ArticleAging cell2016
Specific protein homeostatic functions of small heat-shock proteins increase lifespan.
Article in Aging cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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
27 citing papers in PubMed, 55 citations in OpenAlex.
- Review
- Reserpine prolongs lifespan but compromises locomotion and heat-stress resilience in Drosophila melanogaster.npj aging · 2026Article
- Small Heat Shock Proteins: Protein Aggregation Amelioration and Neuro- and Age-Protective Roles.International journal of molecular sciences · 2025Review
- Multiple factors contribute to female dominance in migratory bioflows.Open biology · 2025Article
- A short-lived fish with long-lasting effects: hallmarks of aging inFrontiers in aging · 2025Review
- Egg Protein Compositions over Embryonic Development inAnimals : an open access journal from MDPI · 2024Article
- The C. elegans Myc-family of transcription factors coordinate a dynamic adaptive response to dietary restriction.GeroScience · 2024Article
- Article
- Ageing in the brain: mechanisms and rejuvenating strategies.Cellular and molecular life sciences : CMLS · 2023Review
- Long ant life span is maintained by a unique heat shock factor.Genes & development · 2023Article
- Heat Shock Proteins in Tooth Development and Injury Repair.International journal of molecular sciences · 2023Review
- The cytoprotective sequestration activity of small heat shock proteins is evolutionarily conserved.The Journal of cell biology · 2022Article
- Article
- The transcriptional response to oxidative stress is independent of stress-granule formation.Molecular biology of the cell · 2022Article
- Chromatin accessibility profiling provides insights into larval cuticle color and adult longevity in butterflies.Zoological research · 2021Article
- Ovary Proteome Analysis Reveals RH36 Regulates Reproduction via Vitellin Uptake Mediated by HSP70 Protein in Hard Ticks.Frontiers in cellular and infection microbiology · 2020Article
- Transcriptional analysis of insect extreme freeze tolerance.Proceedings. Biological sciences · 2019Article
- Quantitative iTRAQ-based proteomic analysis of differentially expressed proteins in aging in human and monkey.BMC genomics · 2019Article
- Molecular characterization, tissue-specific expression, and RNA knockdown of the putative heat shock cognate 70 protein from Rhipicephalus haemaphysaloides.Parasitology research · 2019Article
- Small Heat Shock Proteins, Big Impact on Protein Aggregation in Neurodegenerative Disease.Frontiers in pharmacology · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During aging, oxidized, misfolded, and aggregated proteins accumulate in cells, while the capacity to deal with protein damage declines severely. To cope with the toxicity of damaged proteins, cells rely on protein quality control networks, in particular proteins belonging to the family of heat-shock proteins (HSPs). As safeguards of the cellular proteome, HSPs assist in protein folding and prevent accumulation of damaged, misfolded proteins. Here, we compared the capacity of all Drosophila melanogaster small HSP family members for their ability to assist in refolding stress-denatured substrates and/or to prevent aggregation of disease-associated misfolded proteins. We identified CG14207 as a novel and potent small HSP member that exclusively assisted in HSP70-dependent refolding of stress-denatured proteins. Furthermore, we report that HSP67BC, which has no role in protein refolding, was the most effective small HSP preventing toxic protein aggregation in an HSP70-independent manner. Importantly, overexpression of both CG14207 and HSP67BC in Drosophila leads to a mild increase in lifespan, demonstrating that increased levels of functionally diverse small HSPs can promote longevity in vivo.
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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.