Evidence map›Paper›PMID 22215586›Full record

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

Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy.

Eri Sakata, Stefan Bohn, Oana Mihalache, Petra Kiss, Florian Beck, Istvan Nagy, Stephan Nickell, Keiji Tanaka, Yasushi Saeki, Friedrich Förster 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 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
7.0field-weighted citation impact, top 2% 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

74 citing papers in PubMed, 120 citations in OpenAlex.

  1. Article
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  6. Bimodular architecture of bacterial effector SAP05 that drives ubiquitin-independent targeted protein degradation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Article
  8. Review
  9. Review
  10. Ubiquitin modulates 26Science advances · 2022
    Article
  11. Article
  12. Review
  13. Article
  14. Monoubiquitination in Homeostasis and Cancer.International journal of molecular sciences · 2022
    Review
  15. Review
  16. Mechanisms of substrate recognition by the 26S proteasome.Current opinion in structural biology · 2021
    Review
  17. Review
  18. Article
  19. Review
  20. Article

14 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 2 countries.

Eri SakataDepartment of Molecular Structural Biology, Max-Planck-Institute of Biochemistry, Martinsried 82152, Germany.
Stefan Bohn
Oana Mihalache
Petra Kiss
Florian Beck
Istvan Nagy
Stephan Nickell
Keiji Tanaka
Yasushi Saeki
Friedrich Förster
Wolfgang Baumeister
Max Planck Institute of Biochemistry · DETokyo Metropolitan Institute of Medical Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two canonical subunits of the 26S proteasome, Rpn10 and Rpn13, function as ubiquitin (Ub) receptors. The mutual arrangement of these subunits--and all other non-ATPase subunits--in the regulatory particle is unknown. Using electron cryomicroscopy, we calculated difference maps between wild-type 26S proteasome from Saccharomyces cerevisiae and deletion mutants (rpn10Δ, rpn13Δ, and rpn10Δrpn13Δ). These maps allowed us to localize the two Ub receptors unambiguously. Rpn10 and Rpn13 mapped to the apical part of the 26S proteasome, above the N-terminal coiled coils of the AAA-ATPase heterodimers Rpt4/Rpt5 and Rpt1/Rpt2, respectively. On the basis of the mutual positions of Rpn10 and Rpn13, we propose a model for polyubiquitin binding to the 26S proteasome.

Indexed as

AnimalsCryoelectron MicroscopyDrosophila melanogasterMass SpectrometryModels, MolecularProteasome Endopeptidase ComplexSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsProteasome Endopeptidase ComplexRPN10 protein, S cerevisiaeRPN13 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID22215586
PMCPMC3277190
OpenAlexW2166475702

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.