Evidence map›Paper›PMID 20467039›Full record

ArticleMolecular & cellular proteomics : MCP2010

Toward an integrated structural model of the 26S proteasome.

Friedrich Förster, Keren Lasker, Stephan Nickell, Andrej Sali, Wolfgang Baumeister

Abstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Go hybrid: EM, crystallography, and beyond.Current opinion in structural biology · 2012
    Review
  12. Near-atomic resolution structural model of the yeast 26S proteasome.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  13. Article
  14. Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  15. Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  16. The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes together.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  17. Article
  18. Article
  19. The N-end rule pathway and regulation by proteolysis.Protein science : a publication of the Protein Society · 2011
    Review
  20. Context-dependent resistance to proteolysis of intrinsically disordered proteins.Protein science : a publication of the Protein Society · 2011
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Friedrich FörsterDepartment of Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany. foerster@biochem.mpg.de
Keren Lasker
Stephan Nickell
Andrej Sali
Wolfgang Baumeister

Funding

Center for Protein Folding Machinery (RMI)PN2EY016525 · NEI · BAYLOR COLLEGE OF MEDICINE · PI CHIU, WAH · 2005 to 2015
$33.6M
NEW TOOLS FOR EXPLORING THE DYNAMIC INTERACTOME(RMI)U54RR022220 · NCRR · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2005 to 2011
$19.3M
IMP: Software for Hybrid Determination of Macromolecular Assembly StructuresR01GM083960 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SALI, ANDREJ · 2008 to 2024
$5.2M
Protein Modeling by Satisfaction of Spatial RestraintsR01GM054762 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SALI, ANDREJ · 2001 to 2008
$2.1M
NCRR NIH HHS U54 RR022220NEI NIH HHS PN2 EY016525NIGMS NIH HHS R01 GM054762NIGMS NIH HHS R01 GM083960NIGMS NIH HHS R01 GM54762
6 · The paper itself

Abstract

The 26S proteasome is the end point of the ubiquitin-proteasome pathway and degrades ubiquitylated substrates. It is composed of the 20S core particle (CP), where degradation occurs, and the 19S regulatory particle (RP), which ensures substrate specificity of degradation. Whereas the CP is resolved to atomic resolution, the architecture of the RP is largely unknown. We provide a comprehensive analysis of the current structural knowledge on the RP, including structures of the RP subunits, physical protein-protein interactions, and cryoelectron microscopy data. These data allowed us to compute an atomic model for the CP-AAA-ATPase subcomplex. In addition to this atomic model, further subunits can be mapped approximately, which lets us hypothesize on the substrate path during its degradation.

Indexed as

Models, MolecularAnimalsCryoelectron MicroscopyProteasome Endopeptidase ComplexProtein BindingProtein SubunitsATP dependent 26S proteaseProteasome Endopeptidase ComplexProtein Subunits

Identifiers

PMID20467039
PMCPMC2938054

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.