ReviewNature reviews. Molecular cell biology2013
Chaperone machines for protein folding, unfolding and disaggregation.
Review in Nature reviews. Molecular cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 573 papers.
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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.
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Who cites it
573 citing papers in PubMed.
- Polyphenols at the Helm: Excited State Photophysics and Mechanistic Insights Into Protein-Aggregation Inhibition Through Ultrafast Studies.Chemistry, an Asian journal · 2026Article
- Conserved HSP60 structure with lineage- and context-specific regulation in cnidarians.Life science alliance · 2026Article
- Sigma-1 Expression in Chronic Mouse Models of Temporal Lobe Epilepsy.Molecular neurobiology · 2026Article
- YTHDC1 functions as a molecular chaperone to suppress ALS-linked hnRNPA1 mutants from aggregation.Nature communications · 2026Article
- GWAS-informed genomic selection for cold tolerance in pepper (Capsicum annuum L.).BMC plant biology · 2026Article
- Repair of DNA and protein damages caused by formaldehyde improves methanol assimilation.Fundamental research · 2026Article
- Overcoming cellular secretion bottlenecks: advanced secretion engineering and molecular tailoring for next-generation microbial α-amylases with enhanced industrial performance.World journal of microbiology & biotechnology · 2026Review
- Structural and immunogenic evaluation of silk proteins from Bombyx mori using advanced bioinformatics and deep learning for biomaterials applications.Journal, genetic engineering & biotechnology · 2026Article
- Enhancing soluble expression and purification of a bispecific scFv antibody inResearch in pharmaceutical sciences · 2026Article
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- Placental Heat Shock Protein (HSP) Expression in Fetal Growth Restriction (FGR) Pregnancies: A Case-Control Immunohistochemistry Study.International journal of molecular sciences · 2026Article
- Distinct phosphorylation mechanisms as dynamic switches for Hsp90 regulation.Nature communications · 2026Article
- Exploring the Holdase Activity of Supramolecular Chaperones with Amyloid-Forming Peptides and Insulin.Biomacromolecules · 2026Article
- Heat Shock Proteins as Targets for Cancer Therapeutics.Journal of clinical medicine · 2026Review
- ATP modulates holdase activity of fungal and human 110-kilodalton heat shock proteins to promote protein folding.Protein science : a publication of the Protein Society · 2026Article
- Evaluation of Hsp70 and Apoptotic Markers in Canine Cutaneous Lupus Erythematosus.Veterinary sciences · 2026Article
- How Does Genetic Information Enable Life?Bulletin of mathematical biology · 2026Article
- Transgenerational effects of heat shock on gene regulation and fitness-related traits in natural Drosophila populations.Molecular biology and evolution · 2026Article
- Chaperonin in health and disease.Molecular biomedicine · 2026Review
513 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
1 author.
Funding
Abstract
Molecular chaperones are diverse families of multidomain proteins that have evolved to assist nascent proteins to reach their native fold, protect subunits from heat shock during the assembly of complexes, prevent protein aggregation or mediate targeted unfolding and disassembly. Their increased expression in response to stress is a key factor in the health of the cell and longevity of an organism. Unlike enzymes with their precise and finely tuned active sites, chaperones are heavy-duty molecular machines that operate on a wide range of substrates. The structural basis of their mechanism of action is being unravelled (in particular for the heat shock proteins HSP60, HSP70, HSP90 and HSP100) and typically involves massive displacements of 20-30 kDa domains over distances of 20-50 Å and rotations of up to 100°.
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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.