteins reverses cellular mono-ADP-ribosylation Active DNA demethylation in post-mitotic neurons: a reason for optimism Pleiotropic cellular functions of PARP1 in longevity and aging: genome maintenance meets inflammation Metabolic modulation of chromatin: implications for DNA repair and genomic integrity The role of poly(ADP-ribosyl)ation in DNA damage response and cancer chemotherapy Protein lysine acetylation by p300/CBP The zinc-finger domains of PARP1 cooperate to recognize DNA strand breaks ADP-ribosyltransferases and poly ADP-ribosylation Computer-aided Molecular Design of Compounds Targeting Histone Modifying Enzymes Electron transfer dissociation mass spectrometry in proteomics Mitochondrial health, the epigenome and healthspan Serine ADP-Ribosylation Depends on HPF1 Quantitative proteomic analysis of histone modifications Histopathological spectrum of paediatric diffuse intrinsic pontine glioma: diagnostic and therapeutic implications.Poly(ADP-ribose)polymerase-1 (PARP1) controls adipogenic gene expression and adipocyte function.Molecular Insights into Poly(ADP-ribose) Recognition and Processing.The SERTAD protein Taranis plays a role in Polycomb-mediated gene repression.Family-wide analysis of poly(ADP-ribose) polymerase activity The role of ADP-ribosylation in regulating DNA double-strand break repair PARP1 promotes nucleotide excision repair through DDB2 stabilization and recruitment of ALC1 Transition-state analysis of 2-O-acetyl-ADP-ribose hydrolysis by human macrodomain 1.Poly(ADP-ribosyl)ation acts in the DNA demethylation of mouse primordial germ cells also with DNA damage-independent roles.MacroH2A1.1 and PARP-1 cooperate to regulate transcription by promoting CBP-mediated H2B acetylation.Poly(ADP-ribose) metabolism is essential for proper nucleoprotein exchange during mouse spermiogenesis Poly(ADP-ribosyl)ation is involved in the epigenetic control of TET1 gene transcription.A comprehensive view of the epigenetic landscape. Part II: Histone post-translational modification, nucleosome level, and chromatin regulation by ncRNAs.The redox basis of epigenetic modifications: from mechanisms to functional consequences.Kinetic control of one-pot trans-splicing reactions by using a wild-type and designed split intein Breaking the histone code with quantitative mass spectrometry.PARPs and ADP-Ribosylation: 50 Years … and Counting.New PARP targets for cancer therapy Poly(ADP-Ribosyl)ation Affects Histone Acetylation and Transcription.A Review of Tandem Mass Spectrometry Characterization of Adenosine Diphosphate-Ribosylated Peptides.ARTD1 Suppresses Interleukin 6 Expression by Repressing MLL1-Dependent Histone H3 Trimethylation.Regulation of chromatin structure by poly(ADP-ribosyl)ation.Poly(ADP-ribose) polymerase 1 is a novel target to promote axonal regeneration.Crosstalk between SET7/9-dependent methylation and ARTD1-mediated ADP-ribosylation of histone H1.4.The Genomes of Three Uneven Siblings: Footprints of the Lifestyles of Three Trichoderma Species.

P2860

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P2860

PARP1 ADP-ribosylates lysine residues of the core histone tails.

http://www.wikidata.org/entity/Q34246667

description

2010 nî lūn-bûn

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2010 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2010 թվականի հունիսին հրատարակված գիտական հոդված

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2010年の論文

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2010年学术文章

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2010年学术文章

@zh-cn

2010年学术文章

@zh-hans

2010年学术文章

@zh-my

2010年学术文章

@zh-sg

2010年學術文章

@yue

name

PARP1 ADP-ribosylates lysine residues of the core histone tails.

@ast

PARP1 ADP-ribosylates lysine residues of the core histone tails.

@en

PARP1 ADP-ribosylates lysine residues of the core histone tails.

@nl

type

label

PARP1 ADP-ribosylates lysine residues of the core histone tails.

@ast

PARP1 ADP-ribosylates lysine residues of the core histone tails.

@en

PARP1 ADP-ribosylates lysine residues of the core histone tails.

@nl

prefLabel

PARP1 ADP-ribosylates lysine residues of the core histone tails.

@ast

PARP1 ADP-ribosylates lysine residues of the core histone tails.

@en

PARP1 ADP-ribosylates lysine residues of the core histone tails.

@nl

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P1433

Nucleic Acids Research

P1476

PARP1 ADP-ribosylates lysine residues of the core histone tails.

@en

P2093

Amedeo Caflisch

http://www.w3.org/2001/XMLSchema#string

Andrea Pozivil

http://www.w3.org/2001/XMLSchema#string

Bernd Roschitzki

http://www.w3.org/2001/XMLSchema#string

Danzhi Huang

http://www.w3.org/2001/XMLSchema#string

Dorothea Rutishauser

http://www.w3.org/2001/XMLSchema#string

Peter Gehrig

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Simon Messner

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P2860

Crystal structure of the nucleosome core particle at 2.8 A resolution

Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin remodeling enzyme ALC1

Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry.

Poly(ADP-ribosyl)ation directs recruitment and activation of an ATP-dependent chromatin remodeler

CHARMM: the biomolecular simulation program

Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?

Comparison of simple potential functions for simulating liquid water

Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 a resolution

A macrodomain-containing histone rearranges chromatin upon sensing PARP1 activation

Inhibitor and NAD+ binding to poly(ADP-ribose) polymerase as derived from crystal structures and homology modeling

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6350-6362

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scholarly article

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10.1093/NAR/GKQ463

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P407

P433

19

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P478

38

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P50

Michael O Hottiger

Matthias Altmeyer

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2010-06-04T00:00:00Z

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44651759

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20525793

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2965223

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