Lack of proteasome active site allostery as revealed by subunit-specific inhibitors.

@article{Myung2001LackOP,
  title={Lack of proteasome active site allostery as revealed by subunit-specific inhibitors.},
  author={Jayhyuk Myung and Kyung Bo Kim and Kristina Lindsten and Nico P Dantuma and Craig M Crews},
  journal={Molecular cell},
  year={2001},
  volume={7 2},
  pages={411-20}
}
The chymotrypsin-like (CT-L) activity of the proteasome is downregulated by substrates of the peptidyl-glutamyl peptide hydrolyzing (PGPH) activity. To investigate the nature of such interactions, we synthesized selective alpha',beta'-epoxyketone inhibitors of the PGPH activity. In cellular proliferation and protein degradation assays, these inhibitors revealed that selective PGPH inhibition was insufficient to inhibit protein degradation, indicating that the CT-L and PGPH sites function… CONTINUE READING

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