About: PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase

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About: PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase Goto Sponge Distinct Permalink

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scientific journal article

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rdf:type	Item
description	artículu científicu espublizáu en 1999 (ast) vědecký článek publikovaný v roce 1999 (cs) наукова стаття, опублікована в червні 1999 (uk) 1999 թուականի Յունիսին հրատարակուած գիտական յօդուած (hyw) 1999 թվականի հունիսին հրատարակված գիտական հոդված (hy) научни чланак (објављен 1999/06/18) (sr) vedecký článok (publikovaný 1999/06/18) (sk) مقالة علمية (نشرت في 18-6-1999) (ar) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im Juni 1999 veröffentlichter wissenschaftlicher Artikel (de) scientific journal article (en) wetenschappelijk artikel (gepubliceerd op 1999/06/18) (nl)
publication date	wds:Q28511873-66F0503E-B594-4BA4-83FF-520915D1A1CE
publication date	1999-06-18 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28511873-D2EA039B-3F0E-4EC5-BD05-8739EAE80AD1
language of work or name	English
author name string	wds:Q28511873-17275CD0-5384-4967-9A31-DA5FCD8A5D98 wds:Q28511873-1FE7B45C-1A00-4E72-A8FF-B3BF37AE58AF wds:Q28511873-8C9EF381-E597-43E5-A092-A391FF2176DC wds:Q28511873-AF6F1611-3827-4ABC-9F87-4A693A7730C6 wds:Q28511873-B23EFAEF-5768-49C9-80FF-B86A527E431B wds:Q28511873-BC788F68-2991-4C8C-A8FD-CB4B69143EE9 wds:Q28511873-C9ACE726-9237-40E8-BBE3-3A6EF324A0F3 wds:Q28511873-DBBAA5DF-B56D-46C7-9C1A-6C243977C18B wds:Q28511873-DE6F7A0A-1CC6-4597-A93A-94EFDF903959 wds:Q28511873-F2FDD2B6-6EBE-4B8E-BE9A-2490E7EBD667
OpenCitations bibliographic resource ID	wds:Q28511873-70D194DD-A020-49E0-91EF-A8C8463C53FF
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/3006461
author name string	G. de Murcia J. Ménissier-de Murcia V. Schreiber S. Muller C. Niedergang P. Decker J. C. Amé F. Apiou T. Höger V. Rolli
OpenCitations bibliographic resource ID	3006461
rdfs:label	PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase (en) PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase (nl) PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase (ast)
skos:prefLabel	PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase (en) PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase (nl) PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase (ast)
name	PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase (en) PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase (nl) PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase (ast)
title	wds:Q28511873-370A535C-ED28-4100-8BA2-708B2518B46F
title	PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase (en)
page(s)	wds:Q28511873-397B467D-5DBC-4955-8895-7E2B86A55B8D
page(s)	17860–17868
instance of	wds:Q28511873-66F31442-06E6-4282-9BDE-DD1CDA80BBE4
instance of	scholarly article
main subject	wds:Q28511873-1E73D357-F35F-4C46-AE99-D09723CD60AD
main subject	Poly (ADP-ribose) polymerase family, member 2
PubMed ID	wds:Q28511873-35FC8449-27D0-44E4-B068-454CBC9826F8
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10364231
PubMed ID	10364231
published in	wds:Q28511873-8FC0E49D-4928-4AF9-939A-D89E22C459ED
published in	Journal of Biological Chemistry
issue	wds:Q28511873-A1DA48AE-E9D2-4E48-B467-F11C5FD7229C
volume	wds:Q28511873-12BA198A-12A5-45EA-9BCA-1C0075B4434E
issue	25
volume	274
DOI	wds:Q28511873-C58CEA51-C3EA-458D-8B66-12E130727149
DOI	http://dx.doi.org/10.1074/JBC.274.25.17860
DOI	10.1074/JBC.274.25.17860
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28511873
is cites work of	PARP-10, a novel Myc-interacting protein with poly(ADP-ribose) polymerase activity, inhibits transformation Active caspase-8 translocates into the nucleus of apoptotic cells to inactivate poly(ADP-ribose) polymerase-2 Poly(ADP-ribose)-dependent regulation of Snail1 protein stability Telomerase inhibition with a novel G-quadruplex-interactive agent, telomestatin: in vitro and in vivo studies in acute leukemia Regulation of Chromatin Structure and Gene Activity by Poly(ADP-Ribose) Polymerases Caspase-3-mediated processing of poly(ADP-ribose) glycohydrolase during apoptosis Poly(ADP-ribose)glycohydrolase is an upstream regulator of Ca2+ fluxes in oxidative cell death The ups and downs of tannins as inhibitors of poly(ADP-ribose)glycohydrolase. Poly(ADP-ribosyl)ation of p53 in vitro and in vivo modulates binding to its DNA consensus sequence Base excision repair is efficient in cells lacking poly(ADP-ribose) polymerase 1. The genes pme-1 and pme-2 encode two poly(ADP-ribose) polymerases in Caenorhabditis elegans Single molecule detection of PARP1 and PARP2 interaction with DNA strand breaks and their poly(ADP-ribosyl)ation using high-resolution AFM imaging. Comparative characterisation of poly(ADP-ribose) polymerase-1 from two mammalian species with different life span Trapping of PARP1 and PARP2 by Clinical PARP Inhibitors Feedback-regulated poly(ADP-ribosyl)ation by PARP-1 is required for rapid response to DNA damage in living cells Spatial and temporal cellular responses to single-strand breaks in human cells. A Clickable Aminooxy Probe for Monitoring Cellular ADP-Ribosylation. Poly(ADP-ribose) polymerase: the nuclear target in signal transduction and its role in brain ischemia-reperfusion injury. Identifying Direct Protein Targets of Poly-ADP-Ribose Polymerases (PARPs) Using Engineered PARP Variants-Orthogonal Nicotinamide Adenine Dinucleotide (NAD+) Analog Pairs. PARP1 is activated at telomeres upon G4 stabilization: possible target for telomere-based therapy Photoaffinity labeling of mouse fibroblast enzymes by a base excision repair intermediate. Evidence for the role of poly(ADP-ribose) polymerase-1 in DNA repair BRCA1, PARP, and 53BP1: conditional synthetic lethality and synthetic viability Misregulation of gene expression in primary fibroblasts lacking poly(ADP-ribose) polymerase Chromosomal aberrations in PARP(-/-) mice: genome stabilization in immortalized cells by reintroduction of poly(ADP-ribose) polymerase cDNA. Poly-ADP-ribose polymerase: machinery for nuclear processes The recognition and removal of cellular poly(ADP-ribose) signals. Cloning and characterization of a new member of the Nudix hydrolases from human and mouse Targeting telomeres and telomerase Poly(ADP-ribose)polymerase-1 (PARP-1) in carcinogenesis: potential role of PARP inhibitors in cancer treatment Poly(ADP-ribose) polymerase-1: what have we learned from the deficient mouse model?

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