Evidence map›Paper›PMID 36671396›Full record

ArticleBiomolecules2022

Hsp70 and Hsp110 Chaperones Promote Early Steps of Proteasome Assembly.

Ana C Matias, Joao Matos, R Jürgen Dohmen, Paula C Ramos

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biomolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Mechanism of autocatalytic activation during proteasome assembly.Nature structural & molecular biology · 2024
    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 2 institutions in 2 countries.

Ana C MatiasCenter of Molecular Biosciences, Institute for Genetics, Department of Biology, Faculty of Natural Sciences and Mathematics, University of Cologne, 50674 Cologne, Germany.ORCID 0000-0002-6385-9117
Joao MatosDepartamento de Química e Bioquímica, Faculdade de Ciências e Tecnologia, Universidade do Algarve, 8000-117 Faro, Portugal.
R Jürgen DohmenCenter of Molecular Biosciences, Institute for Genetics, Department of Biology, Faculty of Natural Sciences and Mathematics, University of Cologne, 50674 Cologne, Germany.ORCID 0000-0002-5756-6780
Paula C RamosCenter of Molecular Biosciences, Institute for Genetics, Department of Biology, Faculty of Natural Sciences and Mathematics, University of Cologne, 50674 Cologne, Germany.
University of Cologne · DEUniversity of Algarve · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Whereas assembly of the 20S proteasome core particle (CP) in prokaryotes apparently occurs spontaneously, the efficiency of this process in eukaryotes relies on the dedicated assembly chaperones Ump1, Pba1-Pba2, and Pba3-Pba4. For mammals, it was reported that CP assembly initiates with formation of a complete α-ring that functions as a template for β subunit incorporation. By contrast, we were not able to detect a ring composed only of a complete set of α subunits in

Indexed as

Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsHSP70 Heat-Shock ProteinsHumansMolecular ChaperonesProteasome Endopeptidase ComplexHSP70 Heat-Shock ProteinsMolecular ChaperonesPba1 protein, S cerevisiaePba2 protein, S cerevisiaeProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinschaperonesHsp110Hsp70proteasome biogenesisSsa1Sse1

Identifiers

PMID36671396
PMCPMC9855889
OpenAlexW4312070193

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.