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 Fiore
Penultimo
;
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.
Animals; Proto-Oncogene Proteins; Oncogenes; Genes; Receptor, erbB-2; Cells, Cultured; Protein-Tyrosine Kinases; Mice; Cell Transformation, Neoplastic; Genes, Regulator
Settore MED/04 - Patologia Generale
dic-1988
Article (author)
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/195700
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