Evidence map›Paper›PMID 10363640›Full record

ReviewMolecular biology reports1999

Phosphorylation of proteasomes in mammalian cells.

S Bose, G G Mason, A J Rivett

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular biology reports, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

12 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Review
  3. Oxidative stress-mediated regulation of proteasome complexes.Molecular & cellular proteomics : MCP · 2011
    Review
  4. Review
  5. ASK1 negatively regulates the 26 S proteasome.The Journal of biological chemistry · 2010
    Article
  6. Potential roles for PA28beta in gastric adenocarcinoma development and diagnosis.Journal of cancer research and clinical oncology · 2010
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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 at 2 institutions in 1 country.

S BoseDepartment of Biochemistry, School of Medical Sciences, University of Bristol, UK.
G G Mason
A J Rivett
University of Bristol · GBBristol Royal Infirmary · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

20S proteasomes are large (700 kDa) proteinase complexes which form the central catalytic core of larger complexes (26S proteasomes or PA28-20S complexes) formed by association with regulatory particles. These larger complexes are involved in diverse regulatory processes in the cell including cyclin breakdown, proteolytic control of transcription factors and other short-lived regulatory proteins, and antigen presentation. In order to carry out these diverse functions the proteasome complexes must be held under tight regulatory control. The early recognition of potential phosphorylation sites in a number of core and regulatory subunits suggested that some control of the complexes activities may be via phosphorylation. We have investigated the role of phosphorylation in determining proteasome localization, activities and association with regulatory complexes.

Indexed as

Adenosine TriphosphatasesAnimalsCell LineCysteine EndopeptidasesHumansMultienzyme ComplexesPeptide HydrolasesPhosphorylationProteasome Endopeptidase ComplexRatsAdenosine TriphosphatasesATP dependent 26S proteaseCysteine EndopeptidasesMultienzyme ComplexesPeptide HydrolasesProteasome Endopeptidase Complex

Identifiers

PMID10363640
OpenAlexW247852621

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.