Towards elucidation of the role of ubiquitination in the pathogenesis of Parkinson's disease with semisynthetic ubiquitinated α-synuclein.

@article{Hejjaoui2011TowardsEO,
  title={Towards elucidation of the role of ubiquitination in the pathogenesis of Parkinson's disease with semisynthetic ubiquitinated α-synuclein.},
  author={Mirva Hejjaoui and Mahmood Haj-Yahya and K S Ajish Kumar and Ashraf Brik and Hilal A Lashuel},
  journal={Angewandte Chemie},
  year={2011},
  volume={50 2},
  pages={405-9}
}
The ubiquitination of lysine residues has emerged as an important mechanism for the regulation of a variety of cellular processes, such as cell signaling, DNA repair, and protein degradation by the 26S proteasome. Until recently, studies aimed at deciphering the effect of ubiquitination on protein function have relied primarily on biochemical approaches to reconstitute the ubiquitinated protein in vitro. As a result, progress in the field has been very much dependent on the discovery of the E2… CONTINUE READING
23 Citations
1 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 23 extracted citations

References

Publications referenced by this paper.

Characterization of a-syn monoubiquitinated at K6

  • K. S. Ajish Kumar, M. Haj-Yahya, D. Olschewski, H. A. Lashuel, A. Brik, Angew. Chem
  • TEM images of WT a-syn and T7-Ub-a-syn
  • 2009
1 Excerpt

Similar Papers

Loading similar papers…