About: Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1 Goto Sponge NotDistinct Permalink

An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

scientific article (publication date: 21 June 2002)

Attributes	Values
rdf:type	Item
description	artículu científicu espublizáu en 2002 (ast) vědecký článek publikovaný v roce 2002 (cs) наукова стаття, опублікована в червні 2002 (uk) 2002 թուականի Յունիսին հրատարակուած գիտական յօդուած (hyw) 2002 թվականի հունիսին հրատարակված գիտական հոդված (hy) vedecký článok (publikovaný 2002/06/21) (sk) wetenschappelijk artikel (gepubliceerd op 2002/06/21) (nl) مقالة علمية (نشرت في 21-6-2002) (ar) article publié dans la revue scientifique Journal of Biological Chemistry (fr) scientific article (publication date: 21 June 2002) (en) im Juni 2002 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q28214401-74982D2D-5375-4B9E-91A1-3C61C12A63BA
publication date	2002-06-21 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28214401-75B772C9-5E9E-4F36-AAD4-7A85CEF4FBFA
language of work or name	English
author name string	wds:Q28214401-3AF6E400-067D-441C-AAAF-88F9C6475853 wds:Q28214401-4A8FC3C3-3119-410E-9CE5-246649DAD00E wds:Q28214401-52289658-0C18-471E-8D49-42D9100E0E08 wds:Q28214401-6E24B686-FC48-4F07-A359-D51D1DD7E8A9 wds:Q28214401-8D0F83E7-6B71-42CC-8BE1-7A1BE64EDAC5 wds:Q28214401-FDBA735C-9F03-402B-885F-4231A9F28184
OpenCitations bibliographic resource ID	wds:Q28214401-32BC2B14-B9E4-4B1D-A22D-F74A2204F02D
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/1240989
author name string	Gilbert de Murcia Valérie Schreiber Josiane Ménissier-de Murcia Bruno Rinaldi Inès Schultz Jean-Christophe Amé
OpenCitations bibliographic resource ID	1240989
rdfs:label	Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1 (en) Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1 (nl) Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1 (ast)
skos:prefLabel	Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1 (en) Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1 (nl) Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1 (ast)
name	Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1 (en) Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1 (nl) Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1 (ast)
author	wds:Q28214401-93062E4E-0F2D-4F4E-B5A1-A9E98DD0D91E wds:Q28214401-C9C837D9-3719-4A45-869E-8FE6311985A0
author	Pascal Dollé Valérie Fraulob
title	wds:Q28214401-837E56F4-F573-42CE-9217-9353664A9126
title	Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1 (en)
page(s)	wds:Q28214401-0A3F6A73-F1DA-477E-B756-0F31E0025309
page(s)	23028-36
instance of	wds:Q28214401-FB34EE20-00BC-4E53-B10E-6E0F3DACAB36
instance of	scholarly article
main subject	wds:Q28214401-31492841-8850-435B-B63F-3BDE86940ADF wds:Q28214401-B7D2C76D-DA94-4780-B95C-939100912373
main subject	Poly (ADP-ribose) polymerase family, member 2 Poly [ADP-ribose] polymerase 1
PubMed ID	wds:Q28214401-CE30845A-193C-45B1-9994-F3573C57D557
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11948190
PubMed ID	11948190
published in	wds:Q28214401-62898941-D830-433F-AD50-F88D7604F16E
published in	Journal of Biological Chemistry
issue	wds:Q28214401-B2950269-45BC-4272-8869-F03825E59B31
volume	wds:Q28214401-713B122C-7479-4279-8207-3123F5C92F18
issue	25
volume	277
DOI	wds:Q28214401-70137A47-C378-4C74-997E-DF0CB51784E4
DOI	http://dx.doi.org/10.1074/JBC.M202390200
DOI	10.1074/JBC.M202390200
is owl:sameAs of	Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28214401
is cites work of	PARP-10, a novel Myc-interacting protein with poly(ADP-ribose) polymerase activity, inhibits transformation Complementary quantitative proteomics reveals that transcription factor AP-4 mediates E-box-dependent complex formation for transcriptional repression of HDM2 Telomerase inhibition with a novel G-quadruplex-interactive agent, telomestatin: in vitro and in vivo studies in acute leukemia PARP1 Is a TRF2-associated poly(ADP-ribose)polymerase and protects eroded telomeres On PAR with PARP: cellular stress signaling through poly(ADP-ribose) and PARP-1. 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. Identification of three critical acidic residues of poly(ADP-ribose) glycohydrolase involved in catalysis: determining the PARG catalytic domain Single molecule detection of PARP1 and PARP2 interaction with DNA strand breaks and their poly(ADP-ribosyl)ation using high-resolution AFM imaging. Translocation of XRCC1 and DNA ligase IIIalpha from centrosomes to chromosomes in response to DNA damage in mitotic human cells XRCC1 co-localizes and physically interacts with PCNA Early embryonic lethality due to targeted inactivation of DNA ligase III In situ analysis of repair processes for oxidative DNA damage in mammalian cells. Direct interaction between XRCC1 and UNG2 facilitates rapid repair of uracil in DNA by XRCC1 complexes A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage XRCC1 interacts with the p58 subunit of DNA Pol alpha-primase and may coordinate DNA repair and replication during S phase. A phase 1 safety study of veliparib combined with cisplatin and etoposide in extensive stage small cell lung cancer: A trial of the ECOG-ACRIN Cancer Research Group (E2511). Trapping of PARP1 and PARP2 by Clinical PARP Inhibitors Nuclear PARP-1 protein overexpression is associated with poor overall survival in early breast cancer Feedback-regulated poly(ADP-ribosyl)ation by PARP-1 is required for rapid response to DNA damage in living cells Physical and functional interaction between DNA ligase IIIalpha and poly(ADP-Ribose) polymerase 1 in DNA single-strand break repair Spatial and temporal cellular responses to single-strand breaks in human cells. Poly(ADP-ribose) polymerase: the nuclear target in signal transduction and its role in brain ischemia-reperfusion injury. PARP1 is activated at telomeres upon G4 stabilization: possible target for telomere-based therapy The DNA binding and catalytic domains of poly(ADP-ribose) polymerase 1 cooperate in the regulation of chromatin structure and transcription Poly(ADP-ribose)polymerase-1 (PARP-1) in carcinogenesis: potential role of PARP inhibitors in cancer treatment Conformational effects of a common codon 399 polymorphism on the BRCT1 domain of the XRCC1 protein Human RECQ1 promotes restart of replication forks reversed by DNA topoisomerase I inhibition Identification of candidate substrates for poly(ADP-ribose) polymerase-2 (PARP2) in the absence of DNA damage using high-density protein microarrays The role of poly(ADP-ribose) in the DNA damage signaling network PARP16/ARTD15 is a novel endoplasmic-reticulum-associated mono-ADP-ribosyltransferase that interacts with, and modifies karyopherin-ß1 Poly(ADP-ribose): novel functions for an old molecule

Faceted Search & Find service v1.16.117 as of May 05 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3239 as of May 5 2024, on Linux (x86_64-centos_6-linux-gnu), Single-Server Edition (378 GB total memory, 196 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software