Structural determinants of ubiquitin conjugation in Entamoeba histolytica.

@article{Bosch2013StructuralDO,
  title={Structural determinants of ubiquitin conjugation in Entamoeba histolytica.},
  author={Dustin E. Bosch and David P. Siderovski},
  journal={The Journal of biological chemistry},
  year={2013},
  volume={288 4},
  pages={2290-302}
}
Ubiquitination is important for numerous cellular processes in most eukaryotic organisms, including cellular proliferation, development, and protein turnover by the proteasome. The intestinal parasite Entamoeba histolytica harbors an extensive ubiquitin-proteasome system. Proteasome inhibitors are known to impair parasite proliferation and encystation, suggesting the ubiquitin-proteasome pathway as a viable therapeutic target. However, no functional studies of the E. histolytica ubiquitination… CONTINUE READING