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Volumn 583, Issue 4, 2009, Pages 680-684

Regulation of the activity and expression of ERK8 by DNA damage

Author keywords

DNA damage; ERK8; MAPK; MMS

Indexed keywords

ENZYME INHIBITOR; EXTRACELLULAR SIGNAL REGULATED KINASE 8; HYDROGEN PEROXIDE; MITOGEN ACTIVATED PROTEIN KINASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROTEASOME; UNCLASSIFIED DRUG;

EID: 59849124116     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.01.011     Document Type: Article
Times cited : (30)

References (6)
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    • Hickson I., et al. Identification and characterization of a novel and specific inhibitor of the ataxia-telangiectasia mutated kinase ATM. Cancer Res. 64 (2004) 9152-9159
    • (2004) Cancer Res. , vol.64 , pp. 9152-9159
    • Hickson, I.1
  • 4
    • 17244373777 scopus 로고    scopus 로고
    • Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy
    • Farmer H., et al. Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy. Nature 434 (2005) 917-921
    • (2005) Nature , vol.434 , pp. 917-921
    • Farmer, H.1
  • 5
    • 20244389572 scopus 로고    scopus 로고
    • Phthalazinones. Part 1: The design and synthesis of a novel series of potent inhibitors of poly(ADP-ribose)polymerase
    • Loh Jr. V.M., et al. Phthalazinones. Part 1: The design and synthesis of a novel series of potent inhibitors of poly(ADP-ribose)polymerase. Bioorg. Med. Chem. Lett. 15 (2005) 2235-2238
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 2235-2238
    • Loh Jr., V.M.1
  • 6
    • 0037080675 scopus 로고    scopus 로고
    • Regulation of ATR substrate selection by Radl7-dependent loading of Rad9 complexes onto chromatin
    • Zou L., Cortez D., and Elledge S.J. Regulation of ATR substrate selection by Radl7-dependent loading of Rad9 complexes onto chromatin. Genes Dev. 16 (2002) 198-208
    • (2002) Genes Dev. , vol.16 , pp. 198-208
    • Zou, L.1    Cortez, D.2    Elledge, S.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.