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Volumn 294, Issue 5, 2002, Pages 1109-1113

Dual regulation of phospholipase D1 by protein kinase C α in vivo

Author keywords

Adenovirus vector; G361; Melanoma cells; MeWo; Phorbol ester; Phospholipase D; Phosphorylation; Protein kinase C; Protein protein interaction

Indexed keywords

2 [1 (3 DIMETHYLAMINOPROPYL) 3 INDOLYL] 3 (3 INDOLYL)MALEIMIDE; ADENOVIRUS VECTOR; PHORBOL 13 ACETATE 12 MYRISTATE; PHOSPHOLIPASE D1; PROTEIN KINASE C ALPHA; PROTEIN KINASE C BETA; PROTEIN KINASE C INHIBITOR;

EID: 0036289708     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(02)00614-9     Document Type: Article
Times cited : (28)

References (31)
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    • Phospholipase D is associated in a phorbol ester-dependent manner with protein kinase C-α and with a 220-kDa protein which is phosphorylated on serine and threonine
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 533-537
    • Min, D.S.1    Exton, J.H.2
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    • A point mutation at the putative ATP-binding site of protein kinase Cα abolishes the kinase activity and renders it down-regulation-insensitive. A molecular link between autophosphorylation and down-regulation
    • (1990) J. Biol. Chem. , vol.265 , pp. 6296-6300
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.