Evidence map›Paper›PMID 19921466›Full record

ArticleCell stress & chaperones2010

Why proteins without an alpha-crystallin domain should not be included in the human small heat shock protein family HSPB.

Guido Kappé, Wilbert C Boelens, Wilfried W de Jong

Abstract read
In one paragraph

Article in Cell stress & chaperones, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Small Heat Shock Proteins in Retinal Diseases.Frontiers in molecular biosciences · 2022
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Hydrophobic residues of melittin mediate its binding to αA-crystallin.Protein science : a publication of the Protein Society · 2020
    Article
  17. Article
  18. Article
  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

3 authors.

Guido KappéDepartment of Biomolecular Chemistry 271, Nijmegen Center for Molecular Life Sciences, Radboud University, P.O. Box 9101, 6500 HB, Nijmegen, The Netherlands.
Wilbert C Boelens
Wilfried W de Jong

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The presence of an alpha-crystallin domain documents the evolutionary relatedness of the ubiquitous family of small heat shock proteins. Sequence and three-dimensional structure provide no evidence for the presence of such a domain in HSPC034, recently proposed as the 11th member of the human HSPB family. Also, phylogenetic analyses detect no relationship between HSPC034 and the human HSPB1-10 sequences. Arguments are provided as to why inclusion in the HSPB family of proteins like HSPC034, which resemble small heat shock proteins in being heat-inducible and having chaperone-like properties and a low monomeric mass, but are evolutionarily unrelated, is misleading and confusing.

Indexed as

alpha-CrystallinsAmino Acid SequenceHeat-Shock Proteins, SmallHumansIntracellular Signaling Peptides and ProteinsMolecular Sequence DataPhylogenyProteinsProtein Structure, TertiarySequence AlignmentTerminology as Topicalpha-CrystallinsHeat-Shock Proteins, SmallHSPB11 protein, humanIntracellular Signaling Peptides and ProteinsProteins

Identifiers

PMID19921466
PMCPMC3082639

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.