Evidence map›Paper›PMID 31473102›Full record

ArticleMolecular cell2019

Characterization of Fully Recombinant Human 20S and 20S-PA200 Proteasome Complexes.

Ana Toste Rêgo, Paula C A da Fonseca

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

76 citing papers in PubMed, 118 citations in OpenAlex.

  1. Article
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  6. Plasticity in the structure and assembly of proteasomes.The Journal of biological chemistry · 2026
    Review
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  12. Review
  13. A recombinant expression system for thebioRxiv : the preprint server for biology · 2025
    Article
  14. Age-Associated Proteomic Changes in Human Spermatozoa.International journal of molecular sciences · 2025
    Article
  15. Enhancing schistosomiasis drug discovery approaches with optimized proteasome substrates.Protein science : a publication of the Protein Society · 2025
    Article
  16. Article
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  20. Article

16 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Ana Toste RêgoMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Paula C A da FonsecaMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK. Electronic address: pauladf@mrc-lmb.cam.ac.uk.
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_UP_1201/5
6 · The paper itself

Abstract

Proteasomes are essential in all eukaryotic cells. However, their function and regulation remain considerably elusive, particularly those of less abundant variants. We demonstrate the human 20S proteasome recombinant assembly and confirmed the recombinant complex integrity biochemically and with a 2.6 Å resolution cryo-EM map. To assess its competence to form higher-order assemblies, we prepared and analyzed recombinant human 20S-PA200, a poorly characterized nuclear complex. Its 3.0 Å resolution cryo-EM structure reveals the PA200 unique architecture; the details of its intricate interactions with the proteasome, resulting in unparalleled proteasome α ring rearrangements; and the molecular basis for PA200 allosteric modulation of the proteasome active sites. Non-protein cryo-EM densities could be assigned to PA200-bound inositol phosphates, and we speculate regarding their functional role. Here we open extensive opportunities to study the fundamental properties of the diverse and distinct eukaryotic proteasome variants and to improve proteasome targeting under different therapeutic conditions.

Indexed as

Allosteric RegulationAnimalsBinding SitesHumansInositol PhosphatesModels, MolecularNuclear ProteinsProteasome Endopeptidase ComplexProtein BindingProtein ConformationProteolysisRecombinant ProteinsSf9 CellsSpodopteraStructure-Activity RelationshipInositol PhosphatesNuclear ProteinsProteasome Endopeptidase ComplexPSME4 protein, humanRecombinant Proteins20S-PA200atomic modelcryo-EMhumanPA200proteasomerecombinantregulatorstructure

Identifiers

PMID31473102
PMCPMC6863390
OpenAlexW2970566419

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.