XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage
about
3-Methyladenine-DNA glycosylase (MPG protein) interacts with human RAD23 proteinsThe role of poly(ADP-ribose) in the DNA damage signaling networkSmoking modifies the relationship between XRCC1 haplotypes and HPV16-negative head and neck squamous cell carcinomaFunction of BRCA1 in the DNA damage response is mediated by ADP-ribosylationHuman RECQL5 participates in the removal of endogenous DNA damagePoly(ADP-ribose)-dependent regulation of Snail1 protein stabilityOpposing roles of mitochondrial and nuclear PARP1 in the regulation of mitochondrial and nuclear DNA integrity: implications for the regulation of mitochondrial functionCooperation of the Cockayne syndrome group B protein and poly(ADP-ribose) polymerase 1 in the response to oxidative stress.PARP-1 transcriptional activity is regulated by sumoylation upon heat shockDomain specific interaction in the XRCC1-DNA polymerase beta complexMitochondrial DNA ligase III function is independent of Xrcc1.Structure of an XRCC1 BRCT domain: a new protein-protein interaction moduleXRCC1 coordinates the initial and late stages of DNA abasic site repair through protein-protein interactionsEarly embryonic lethality in PARP-1 Atm double-mutant mice suggests a functional synergy in cell proliferation during developmentA cell cycle-specific requirement for the XRCC1 BRCT II domain during mammalian DNA strand break repairTranslocation of XRCC1 and DNA ligase IIIalpha from centrosomes to chromosomes in response to DNA damage in mitotic human cellsXRCC1 co-localizes and physically interacts with PCNAFunctional Evolution of BRCT Domains from Binding DNA to ProteinPARP1 suppresses homologous recombination events in mice in vivoBRCT domains: easy as one, two, threeMolecular mechanism of DNA deadenylation by the neurological disease protein aprataxinPARP inhibition versus PARP-1 silencing: different outcomes in terms of single-strand break repair and radiation susceptibilityPhysical and functional interaction between DNA ligase IIIalpha and poly(ADP-Ribose) polymerase 1 in DNA single-strand break repairRegulation of poly(ADP-ribose) polymerase 1 activity by the phosphorylation state of the nuclear NAD biosynthetic enzyme NMN adenylyl transferase 1Genetic cooperation between the Werner syndrome protein and poly(ADP-ribose) polymerase-1 in preventing chromatid breaks, complex chromosomal rearrangements, and cancer in micePoly(ADP-ribose) polymerase (PARP-1) is not involved in DNA double-strand break recoveryHuman base excision repair enzymes apurinic/apyrimidinic endonuclease1 (APE1), DNA polymerase beta and poly(ADP-ribose) polymerase 1: interplay between strand-displacement DNA synthesis and proofreading exonuclease activityAPE1 overexpression in XRCC1-deficient cells complements the defective repair of oxidative single strand breaks but increases genomic instabilityXRCC1 is required for DNA single-strand break repair in human cells.Poly(ADP-RIBOSE) polymerase-1 (Parp-1) antagonizes topoisomerase I-dependent recombination stimulation by P53XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damageInhibition of poly (ADP-ribose) polymerase activates ATM which is required for subsequent homologous recombination repairFunctions of PARylation in DNA Damage Repair PathwaysXRCC1 and OGG1 Gene Polymorphisms and Breast Cancer: A Systematic Review of LiteratureTrial watch - inhibiting PARP enzymes for anticancer therapyRole of Biomarkers in the Development of PARP InhibitorsHomologous Recombination Deficiency: Exploiting the Fundamental Vulnerability of Ovarian CancerBeyond Breast and Ovarian Cancers: PARP Inhibitors for BRCA Mutation-Associated and BRCA-Like Solid TumorsPleiotropic cellular functions of PARP1 in longevity and aging: genome maintenance meets inflammationStructure and function of the ARH family of ADP-ribosyl-acceptor hydrolases
