Evidence map›Paper›PMID 22799889›Full record

ReviewChemical research in toxicology2012

Small molecule activators of the heat shock response: chemical properties, molecular targets, and therapeutic promise.

James D West, Yanyu Wang, Kevin A Morano

Abstract readReview
In one paragraph

Review in Chemical research in toxicology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

33 citing papers in PubMed, 58 citations in OpenAlex.

  1. Disulphide maintenance systems and proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  2. Review
  3. Article
  4. Monitoring of the Heat Shock Response with a Real-Time Luciferase Reporter.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. The heat shock response and small molecule regulators.European journal of medicinal chemistry · 2021
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
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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 2 institutions in 1 country.

James D WestBiochemistry and Molecular Biology Program, Departments of Biology and Chemistry, The College of Wooster, Wooster, Ohio 44691, USA. jwest@wooster.edu
Yanyu Wang
Kevin A Morano
The University of Texas Health Science Center at Houston · USCollege of Wooster · US

Funding

Hsp110 protein chaperone function in yeastR01GM074696 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI MORANO, KEVIN ANTHONY · 2006 to 2015
$2.8M
NIGMS NIH HHS GM074696NIGMS NIH HHS R01 GM074696
6 · The paper itself

Abstract

All cells have developed various mechanisms to respond and adapt to a variety of environmental challenges, including stresses that damage cellular proteins. One such response, the heat shock response (HSR), leads to the transcriptional activation of a family of molecular chaperone proteins that promote proper folding or clearance of damaged proteins within the cytosol. In addition to its role in protection against acute insults, the HSR also regulates lifespan and protects against protein misfolding that is associated with degenerative diseases of aging. As a result, identifying pharmacological regulators of the HSR has become an active area of research in recent years. Here, we review progress made in identifying small molecule activators of the HSR, what cellular targets these compounds interact with to drive response activation, and how such molecules may ultimately be employed to delay or reverse protein misfolding events that contribute to a number of diseases.

Indexed as

Amino Acid SequenceAnimalsDNA-Binding ProteinsHeat-Shock ProteinsHeat-Shock ResponseHeat Shock Transcription FactorsHumansMolecular Sequence DataProtein FoldingProteostasis DeficienciesSmall Molecule LibrariesTranscription FactorsDNA-Binding ProteinsHeat-Shock ProteinsHeat Shock Transcription FactorsSmall Molecule LibrariesTranscription Factors

Identifiers

PMID22799889
PMCPMC3472121
OpenAlexW2056966915

What OpenQuestion holds

Textmetadata
LicenceTDM
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.