| Literature DB >> 2907606 |
O Segatto1, C R King, J H Pierce, P P Di Fiore, S A Aaronson.
Abstract
Compared with normal erbB-2 gp185, mutant erbB-2 proteins generated by mutations either in the transmembrane domain or by NH2-terminal deletion are able to transform NIH 3T3 cells at a 10- to 100-fold greater efficiency. Mutant proteins of both classes show increased tyrosine kinase activity, suggesting that an abnormal level of receptor-associated tyrosine kinase activity is a major determinant of erbB-2 oncogenic potential.Entities:
Mesh:
Substances:
Year: 1988 PMID: 2907606 PMCID: PMC365664 DOI: 10.1128/mcb.8.12.5570-5574.1988
Source DB: PubMed Journal: Mol Cell Biol ISSN: 0270-7306 Impact factor: 4.272