Evidence map›Paper›PMID 19145068›Full record

ReviewProceedings of the Japan Academy. Series B, Physical and biological sciences2009

The proteasome: overview of structure and functions.

Keiji Tanaka

Abstract readReview
In one paragraph

Review in Proceedings of the Japan Academy. Series B, Physical and biological sciences, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 447 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
447citing papers in PubMed, 1 pooled it
–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

447 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Osmotic Remodeling of Extracellular Vesicles for Precision Nanomedicine.Small (Weinheim an der Bergstrasse, Germany) · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. The pivotal role of β-lactone stereochemistry in the development of SARS-CoV-2 MProtein science : a publication of the Protein Society · 2026
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. ACS chemical neuroscience · 2026
    Article
  20. Ligand-driven modulation of chaperone-cochaperone networks shapes proteostasis outcomes.Protein science : a publication of the Protein Society · 2026
    Article

387 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

1 author.

Keiji TanakaLaboratory of Frontier Science, Tokyo Metropolitan Institute of Medical Science, Japan. tanaka-kj@igakuken.or.jp

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The proteasome is a highly sophisticated protease complex designed to carry out selective, efficient and processive hydrolysis of client proteins. It is known to collaborate with ubiquitin, which polymerizes to form a marker for regulated proteolysis in eukaryotic cells. The highly organized proteasome plays a prominent role in the control of a diverse array of basic cellular activities by rapidly and unidirectionally catalyzing biological reactions. Studies of the proteasome during the past quarter of a century have provided profound insights into its structure and functions, which has appreciably contributed to our understanding of cellular life. Many questions, however, remain to be elucidated.

Indexed as

EndopeptidasesMolecular ChaperonesProteasome Endopeptidase ComplexUbiquitinUbiquitin-Protein LigasesEndopeptidasesMolecular ChaperonesProteasome Endopeptidase ComplexUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID19145068
PMCPMC3524306

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.