Evidence map›Paper›PMID 22927375›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Near-atomic resolution structural model of the yeast 26S proteasome.

Florian Beck, Pia Unverdorben, Stefan Bohn, Andreas Schweitzer, Günter Pfeifer, Eri Sakata, Stephan Nickell, Jürgen M Plitzko, Elizabeth Villa, Wolfgang Baumeister and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 148 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
148citing papers in PubMed, 1 pooled it
16.4field-weighted citation impact, top 1% of its field
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

148 citing papers in PubMed, 1 synthesis or guideline pooled it, 258 citations in OpenAlex.

  1. Pooled it
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  13. Proteasomal subunit depletions differentially affect germline integrity inFrontiers in cell and developmental biology · 2022
    Article
  14. Article
  15. Concept and application of circulating proteasomes.Experimental & molecular medicine · 2021
    Review
  16. Review
  17. Review
  18. The Cryo-EM Effect: Structural Biology of Neurodegenerative Disease Proteostasis Factors.Journal of neuropathology and experimental neurology · 2021
    Review
  19. Article
  20. Article

88 more citing papers are in PubMed but not listed here.

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

11 authors at 2 institutions in 1 country.

Florian BeckDepartment of Molecular Structural Biology, Max-Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Pia Unverdorben
Stefan Bohn
Andreas Schweitzer
Günter Pfeifer
Eri Sakata
Stephan Nickell
Jürgen M Plitzko
Elizabeth Villa
Wolfgang Baumeister
Friedrich Förster
Max Planck Society · DEMax Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The 26S proteasome operates at the executive end of the ubiquitin-proteasome pathway. Here, we present a cryo-EM structure of the Saccharomyces cerevisiae 26S proteasome at a resolution of 7.4 Å or 6.7 Å (Fourier-Shell Correlation of 0.5 or 0.3, respectively). We used this map in conjunction with molecular dynamics-based flexible fitting to build a near-atomic resolution model of the holocomplex. The quality of the map allowed us to assign α-helices, the predominant secondary structure element of the regulatory particle subunits, throughout the entire map. We were able to determine the architecture of the Rpn8/Rpn11 heterodimer, which had hitherto remained elusive. The MPN domain of Rpn11 is positioned directly above the AAA-ATPase N-ring suggesting that Rpn11 deubiquitylates substrates immediately following commitment and prior to their unfolding by the AAA-ATPase module. The MPN domain of Rpn11 dimerizes with that of Rpn8 and the C-termini of both subunits form long helices, which are integral parts of a coiled-coil module. Together with the C-terminal helices of the six PCI-domain subunits they form a very large coiled-coil bundle, which appears to serve as a flexible anchoring device for all the lid subunits.

Indexed as

Models, MolecularCryoelectron MicroscopyEndopeptidasesMolecular Dynamics SimulationProteasome Endopeptidase ComplexProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsATP dependent 26S proteaseEndopeptidasesProteasome Endopeptidase ComplexRPN11 protein, S cerevisiaeRpn8 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID22927375
PMCPMC3443124
OpenAlexW2085175631

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.