ReviewCellular and molecular life sciences : CMLS2015
Small heat-shock proteins: important players in regulating cellular proteostasis.
Review in Cellular and molecular life sciences : CMLS, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.
What it found
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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.
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.
Who cites it
96 citing papers in PubMed, 194 citations in OpenAlex.
- Proteostasis Dysfunction and Heat Shock Protein Networks in Intervertebral Disc Degeneration: Molecular Mechanisms and Therapeutic Opportunities.Current issues in molecular biology · 2026Review
- Usnic acid inhibits colorectal cancer liver metastasis by targeting CRYAB phosphorylation and inducing ferroptosis.Cell communication and signaling : CCS · 2026Article
- Adverse effects of thermal pollution on rainbow trout (Oncorhynchus mykiss): unveiling the roles of heat shock proteins and acute-phase proteinsMette.Veterinary research communications · 2026Review
- Regulatory role of serine 59 in the oligomeric dynamics and chaperone function of αB-crystallin.Scientific reports · 2025Article
- Cellular strategies for surviving the alpine extremes: methylerythritol phosphate pathway-driven isoprenoid biosynthesis and stress resilience.Protoplasma · 2025Review
- Functional proteomic insights into the lateral oviduct-associated secretions of a bean bug.iScience · 2025Article
- The interaction of Cu(II) and Zn(II) with peptide fragment of HSPB1 and its analogs.Frontiers in molecular biosciences · 2025Article
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- Cancer-specific alterations in nuclear matrix proteins determined by multi-omics analyses of ductal carcinomaFrontiers in oncology · 2024Article
- A review on oligomeric polydispersity and oligomers-dependent holding chaperone activity of the small heat-shock protein IbpB of Escherichia coli.Cell stress & chaperones · 2023Review
- Human Small Heat Shock Protein B8 Inhibits Protein Aggregation without Affecting the Native Folding Process.Journal of the American Chemical Society · 2023Article
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- Oligomeric State and Holding Activity of Hsp60.International journal of molecular sciences · 2023Article
- Heat-Shock Proteins in Leukemia and Lymphoma: Multitargets for Innovative Therapeutic Approaches.Cancers · 2023Review
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- Cytoplasmic molecular chaperones in Pseudomonas species.Journal of microbiology (Seoul, Korea) · 2022Review
- High mRNA Expression Levels of Heat Shock Protein Family B Member 2 (International journal of molecular sciences · 2022Article
- Effect of Betaine and Arginine on Interaction of αB-Crystallin with Glycogen PhosphorylaseInternational journal of molecular sciences · 2022Article
36 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Small heat-shock proteins (sHsps) are a diverse family of intra-cellular molecular chaperone proteins that play a critical role in mitigating and preventing protein aggregation under stress conditions such as elevated temperature, oxidation and infection. In doing so, they assist in the maintenance of protein homeostasis (proteostasis) thereby avoiding the deleterious effects that result from loss of protein function and/or protein aggregation. The chaperone properties of sHsps are therefore employed extensively in many tissues to prevent the development of diseases associated with protein aggregation. Significant progress has been made of late in understanding the structure and chaperone mechanism of sHsps. In this review, we discuss some of these advances, with a focus on mammalian sHsp hetero-oligomerisation, the mechanism by which sHsps act as molecular chaperones to prevent both amorphous and fibrillar protein aggregation, and the role of post-translational modifications in sHsp chaperone function, particularly in the context of disease.
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Registered trials
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.