Evidence map›Paper›PMID 15665121›Full record

ArticleBiophysical journal2005

A mathematical model of protein degradation by the proteasome.

Fabio Luciani, Can Keşmir, Michele Mishto, Michal Or-Guil, Rob J de Boer

Abstract read
In one paragraph

Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Frontiers in microbiology · 2024
    Article
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  4. Review
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  12. A systems view of the protein expression process.Systems and synthetic biology · 2011
    Article
  13. Article
  14. Article
  15. 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
  16. 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

5 authors.

Fabio LucianiInstitute for Theoretical Biology, Humboldt University-Berlin, Berlin, Germany.
Can Keşmir
Michele Mishto
Michal Or-Guil
Rob J de Boer

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The proteasome is the major protease for intracellular protein degradation. The influx rate of protein substrates and the exit rate of the fragments/products are regulated by the size of the axial channels. Opening the channels is known to increase the overall degradation rate and to change the length distribution of fragments. We develop a mathematical model with a flux that depends on the gate size and a phenomenological cleavage mechanism. The model has Michaelis-Menten kinetics with a V(max) that is inversely related to the length of the substrate, as observed in the in vitro experiments. We study the distribution of fragment lengths assuming that proteasomal cleavage takes place at a preferred distance from the ends of a protein fragment, and find multipeaked fragment length distributions similar to those found experimentally. Opening the gates in the model increases the degradation rate, increases the average length of the fragments, and increases the peak in the distribution around a length of 8-10 amino acids. This behavior is also observed in immunoproteasomes equipped with PA28. Finally, we study the effect of re-entry of processed fragments in the degradation kinetics and conclude that re-entry is only expected to affect the cleavage dynamics when short fragments enter the proteasome much faster than the original substrate. In summary, the model proposed in this study captures the known characteristics of proteasomal degradation, and can therefore help to quantify MHC class I antigen processing and presentation.

Indexed as

Antigen PresentationBiodegradation, EnvironmentalBiophysicsCysteine EndopeptidasesHistocompatibility Antigens Class IHumansKineticsModels, StatisticalModels, TheoreticalMultienzyme ComplexesMuscle ProteinsNormal DistributionProteasome Endopeptidase ComplexProteinsSubstrate SpecificityTime FactorsCysteine EndopeptidasesHistocompatibility Antigens Class IMultienzyme ComplexesMuscle ProteinsProteasome Endopeptidase ComplexProteinsPSME1 protein, human

Identifiers

PMID15665121
PMCPMC1305341

What OpenQuestion holds

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Registered trials

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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.