Evidence map›Paper›PMID 11139393›Full record

ArticleThe Biochemical journal2001

gamma-Interferon decreases the level of 26 S proteasomes and changes the pattern of phosphorylation.

S Bose, P Brooks, G G Mason, A J Rivett

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

21 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Adaptation of the Tumor Antigen Presentation Machinery to Ionizing Radiation.Journal of immunology (Baltimore, Md. : 1950) · 2023
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  6. Islet stress, degradation and autoimmunity.Diabetes, obesity & metabolism · 2018
    Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Immunoproteasomes: structure, function, and antigen presentation.Progress in molecular biology and translational science · 2012
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

4 authors at 1 institution in 1 country.

S BoseDepartment of Biochemistry, University of Bristol, School of Medical Sciences, Bristol BS8 1TD, U.K.
P Brooks
G G Mason
A J Rivett
University of Bristol · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In mammalian cells proteasomes can be activated by two different types of regulatory complexes which bind to the ends of the proteasome cylinder. Addition of two 19 S (PA700; ATPase) complexes forms the 26 S proteasome, which is responsible for ATP-dependent non-lysosomal degradation of intracellular proteins, whereas 11 S complexes (PA28; REG) have been implicated in antigen processing. The PA28 complex is upregulated in response to gamma-interferon (gamma-IFN) as are three non-essential subunits of the 20 S proteasome. In the present study we have investigated the effects of gamma-IFN on the level of different proteasome complexes and on the phosphorylation of proteasome subunits. After treatment of cells with gamma-IFN, the level of 26 S proteasomes decreased and there was a concomitant increase in PA28-proteasome complexes. However, no free 19 S regulatory complexes were detected. The majority of the gamma-IFN-inducible proteasome subunits LMP2 and LMP7 were present in PA28-proteasome complexes, but these subunits were also found in 26 S proteasomes. The level of phosphorylation of both 20 S and 26 S proteasome subunits was found to decrease after gamma-IFN treatment of cells. The C8 alpha subunit showed more than a 50% decrease in phosphorylation, and the phosphorylation of C9 was only barely detectable after gamma-IFN treatment. These results suggest that association of regulatory components to 20 S proteasomes is regulated, and that phosphorylation of proteasome alpha subunits may be one mode of regulation.

Indexed as

Muscle ProteinsProteasome Endopeptidase ComplexCell LineChromatography, GelDown-RegulationHumansImmunoblottingInterferon-gammaModels, ChemicalPeptide HydrolasesPhosphorylationProteinsATP dependent 26S proteaseInterferon-gammaMuscle ProteinsPeptide HydrolasesProteasome Endopeptidase ComplexProteinsPSME1 protein, human

Identifiers

PMID11139393
PMCPMC1221571
OpenAlexW2079364668

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.