Structure of the human 26S proteasome at a resolution of 3.9 Å.

@article{Schweitzer2016StructureOT,
  title={Structure of the human 26S proteasome at a resolution of 3.9 {\AA}.},
  author={Andreas Schweitzer and Antje Aufderheide and Till Rudack and Florian Beck and G{\"u}nter Pfeifer and J{\"u}rgen M Plitzko and Eri Sakata and Klaus Schulten and Friedrich F{\"o}rster and Wolfgang Baumeister},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2016},
  volume={113 28},
  pages={7816-21}
}
Protein degradation in eukaryotic cells is performed by the Ubiquitin-Proteasome System (UPS). The 26S proteasome holocomplex consists of a core particle (CP) that proteolytically degrades polyubiquitylated proteins, and a regulatory particle (RP) containing the AAA-ATPase module. This module controls access to the proteolytic chamber inside the CP and is surrounded by non-ATPase subunits (Rpns) that recognize substrates and deubiquitylate them before unfolding and degradation. The architecture… CONTINUE READING
Recent Discussions
This paper has been referenced on Twitter 6 times over the past 90 days. VIEW TWEETS
28 Citations
74 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 28 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 74 references

Structure of the 26S proteasome with ATP-γS bound provides insights into the mechanism of nucleotide-dependent substrate translocation

  • P Sled z
  • Proc Natl Acad Sci USA
  • 2013
Highly Influential
14 Excerpts

2 . 3 Å resolution cryoEM structure of human p 97 and mechanism of allosteric inhibition

  • S Nickell
  • Science
  • 2016

Computational methodologies for real-space structural refinement of large macromolecular complexes

  • BC Goh
  • Annu Rev Biophys
  • 2016
1 Excerpt

Similar Papers

Loading similar papers…