ReviewDisease models & mechanisms2016
Model systems of protein-misfolding diseases reveal chaperone modifiers of proteotoxicity.
Review in Disease models & mechanisms, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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.
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Who cites it
27 citing papers in PubMed.
- Lysosomal targeting of liposomes with acidic pH and Cathepsin B induces protein aggregate clearance.Cell communication and signaling : CCS · 2025Article
- Computational Tools and Methods for the Study of Systemic Amyloidosis at the Clinical and Molecular Level.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Activation of the heat shock response as a therapeutic strategy for tau toxicity.Disease models & mechanisms · 2024Article
- Review
- Systems-level analyses of protein-protein interaction network dysfunctions via epichaperomics identify cancer-specific mechanisms of stress adaptation.Nature communications · 2023Article
- Hsp40 overexpression in pacemaker neurons delays circadian dysfunction in a Drosophila model of Huntington's disease.Disease models & mechanisms · 2022Article
- Modifier pathways in polyglutamine (PolyQ) diseases: from genetic screens to drug targets.Cellular and molecular life sciences : CMLS · 2022Review
- Protective Effect of Liposomal Epigallocatechin-Gallate in Experimental Gentamicin-Induced Hepatotoxicity.Antioxidants (Basel, Switzerland) · 2022Article
- The penalty of stress - Epichaperomes negatively reshaping the brain in neurodegenerative disorders.Journal of neurochemistry · 2021Review
- The functions and regulation of heat shock proteins; key orchestrators of proteostasis and the heat shock response.Archives of toxicology · 2021Review
- Molecular Stressors Engender Protein Connectivity Dysfunction through Aberrant N-Glycosylation of a Chaperone.Cell reports · 2020Article
- Cross organelle stress response disruption promotes gentamicin-induced proteotoxicity.Cell death & disease · 2020Article
- A Chemical Biology Approach to the Chaperome in Cancer-HSP90 and Beyond.Cold Spring Harbor perspectives in biology · 2020Review
- A functional unfolded protein response is required for chronological aging in Saccharomyces cerevisiae.Current genetics · 2020Article
- Chaperome Networks - Redundancy and Implications for Cancer Treatment.Advances in experimental medicine and biology · 2020Review
- Individualized management of genetic diversity in Niemann-Pick C1 through modulation of the Hsp70 chaperone system.Human molecular genetics · 2020Article
- Effects on the Caco-2 Cells of a Hypoglycemic Protein from Lupin Seeds in a Solution and Adsorbed on Polystyrene Nanoparticles to Mimic a Complex Food Matrix.Biomolecules · 2019Article
- Not quite the SSAme: unique roles for the yeast cytosolic Hsp70s.Current genetics · 2019Review
- Review
- Modulating protein-protein interaction networks in protein homeostasis.Current opinion in chemical biology · 2019Review
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chaperones and co-chaperones enable protein folding and degradation, safeguarding the proteome against proteotoxic stress. Chaperones display dynamic responses to exogenous and endogenous stressors and thus constitute a key component of the proteostasis network (PN), an intricately regulated network of quality control and repair pathways that cooperate to maintain cellular proteostasis. It has been hypothesized that aging leads to chronic stress on the proteome and that this could underlie many age-associated diseases such as neurodegeneration. Understanding the dynamics of chaperone function during aging and disease-related proteotoxic stress could reveal specific chaperone systems that fail to respond to protein misfolding. Through the use of suppressor and enhancer screens, key chaperones crucial for proteostasis maintenance have been identified in model organisms that express misfolded disease-related proteins. This review provides a literature-based analysis of these genetic studies and highlights prominent chaperone modifiers of proteotoxicity, which include the HSP70-HSP40 machine and small HSPs. Taken together, these studies in model systems can inform strategies for therapeutic regulation of chaperone functionality, to manage aging-related proteotoxic stress and to delay the onset of neurodegenerative diseases.
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