Evidence map›Paper›PMID 26393687›Full record

ArticleeLife2015

Quantitative time-resolved analysis reveals intricate, differential regulation of standard- and immuno-proteasomes.

Juliane Liepe, Hermann-Georg Holzhütter, Elena Bellavista, Peter M Kloetzel, Michael P H Stumpf, Michele Mishto

Abstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Proteasome-GeneratedFrontiers in immunology · 2021
    Article
  9. Response: Commentary: AnFrontiers in immunology · 2021
    Article
  10. Review
  11. Article
  12. Proteolytic dynamics of human 20S thymoproteasome.The Journal of biological chemistry · 2019
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. How to deal with parameters for whole-cell modelling.Journal of the Royal Society, Interface · 2017
    Review
  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

6 authors.

Juliane LiepeCentre for Integrative Systems Biology and Bioinformatics, Department of Life Sciences, Imperial College London, London, United Kingdom.
Hermann-Georg HolzhütterInstitut für Biochemie, Charité - Universitätsmedizin Berlin, Berlin, Germany.
Elena BellavistaDepartment of Experimental, Diagnostic and Specialty Medicine, Alma Mater Studiorum, University of Bologna, Bologna, Italy.
Peter M KloetzelInstitut für Biochemie, Charité - Universitätsmedizin Berlin, Berlin, Germany.
Michael P H StumpfCentre for Integrative Systems Biology and Bioinformatics, Department of Life Sciences, Imperial College London, London, United Kingdom.ORCID http://orcid.org/0000-0002-3577-1222
Michele MishtoInstitut für Biochemie, Charité - Universitätsmedizin Berlin, Berlin, Germany.

Funding

Biotechnology and Biological Sciences Research Council BB/G007934/1National Centre for the Replacement, Refinement and Reduction of Animals in Research NC/K001949/1
6 · The paper itself

Abstract

Proteasomal protein degradation is a key determinant of protein half-life and hence of cellular processes ranging from basic metabolism to a host of immunological processes. Despite its importance the mechanisms regulating proteasome activity are only incompletely understood. Here we use an iterative and tightly integrated experimental and modelling approach to develop, explore and validate mechanistic models of proteasomal peptide-hydrolysis dynamics. The 20S proteasome is a dynamic enzyme and its activity varies over time because of interactions between substrates and products and the proteolytic and regulatory sites; the locations of these sites and the interactions between them are predicted by the model, and experimentally supported. The analysis suggests that the rate-limiting step of hydrolysis is the transport of the substrates into the proteasome. The transport efficiency varies between human standard- and immuno-proteasomes thereby impinging upon total degradation rate and substrate cleavage-site usage.

Indexed as

Gene Expression RegulationAnimalsCell LineHumansKineticsLiverMiceModels, BiologicalProteasome Endopeptidase ComplexProtein TransportProteolysisProteasome Endopeptidase ComplexBayesian analysisbiophysicscomputational biologyexperimental designfunctional analysishumanmouseproteasome regulationproteasome structurestructural biologysystems biology

Identifiers

PMID26393687
PMCPMC4611054

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.