Phosphorylation regulates the interaction and complex formation between wt p53 protein and PARP-1.

@article{WsierskaGdek2003PhosphorylationRT,
  title={Phosphorylation regulates the interaction and complex formation between wt p53 protein and PARP-1.},
  author={J{\'o}zefa Węsierska-Gądek and Jacek Wojciechowski and Gerald Schmid},
  journal={Journal of cellular biochemistry},
  year={2003},
  volume={89 6},
  pages={1260-84}
}
We recently characterized the interaction between poly(ADP-ribose) polymerase-1 (PARP-1) and the product of the tumor suppressor gene p53. We investigated which domains of human PARP-1 and of human wild-type (wt) p53 were involved in this protein-protein interaction. We generated baculoviral constructs encoding full length or distinct functional domains of both proteins. Full length PARP-1 was simultaneously coexpressed in insect cells with full length wt p53 protein or its distinct truncated… CONTINUE READING
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