P2860
Q22254268-51B980B5-8790-475F-A174-AE521AC9321FQ22306473-72BC715A-49A0-400A-B2F2-937887C833C6Q23916001-7FBFA5F8-B717-4257-B756-1ABFCEFFE306Q24293084-8BEBFA24-34FA-4C87-BA49-F222A25B277FQ24298591-DD576490-EC37-4D71-B3CB-6D8E62064A35Q24303474-1EDDBA21-BC2C-4969-AB2C-85BCA1F07E98Q24306488-0B04BFCC-12D6-4D5E-BB18-919A5ABC1F0BQ24316039-A15E8E11-0620-4803-B360-7FC4D9E3F9D2Q24318561-402B46A2-D483-41EE-8598-B33B5BEF5377Q24518994-2D496915-D39E-4D53-94C5-AC44EC22C498Q24523954-BED4D3D5-AA8C-456D-8977-82D0F278444EQ24533379-2AC9C0B5-0EFD-47F5-89AF-D06657EC8143Q24535921-1D23A600-65C7-43DF-A506-9559A5C09A8EQ24551010-3E2C109B-6DE6-419C-A967-284EF4A89F5BQ24554333-670DC052-074F-4774-B537-6E40E07BA2D2Q24557436-B9024158-09F5-4B0B-B4E4-8B4B9BF05FECQ24563578-AA793B95-8A30-4E51-93E0-1E0824ED4139Q24630942-B0D0E287-CCC5-4FD5-8D68-7F12D2D215FEQ24632854-8FB4A50C-B005-4CA5-81E3-FA3A3E97A27AQ24635835-0B7785A5-6DFD-42BD-AF86-10C8CBB23F4EQ24651265-812475E5-383A-44AD-A1E0-9279FE2B9D9BQ24653009-2ABE1FC4-ACAF-4527-BFAC-0B07754B55CBQ24679360-8EAE54CF-1CD1-4401-99F3-A048BF536455Q24681295-842AEBFC-8D2C-4AB2-8C16-8E79AC16EE7CQ24684308-47B9719B-1A84-4668-A5AD-8A8386539ED1Q24793335-A384A2F0-3A47-4434-ABFD-C7D0233E68E2Q24793931-F1AB78CA-5CD8-41FC-A583-5FFBA361C3ABQ24794061-CCBEBA42-C6AF-4631-AE26-FB0A095750B6Q24796404-83E696B0-E8C8-456F-9BD8-D8495290B947Q25256778-7C5C9297-50A9-49CD-B096-2428608BF734Q25257391-D8425D0A-9DD5-49EE-AF9F-7D4AF2B3DBA5Q25257863-7F41B8FC-9179-48C2-80E1-7F9C34B13E54Q26744796-B5B0AD0D-7FC4-4016-8831-C4AF93B2B1ACQ26745671-94C0B3DA-83D9-400C-B57C-215658F67C31Q26745673-8EFCE437-D89B-4F7B-88EA-371189DDB15DQ26753159-EF97456F-A427-4E85-95AB-0BAC856F6116Q26783551-04727007-CAA8-4C50-9F99-9B88CBED58B2Q26852274-6C217A3A-2E91-4763-97B0-27E4FC829A4FQ26858894-7CE2AF76-6D71-48E9-91BA-E44232BC2E5DQ27004584-96DA1BA5-87AE-42B7-B380-90D75AEA1270
P2860
XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage
description
1998 nî lūn-bûn
@nan
1998 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
XRCC1 is specifically associat ...... activity following DNA damage
@ast
XRCC1 is specifically associat ...... activity following DNA damage
@en
XRCC1 is specifically associat ...... activity following DNA damage
@en-gb
XRCC1 is specifically associat ...... activity following DNA damage
@nl
type
label
XRCC1 is specifically associat ...... activity following DNA damage
@ast
XRCC1 is specifically associat ...... activity following DNA damage
@en
XRCC1 is specifically associat ...... activity following DNA damage
@en-gb
XRCC1 is specifically associat ...... activity following DNA damage
@nl
prefLabel
XRCC1 is specifically associat ...... activity following DNA damage
@ast
XRCC1 is specifically associat ...... activity following DNA damage
@en
XRCC1 is specifically associat ...... activity following DNA damage
@en-gb
XRCC1 is specifically associat ...... activity following DNA damage
@nl
P2093
P2860
P3181
P356
P1476
XRCC1 is specifically associat ...... activity following DNA damage
@en
P2093
C Niedergang
G de Murcia
J Menissier-de Murcia
V Schreiber
P2860
P304
P3181
P356
10.1128/MCB.18.6.3563
P407
P577
1998-06-01T00:00:00Z