Evidence map›Paper›PMID 14749732›Full record

ArticleThe EMBO journal2004

Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae.

Martin Haslbeck, Nathalie Braun, Thusnelda Stromer, Bettina Richter, Natascha Model, Sevil Weinkauf, Johannes Buchner

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

83 citing papers in PubMed, 234 citations in OpenAlex.

  1. Article
  2. Article
  3. TaHSP18.6 and TaSRT1 interact to confer resistance toProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. A microaerobically induced small heat shock protein contributes toApplied and environmental microbiology · 2025
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Compatible solutes determine the heat resistance of conidia.Fungal biology and biotechnology · 2023
    Article
  11. Article
  12. Quiescence inAnnual review of genetics · 2022
    Review
  13. Chaperone requirements for de novo folding ofMolecular biology of the cell · 2022
    Article
  14. Article
  15. Differential Roles of Three α-Crystallin Domain-Containing sHsps ofInternational journal of molecular sciences · 2022
    Article
  16. Article
  17. Article
  18. The role of heat shock proteins in preventing amyloid toxicity.Frontiers in molecular biosciences · 2022
    Review
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Martin HaslbeckInstitut für Organische Chemie und Biochemie, Technische Universität München, Garching, Germany.
Nathalie Braun
Thusnelda Stromer
Bettina Richter
Natascha Model
Sevil Weinkauf
Johannes Buchner
Technical University of Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small heat shock proteins (sHsps) are ubiquitous molecular chaperones that prevent the unspecific aggregation of proteins. So far, Hsp26 was the only unambiguously identified member of the sHsp family in Saccharomyces cerevisiae. We show here that the sHsp system in the cytosol of S. cerevisiae consists of two proteins, Hsp26 and Hsp42. Hsp42 forms large dynamic oligomers with a barrel-like structure. In contrast to Hsp26, which functions predominantly at heat shock temperatures, Hsp42 is active as a chaperone under all conditions tested in vivo and in vitro. Under heat shock conditions, both Hsp42 and Hsp26 suppress the aggregation of one-third of the cytosolic proteins. This subset is about 90% overlapping for Hsp42 and Hsp26. The sHsp substrates belong to different biochemical pathways. This indicates a general protective function of sHsps for proteome stability in S. cerevisiae. Consistent with this observation, sHsp knockout strains show phenotypical defects. Taken together, our results define Hsp42 as an important player for protein homeostasis at physiological and under stress conditions.

Indexed as

CytosolGene DeletionHeat-Shock ProteinsProtein DenaturationProteomeSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsHeat-Shock ProteinsHSP26 protein, S cerevisiaeHSP42 protein, S cerevisiaeProteomeSaccharomyces cerevisiae Proteins

Identifiers

PMID14749732
PMCPMC1271810
OpenAlexW2135471957

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.