ArticleCell stress & chaperones2006
Differences in the chaperone-like activities of the four main small heat shock proteins of Drosophila melanogaster.
Article in Cell stress & chaperones, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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.
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
33 citing papers in PubMed, 97 citations in OpenAlex.
- HSP27 regulates force-coordinated DDR1 condensate disassembly and liquid-to-gel phase transition.Science advances · 2026Article
- A novel role for Hsc70-4 in blood cell differentiation inFrontiers in immunology · 2025Article
- Heat Shock Response and Heat Shock Proteins: Current Understanding and Future Opportunities in Human Diseases.International journal of molecular sciences · 2024Review
- Article
- Structural and functional properties of proteins interacting with small heat shock proteins.Cell stress & chaperones · 2020Review
- Transcriptional analysis of insect extreme freeze tolerance.Proceedings. Biological sciences · 2019Article
- Organelle aging: Lessons from model organisms.Journal of genetics and genomics = Yi chuan xue bao · 2019Review
- Recovery from supercooling, freezing, and cryopreservation stress in larvae of the drosophilid fly, Chymomyza costata.Scientific reports · 2018Article
- Identification and expression analysis of multiple small heat shock protein genes in spruce budworm, Choristoneura fumiferana (L.).Cell stress & chaperones · 2018Article
- Stress tolerance in diapausing embryos of Artemia franciscana is dependent on heat shock factor 1 (Hsf1).PloS one · 2018Article
- Maternal loading of a small heat shock protein increases embryo thermal tolerance inThe Journal of experimental biology · 2017Article
- Oligomerization and chaperone-like activity of Drosophila melanogaster small heat shock protein DmHsp27 and three arginine mutants in the alpha-crystallin domain.Cell stress & chaperones · 2017Article
- Oligomeric structure and chaperone-like activity of Drosophila melanogaster mitochondrial small heat shock protein Hsp22 and arginine mutants in the alpha-crystallin domain.Cell stress & chaperones · 2017Article
- Effect of N-terminal region of nuclear Drosophila melanogaster small heat shock protein DmHsp27 on function and quaternary structure.PloS one · 2017Article
- Specific protein homeostatic functions of small heat-shock proteins increase lifespan.Aging cell · 2016Article
- Article
- Drosophila melanogaster Hsp22: a mitochondrial small heat shock protein influencing the aging process.Frontiers in genetics · 2015Review
- Different anti-aggregation and pro-degradative functions of the members of the mammalian sHSP family in neurological disorders.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Review
- Comparative analysis on the expression of inducible HSPs in the silkworm, Bombyx mori.Molecular biology reports · 2012Article
- Heat shock proteins and Drosophila aging.Experimental gerontology · 2011Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Drosophila melanogaster family of small heat shock proteins (sHsps) is composed of 4 main members (Hsp22, Hsp23, Hsp26, and Hsp27) that display distinct intracellular localization and specific developmental patterns of expression in the absence of stress. In an attempt to determine their function, we have examined whether these 4 proteins have chaperone-like activity using various chaperone assays. Heat-induced aggregation of citrate synthase was decreased from 100 to 17 arbitrary units in the presence of Hsp22 and Hsp27 at a 1:1 molar ratio of sHsp to citrate synthase. A 5 M excess of Hsp23 and Hsp26 was required to obtain the same efficiency with either citrate synthase or luciferase as substrate. In an in vitro refolding assay with reticulocyte lysate, more than 50% of luciferase activity was recovered when heat denaturation was performed in the presence of Hsp22, 40% with Hsp27, and 30% with Hsp23 or Hsp26. These differences in luciferase reactivation efficiency seemed related to the ability of sHsps to bind their substrate at 42 degrees C, as revealed by sedimentation analysis of sHsp and luciferase on sucrose gradients. Therefore, the 4 main sHsps of Drosophila share the ability to prevent heat-induced protein aggregation and are able to maintain proteins in a refoldable state, although with different efficiencies. The functional reasons for their distinctive cell-specific pattern of expression could reflect the existence of defined substrates for each sHsp within the different intracellular compartments.
Indexed as
Identifiers
What OpenQuestion holds
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.