The catalytic domain of PKC-ε, in reciprocal PKC-δ and -ε chimeras, is responsible for conferring tumorgenicity to NIH3T3 cells, whereas both regulatory and catalytic domains of PKC-ε contribute to in vitro transformation

Oncogene

Volumn 16, Issue 1, 1998, Pages 53-60

  Wang, Qiming J ^a   Acs, Peter ^a   Goodnight, JoAnne ^a   Blumberg, Peter M ^a   Mischak, Harald ^a   Mushinski, J Frederic ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

Author keywords

Chimeric PKC; NIH3T3; PKC ; PKC ; Transformation; Tumorgenicity

Indexed keywords

CHIMERIC PROTEIN; ISOENZYME; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN KINASE C;

ANCHORAGE INDEPENDENT GROWTH; ANIMAL CELL; ARTICLE; CARCINOGENICITY; CELL DENSITY; CELL STRAIN 3T3; CONTROLLED STUDY; ENZYME STRUCTURE; FIBROBLAST; MALIGNANT TRANSFORMATION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; STRUCTURE ACTIVITY RELATION;

ANIMALIA; MUS MUSCULUS;

EID: 0032495580     PISSN: 09509232     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.onc.1201507     Document Type: Article

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