about
Pachymic acid inhibits growth and induces apoptosis of pancreatic cancer in vitro and in vivo by targeting ER stressA cellular defense pathway regulating transcription through poly(ADP-ribosyl)ation in response to DNA damage2,3,7,8-Tetrachlorodibenzo-p-dioxin poly(ADP-ribose) polymerase (TiPARP, ARTD14) is a mono-ADP-ribosyltransferase and repressor of aryl hydrocarbon receptor transactivationFAM129B/MINERVA, a novel adherens junction-associated protein, suppresses apoptosis in HeLa cellsCooperation of the Cockayne syndrome group B protein and poly(ADP-ribose) polymerase 1 in the response to oxidative stress.Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin remodeling enzyme ALC1XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage6-thioguanine selectively kills BRCA2-defective tumors and overcomes PARP inhibitor resistancePARP1 suppresses homologous recombination events in mice in vivoPARP 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 repairPoly(ADP-ribose) polymerase (PARP-1) has a controlling role in homologous recombinationHuman 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 activityThe N. gonorrhoeae type IV pilus stimulates mechanosensitive pathways and cytoprotection through a pilT-dependent mechanism.The tumor suppressor DAL-1/4.1B and protein methylation cooperate in inducing apoptosis in MCF-7 breast cancer cells.Targeting DNA Replication Stress for Cancer TherapyRole of Biomarkers in the Development of PARP InhibitorsHomologous Recombination Deficiency: Exploiting the Fundamental Vulnerability of Ovarian CancerRepair of oxidative DNA damage and cancer: recent progress in DNA base excision repairAnaplasma phagocytophilum Ats-1 is imported into host cell mitochondria and interferes with apoptosis inductionCrystallographic and biochemical analysis of the mouse poly(ADP-ribose) glycohydrolasePARP inhibitors for BRCA1/2-mutated and sporadic ovarian cancer: current practice and future directionsUse of poly ADP-ribose polymerase [PARP] inhibitors in cancer cells bearing DDR defects: the rationale for their inclusion in the clinicPathophysiological Role of Peroxynitrite Induced DNA Damage in Human Diseases: A Special Focus on Poly(ADP-ribose) Polymerase (PARP)DNA excision repair and DNA damage-induced apoptosis are linked to Poly(ADP-ribosyl)ation but have different requirements for p53Interaction of Oct-1 and automodification domain of poly(ADP-ribose) synthetasePoly(ADP-ribose) polymerase binds with transcription enhancer factor 1 to MCAT1 elements to regulate muscle-specific transcriptionp38 activation is required upstream of potassium current enhancement and caspase cleavage in thiol oxidant-induced neuronal apoptosisEffect of nanostructured TiO₂ crystal phase on photoinduced apoptosis of breast cancer epithelial cellsAn inverse switch in DNA base excision and strand break repair contributes to melphalan resistance in multiple myeloma cellsDepletion of the 110-kilodalton isoform of poly(ADP-ribose) glycohydrolase increases sensitivity to genotoxic and endotoxic stress in miceCombinations of PARP Inhibitors with Temozolomide Drive PARP1 Trapping and Apoptosis in Ewing's SarcomaProliferating cell nuclear antigen-dependent abasic site repair in Xenopus laevis oocytes: an alternative pathway of base excision DNA repairAberrant DNA repair and DNA replication due to an inherited enzymatic defect in human DNA ligase IContribution to regulatory science and a next challenge of the Japanese Environmental Mutagen Society (JEMS)Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functionsPARP inhibition: PARP1 and beyondPoly(adenosine diphosphate-ribose) synthetase inhibitor 3-aminobenzamide alleviates cochlear dysfunction induced by transient ischemia.DNA-Dependent protein kinase is not required for efficient lentivirus integrationHydrostatic pressure induces apoptosis in the human leukaemic T-cell line Jurkat via the mitochondrial pathway.
