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.
Different structural alterations upregulate in vitro tyrosine kinase activity and transforming potency of the erbB-2 gene / O. Segatto, C. R. King, J. H. Pierce, P. P. Di Fiore, S. A. Aaronson. - In: MOLECULAR AND CELLULAR BIOLOGY. - ISSN 0270-7306. - 8:12(1988 Dec), pp. 5570-4-5574.
Different structural alterations upregulate in vitro tyrosine kinase activity and transforming potency of the erbB-2 gene
P. P. Di FiorePenultimo
;
1988
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.
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