Evidence map›Paper›PMID 31767683›Full record

ArticleThe Journal of biological chemistry2020

Regulation of small heat-shock proteins by hetero-oligomer formation.

Evgeny V Mymrikov, Mareike Riedl, Carsten Peters, Sevil Weinkauf, Martin Haslbeck, Johannes Buchner

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Article
  2. Chimerization expands peroxiredoxin scope.Nature chemical biology · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Competing chaperone pathways in α-synuclein disaggregation and aggregation dynamics.Protein science : a publication of the Protein Society · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Medicina (Kaunas, Lithuania) · 2023
    Article
  15. Disordered region encodes α-crystallin chaperone activity toward lens client γD-crystallin.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

6 authors.

Evgeny V MymrikovCenter for Integrated Protein Science, Department of Chemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany.
Mareike RiedlCenter for Integrated Protein Science, Department of Chemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany.
Carsten PetersCenter for Integrated Protein Science, Department of Chemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany.
Sevil WeinkaufCenter for Integrated Protein Science, Department of Chemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany.
Martin HaslbeckCenter for Integrated Protein Science, Department of Chemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany.
Johannes BuchnerCenter for Integrated Protein Science, Department of Chemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany. Electronic address: johannes.buchner@tum.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small heat-shock proteins (sHsps) compose the most widespread family of molecular chaperones. The human genome encodes 10 different sHsps (HspB1-10). It has been shown that HspB1 (Hsp27), HspB5 (αB-crystallin), and HspB6 (Hsp20) can form hetero-oligomers

Indexed as

Protein MultimerizationCaco-2 CellsHeat-Shock Proteins, SmallHEK293 CellsHeLa CellsHep G2 CellsHumansMCF-7 CellsHeat-Shock Proteins, Smallchaperonehetero-oligomersHspBmolecular chaperoneoligomerizationprotein aggregationprotein foldingprotein–protein interactionsmall heat-shock protein (sHsp)

Identifiers

PMID31767683
PMCPMC6952609

What OpenQuestion holds

Textmetadata
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.