Protein abundance changes and ubiquitylation targets identified after inhibition of the proteasome with syringolin A.

@article{Svozil2014ProteinAC,
  title={Protein abundance changes and ubiquitylation targets identified after inhibition of the proteasome with syringolin A.},
  author={Julia Svozil and Matthias Hirsch-Hoffmann and R. Dudler and Wilhelm Gruissem and Katja Baerenfaller},
  journal={Molecular & cellular proteomics : MCP},
  year={2014},
  volume={13 6},
  pages={1523-36}
}
As proteins are the main effectors inside cells, their levels need to be tightly regulated. This is partly achieved by specific protein degradation via the Ubiquitin-26S proteasome system (UPS). In plants, an exceptionally high number of proteins are involved in Ubiquitin-26S proteasome system-mediated protein degradation and it is known to regulate most, if not all, important cellular processes. Here, we investigated the response to the inhibition of the proteasome at the protein level… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 11 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 92 references

NBR1-mediated selective autophagy targets insoluble ubiquitinated protein aggregates in plant stress responses

  • J. Zhou, J. Wang, +4 authors Z. Chen
  • PLoS Genet 9,
  • 2013

Similar Papers

Loading similar papers…