Evidence map›Paper›PMID 10582236›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences1999

The proteasome: a macromolecular assembly designed for controlled proteolysis.

P Zwickl, D Voges, W Baumeister

Abstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Implications for proteasome nuclear localization revealed by the structure of the nuclear proteasome tether protein Cut8.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  14. Peptidomic analysis of human cell lines.Journal of proteome research · 2011
    Article
  15. How is the balance between protein synthesis and degradation achieved?Theoretical biology & medical modelling · 2010
    Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Crystallization and preliminary X-ray analysis of the Thermoplasma acidophilum 20S proteasome in complex with protein substrates.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008
    Article
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

3 authors.

P ZwicklMax-Planck-Institute for Biochemistry, Martinsried, Germany.
D Voges
W Baumeister

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotic cells, the vast majority of proteins in the cytosol and nucleus are degraded via the proteasome-ubiquitin pathway. The 26S proteasome is a huge protein degradation machine of 2.5 MDa, built of approximately 35 different subunits. It contains a proteolytic core complex, the 20S proteasome and one or two 19S regulatory complexes which associate with the termini of the barrel-shaped 20S core. The 19S regulatory complex serves to recognize ubiquitylated target proteins and is implicated to have a role in their unfolding and translocation into the interior of the 20S complex where they are degraded into oligopeptides. While much progress has been made in recent years in elucidating the structure, assembly and enzymatic mechanism of the 20S complex, our knowledge of the functional organization of the 19S regulator is rather limited. Most of its subunits have been identified, but specific functions can be assigned to only a few of them.

Indexed as

Adenosine TriphosphatasesAnimalsCysteine EndopeptidasesHumansMultienzyme ComplexesPeptide HydrolasesProteasome Endopeptidase ComplexProteinsAdenosine TriphosphatasesATP dependent 26S proteaseCysteine EndopeptidasesMultienzyme ComplexesPeptide HydrolasesProteasome Endopeptidase ComplexProteins

Identifiers

PMID10582236
PMCPMC1692663

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.