Molecular cloning and characterization of a cellular phosphoprotein that interacts with a conserved C-terminal domain of adenovirus E1A involved in negative modulation of oncogenic transformation.

@article{Schaeper1995MolecularCA,
  title={Molecular cloning and characterization of a cellular phosphoprotein that interacts with a conserved C-terminal domain of adenovirus E1A involved in negative modulation of oncogenic transformation.},
  author={Ute Schaeper and Jeffrey M Boyd and Suzie Verma and Eugen Uhlmann and Thirugnana Subramanian and G. Chinnadurai},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1995},
  volume={92 23},
  pages={10467-71}
}
The adenovirus type 2/5 E1A proteins transform primary baby rat kidney (BRK) cells in cooperation with the activated Ras (T24 ras) oncoprotein. The N-terminal half of E1A (exon 1) is essential for this transformation activity. While the C-terminal half of E1A (exon 2) is dispensable, a region located between residues 225 and 238 of the 243R E1A protein negatively modulates in vitro T24 ras cooperative transformation as well as the tumorigenic potential of E1A/T24 ras-transformed cells. The same… CONTINUE READING
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