Evidence map›Paper›PMID 20133678›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Nature's molecular sponges: small heat shock proteins grow into their chaperone roles.

Stephen J Eyles, Lila M Gierasch

Open access · greenAbstract readComment
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

45 citing papers in PubMed, 116 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. How the Ectopic Expression of the BarleyInternational journal of molecular sciences · 2025
    Article
  6. Transcriptomic analysis of the response ofFrontiers in microbiology · 2024
    Article
  7. Article
  8. Article
  9. A proteome-wide map of chaperone-assisted protein refolding in a cytosol-like milieu.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Article
  11. Review
  12. General Structural and Functional Features of Molecular Chaperones.Advances in experimental medicine and biology · 2021
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. The Phenotypic Analysis ofFrontiers in microbiology · 2019
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Stephen J EylesDepartment of Polymer Science and Engineering, University of Massachusetts, Amherst, MA 01003, USA.
Lila M Gierasch
University of Massachusetts Amherst · US

Funding

PEPTIDE CONFORMATIONS &INTERACTIONS WITH MEMBRANESR01GM027616 · NIGMS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI GIERASCH, LILA M · 1985 to 2015
$5.3M
NIH DIRECTOR'S PIONEER AWARDDP1OD000945 · OD · UNIVERSITY OF MASSACHUSETTS AMHERST · PI GIERASCH, LILA M · 2006 to 2010
$3.9M
NIGMS NIH HHS GM027616NIGMS NIH HHS R01 GM027616NIH HHS DP1 OD000945NIH HHS OD000945
6 · The paper itself

Abstract

PubMed holds no abstract for this paper.

Indexed as

Heat-Shock Proteins, SmallMolecular ChaperonesPeptidesProtein BindingProtein ConformationProtein FoldingTemperatureHeat-Shock Proteins, SmallMolecular ChaperonesPeptides

Identifiers

PMID20133678
PMCPMC2840345
OpenAlexW2046201295

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.