Opposite effects of the p52shc/p46shc and p66shc splicing isoforms on the EGF receptor-MAP kinase-fos signalling pathway.

@article{Migliaccio1997OppositeEO,
  title={Opposite effects of the p52shc/p46shc and p66shc splicing isoforms on the EGF receptor-MAP kinase-fos signalling pathway.},
  author={Enrica Migliaccio and Simonetta Mele and Anna Elisabetta Salcini and Giuliana Pelicci and K. M. Lai and Giulio Superti-Furga and Tony J. Pawson and Pier Paolo Di Fiore and Luisa Lanfrancone and Pier Giuseppe Pelicci},
  journal={The EMBO journal},
  year={1997},
  volume={16 4},
  pages={706-16}
}
Shc proteins are targets of activated tyrosine kinases and are implicated in the transmission of activation signals to Ras. The p46shc and p52shc isoforms share a C-terminal SH2 domain, a proline- and glycine-rich region (collagen homologous region 1; CH1) and a N-terminal PTB domain. We have isolated cDNAs encoding for a third Shc isoform, p66shc. The predicted amino acid sequence of p66shc overlaps that of p52shc and contains a unique N-terminal region which is also rich in glycines and… CONTINUE READING
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