Evidence map›Paper›PMID 37566026›Full record

ReviewCells2023

Functional Diversity of Mammalian Small Heat Shock Proteins: A Review.

Chaoguang Gu, Xinyi Fan, Wei Yu

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

23 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Heat shock proteins in hypothermia: a review.Frontiers in molecular biosciences · 2025
    Review
  16. Article
  17. Review
  18. Article
  19. Review
  20. Astaxanthin mediated repair of tBHP-Induced cellular injury in chondrocytes.Redox report : communications in free radical research · 2024
    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 at 2 institutions in 2 countries.

Chaoguang GuInstitute of Biochemistry, College of Life Sciences and Medicine, Zhejiang Sci-Tech University, Xiasha High-Tech Zone No.2 Road, Hangzhou 310018, China.
Xinyi FanFaculty of Arts and Science, University of Toronto, Toronto, ON M5S1A1, Canada.
Wei YuInstitute of Biochemistry, College of Life Sciences and Medicine, Zhejiang Sci-Tech University, Xiasha High-Tech Zone No.2 Road, Hangzhou 310018, China.
Zhejiang Sci-Tech University · CNUniversity of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The small heat shock proteins (sHSPs), whose molecular weight ranges from 12∼43 kDa, are members of the heat shock protein (HSP) family that are widely found in all organisms. As intracellular stress resistance molecules, sHSPs play an important role in maintaining the homeostasis of the intracellular environment under various stressful conditions. A total of 10 sHSPs have been identified in mammals, sharing conserved α-crystal domains combined with variable N-terminal and C-terminal regions. Unlike large-molecular-weight HSP, sHSPs prevent substrate protein aggregation through an ATP-independent mechanism. In addition to chaperone activity, sHSPs were also shown to suppress apoptosis, ferroptosis, and senescence, promote autophagy, regulate cytoskeletal dynamics, maintain membrane stability, control the direction of cellular differentiation, modulate angiogenesis, and spermatogenesis, as well as attenuate the inflammatory response and reduce oxidative damage. Phosphorylation is the most significant post-translational modification of sHSPs and is usually an indicator of their activation. Furthermore, abnormalities in sHSPs often lead to aggregation of substrate proteins and dysfunction of client proteins, resulting in disease. This paper reviews the various biological functions of sHSPs in mammals, emphasizing the roles of different sHSPs in specific cellular activities. In addition, we discuss the effect of phosphorylation on the function of sHSPs and the association between sHSPs and disease.

Indexed as

Heat-Shock Proteins, SmallAnimalsHeat-Shock ProteinsHumansMaleMammalsOxidative StressProtein AggregatesHeat-Shock ProteinsHeat-Shock Proteins, SmallProtein Aggregatesdiseasefunctional diversitymammalianphosphorylationsHSPs

Identifiers

PMID37566026
PMCPMC10417760
OpenAlexW4385347355

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.