Evidence map›Paper›PMID 35204754›Full record

ArticleBiomolecules2022

Interaction with the Assembly Chaperone Ump1 Promotes Incorporation of the β7 Subunit into Half-Proteasome Precursor Complexes Driving Their Dimerization.

Jessica Zimmermann, Paula C Ramos, R Jürgen Dohmen

Open access · goldAbstract read
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 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.6field-weighted citation impact, top 37% 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

7 citing papers in PubMed, 7 citations in OpenAlex.

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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

3 authors at 1 institution in 1 country.

Jessica ZimmermannInstitute for Genetics, Center of Molecular Biosciences, Department of Biology, Faculty of Mathematics and Natural Sciences, University of Cologne, 50674 Cologne, Germany.
Paula C RamosInstitute for Genetics, Center of Molecular Biosciences, Department of Biology, Faculty of Mathematics and Natural Sciences, University of Cologne, 50674 Cologne, Germany.
R Jürgen DohmenInstitute for Genetics, Center of Molecular Biosciences, Department of Biology, Faculty of Mathematics and Natural Sciences, University of Cologne, 50674 Cologne, Germany.ORCID 0000-0002-5756-6780
University of Cologne · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biogenesis of the eukaryotic 20S proteasome core particle (PC) is a complex process assisted by specific chaperones absent from the active complex. The first identified chaperone, Ump1, was found in a precursor complex (PC) called 15S PC. Yeast cells lacking Ump1 display strong defects in the autocatalytic processing of β subunits, and consequently have lower proteolytic activity. Here, we dissect an important interaction of Ump1 with the β7 subunit that is critical for proteasome biogenesis. Functional domains of Ump1 and the interacting proteasome subunit β7 were mapped, and the functional consequences of their deletion or mutation were analyzed. Cells in which the first sixteen Ump1 residues were deleted display growth phenotypes similar to

Indexed as

DimerizationMolecular ChaperonesMutationProteasome Endopeptidase ComplexSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMolecular ChaperonesPRE4 protein, S cerevisiaeProteasome Endopeptidase Complexproteasome maturation proteinSaccharomyces cerevisiae Proteins15S precursor complexassemblyPre4proteasomeRpn4SaccharomycesUmp1

Identifiers

PMID35204754
PMCPMC8961534
OpenAlexW4210815731

What OpenQuestion holds

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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.