Identification of the ADP-ribosylation sites in the PARP-1 automodification domain: analysis and implications.

@article{Tao2009IdentificationOT,
  title={Identification of the ADP-ribosylation sites in the PARP-1 automodification domain: analysis and implications.},
  author={Zhihua Tao and Peng Gao and Hung-Wen Liu},
  journal={Journal of the American Chemical Society},
  year={2009},
  volume={131 40},
  pages={14258-60}
}
Poly(ADP-ribose) polymerase-1 (PARP-1) is a multimodular (domains A, B, C, D, E, and F) nuclear protein that participates in many fundamental cellular activities. Stimulated by binding to nicked DNA, PARP-1 catalyzes poly(ADP-ribosyl)ation of the acceptor proteins and itself using NAD(+) as a substrate. Early studies suggested that domain D is likely an interface for protein-protein interaction between PARP-1 and its targets and is also the primary region for automodification. However… CONTINUE READING
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Early experiments showed that ADP-ribose is bound through an ester linkage

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Earlier studies suggested that automodification targets between 2 and 28 acceptor residues in the domain D of PARP-1 (Mendoza-Alvarez, H.; Alvarez-Gonzalez, R

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