Evidence map›Paper›PMID 9228289›Full record

ReviewMolecular biology reports1997

Regulation of proteasome structure and function.

A J Rivett, G G Mason, R Z Murray, J Reidlinger

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular biology reports, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Physical association of ubiquitin ligases and the 26S proteasome.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  8. Review
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

4 authors.

A J RivettDepartment of Biochemistry, University of Bristol, School of Medical Sciences, UK.
G G Mason
R Z Murray
J Reidlinger

Funding

Wellcome Trust
6 · The paper itself

Abstract

Proteasomes are cylindrical particles made up of a stack of four heptameric rings. In animal cells the outer rings are made up of 7 different types of alpha subunits and the inner rings are composed of 7 out of 10 possible different beta subunits. Regulatory complexes can bind to the ends of the cylinder. We have investigated aspects of the assembly, activity and subunit composition of core proteasome particles and 26S proteasomes, the localization of proteasome subpopulations, and the possible role of phosphorylation in determining proteasome localization, activities and association with regulatory components.

Indexed as

Proteasome Endopeptidase ComplexAnimalsArchaeal ProteinsEndopeptidasesHumansPeptide HydrolasesArchaeal ProteinsATP dependent 26S proteaseEndopeptidasesPeptide HydrolasesProteasome Endopeptidase Complexproteasome, Thermoplasma

Identifiers

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.