P2860
Q21090555-596D969D-E734-4458-9080-330E17112252Q24289566-8F06F129-02BE-43D3-9E18-66FD4DFEB906Q24307446-B3A29A39-35CF-45F3-B845-1A6565846A04Q24315123-D8A0B56A-5672-4C3A-B9B7-1B264983B546Q24316039-A59650FE-00C6-4032-BCB9-DD8416A45E5FQ24321560-2C730E4E-1567-483E-A3A3-D752D34CC91FQ24522502-ECEE2BCC-D84C-41DA-83B9-1040715F982CQ24599364-9FC7E93A-323A-412F-8FE1-558785807AF0Q24632854-294AD556-6B27-430B-B45E-5D4674973537Q24653009-30861704-A3ED-4D13-A147-DD64B950748EQ24679360-F21B2D32-000F-4DDD-8BD4-3E307A6E0858Q24685242-6AE2509B-F5BB-40A2-AA9C-1728B558275BQ24793931-5B7BA0A6-E738-4B0B-B0F5-06275D387804Q24803390-CFCDF764-5EEB-4359-9D00-F0B5C2361459Q25257451-C56CBD23-4E2A-4F7F-80BC-46ECEE68F4C0Q26739923-E09EEDE3-C47C-423D-B766-1A3216137290Q26753159-8E830BA8-D0FF-495C-A771-0F0BF10CA097Q26783551-59A56C16-0B06-4FEF-B223-A2ACB704C3ACQ26822957-D8C396BC-1993-4B98-89C6-5AB114DD31A0Q27315871-3F9A8C3D-4585-4816-BD03-6CDF764E9EE2Q27681466-84D6D498-F743-436B-832C-057862A5BD2CQ28071345-BFB0134E-CB08-4C82-B8E8-9E48577C6AAEQ28071541-34AD2767-EDDB-4326-A702-7E3F82682EB1Q28080057-4A0F09AE-4013-4BC3-A1BD-6FDD2B0C61DFQ28115289-C804C227-EA2B-4BAF-AB69-B56613E472BCQ28267283-C5445530-6D3D-4865-9589-4F9A6F1F3CA8Q28291892-DB2A8D0A-0A97-482F-852A-52A7EFA4E328Q28364058-DF12F706-FC7E-4F88-A04F-C2A8B024B78FQ28389693-B5B0530F-C491-4DFC-8582-13BF9F9D1EF8Q28486021-AB79489A-8157-4F1C-A1F1-C443B47B6D62Q28508144-FB38AB38-246B-4DBE-ADBD-1BC819FC6E42Q28550512-46F37B35-E931-43AE-BF1E-82311AB3F459Q28645707-56A1FFE3-D187-437E-9B19-E4A393A930F4Q28645712-296780D5-C401-474C-8C6E-0690F5CD7AB6Q28828228-FE5F359E-4665-4F77-8B24-67CA85A8D584Q29617672-21417130-93F2-49C1-A811-DA648B88E308Q29619617-C83A9B34-3C0B-4792-A145-942DF0C560F2Q32060444-7161A4DA-4DC2-4BF8-9D9B-1F8CC9E7F936Q33181420-8F8D6468-CDC2-42F1-B3D3-A2CCFD0B1925Q33207008-62650165-063B-493C-ADDE-74F1E6394257
P2860
description
1992 nî lūn-bûn
@nan
1992 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի մարտին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Role of poly(ADP-ribose) formation in DNA repair.
@ast
Role of poly(ADP-ribose) formation in DNA repair.
@en
type
label
Role of poly(ADP-ribose) formation in DNA repair.
@ast
Role of poly(ADP-ribose) formation in DNA repair.
@en
prefLabel
Role of poly(ADP-ribose) formation in DNA repair.
@ast
Role of poly(ADP-ribose) formation in DNA repair.
@en
P356
P1433
P1476
Role of poly(ADP-ribose) formation in DNA repair.
@en
P2093
P2888
P304
P356
10.1038/356356A0
P407
P577
1992-03-01T00:00:00Z
P6179
1010557586