Bifunctional inhibitors of the trypsin-like activity of eukaryotic proteasomes.

@article{Loidl1999BifunctionalIO,
  title={Bifunctional inhibitors of the trypsin-like activity of eukaryotic proteasomes.},
  author={G{\"u}nther Loidl and Michael Groll and Hans J{\"u}rgen Musiol and Lars Ditzel and Robert Huber and Luis Moroder},
  journal={Chemistry & biology},
  year={1999},
  volume={6 4},
  pages={197-204}
}
BACKGROUND The 20S proteasome is a multicatalytic protease complex that exhibits trypsin-like, chymotrypsin-like and post-glutamyl-peptide hydrolytic activities associated with the active sites of the beta2, beta5 and beta1 subunits, respectively. Modulation of these activities using inhibitors is essential for a better understanding of the proteasome's mechanism of action. Although there are highly selective inhibitors of the proteasome's chymotryptic activity, inhibitors of similar… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 18 extracted citations

Proteasome inhibitors: complex tools for a complex enzyme.

Current topics in microbiology and immunology • 2002
View 4 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…