Evidence map›Paper›PMID 39907714›Full record

ArticleACS chemical biology2025

Blm10-Based Compounds Add to the Knowledge of How Allosteric Modulators Influence Human 20S Proteasome.

Julia Witkowska, Małgorzata Giżyńska, Przemysław Karpowicz, Daria Sowik, Karolina Trepczyk, Fabian Hennenberg, Ashwin Chari, Artur Giełdoń, Karolina Pierzynowska, Lidia Gaffke and 2 more

Abstract read
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In one paragraph

Article in ACS chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. 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

12 authors.

Julia WitkowskaDepartment of Biomedical Chemistry, Faculty of Chemistry, University of Gdańsk, Gdańsk 80-308, Poland.
Małgorzata GiżyńskaDepartment of Biomedical Chemistry, Faculty of Chemistry, University of Gdańsk, Gdańsk 80-308, Poland.ORCID 0000-0002-3206-5605
Przemysław KarpowiczDepartment of Biomedical Chemistry, Faculty of Chemistry, University of Gdańsk, Gdańsk 80-308, Poland.ORCID 0000-0003-4912-3709
Daria SowikDepartment of Biomedical Chemistry, Faculty of Chemistry, University of Gdańsk, Gdańsk 80-308, Poland.
Karolina TrepczykDepartment of Biomedical Chemistry, Faculty of Chemistry, University of Gdańsk, Gdańsk 80-308, Poland.
Fabian HennenbergDepartment of Structural Dynamics, Max-Planck-Institute for Biophysical Chemistry, Goettingen 37077, Germany.ORCID 0000-0003-3444-0947
Ashwin ChariDepartment of Structural Dynamics, Max-Planck-Institute for Biophysical Chemistry, Goettingen 37077, Germany.
Artur GiełdońDepartment of Theoretical Chemistry, Faculty of Chemistry, University of Gdańsk, Gdańsk 80-308, Poland.ORCID 0000-0003-0415-9214
Karolina PierzynowskaDepartment of Molecular Biology, Faculty of Biology, University of Gdańsk, Gdańsk 80-308, Poland.
Lidia GaffkeDepartment of Molecular Biology, Faculty of Biology, University of Gdańsk, Gdańsk 80-308, Poland.
Grzegorz WęgrzynDepartment of Molecular Biology, Faculty of Biology, University of Gdańsk, Gdańsk 80-308, Poland.
Elżbieta JankowskaDepartment of Biomedical Chemistry, Faculty of Chemistry, University of Gdańsk, Gdańsk 80-308, Poland.ORCID 0000-0002-1099-8885

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteasomes catalyze protein degradation in cells and play an integral role in cellular homeostasis. Its activity decreases with age alongside the load of defective proteins, resulting from mutations or oxidative stress-induced damage. Such proteins are prone to aggregation and, if not efficiently degraded, can form toxic oligomers and amyloid plaques. Developing an effective way to activate the proteasome could prevent such pathologies. Designing activators is not easy because they do not bind in the active site, which is well-defined and highly conserved, but away from it. The structures of proteasome complexes with natural activators can help here, but these are large proteins, some even multimeric, whose activity is difficult to replace with a small-molecule compound. Nevertheless, the use of fragments of such proteins makes it possible to accumulate knowledge about the relevance of various structural elements for efficient and selective activation. Here, we presented peptidic activators of the 20S proteasome, which were designed based on both the

Indexed as

Proteasome Endopeptidase ComplexAllosteric RegulationHumansModels, MolecularSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsBlm10 protein, S cerevisiaeProteasome Endopeptidase ComplexSaccharomyces cerevisiae Proteins

Identifiers

PMID39907714
PMCPMC11851449

What Socratic 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 Socratic graph.