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. 1988 Dec;8(12):5570–5574. doi: 10.1128/mcb.8.12.5570

Different structural alterations upregulate in vitro tyrosine kinase activity and transforming potency of the erbB-2 gene.

O Segatto 1, C R King 1, J H Pierce 1, P P Di Fiore 1, S A Aaronson 1
PMCID: PMC365664  PMID: 2907606

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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