ReviewCell stress & chaperones2020
Mutations in HspB1 and hereditary neuropathies.
Review in Cell stress & chaperones, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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
17 citing papers in PubMed, 21 citations in OpenAlex.
- Review
- Heat shock proteins in male infertility: recent advances and clinical implications.Frontiers in cell and developmental biology · 2026Review
- Navigating the landscape of protein folding and proteostasis: from molecular chaperones to therapeutic innovations.Signal transduction and targeted therapy · 2025Review
- HspB5 Chaperone Structure and Activity Are Modulated by Chemical-Scale Interactions in the ACD Dimer Interface.International journal of molecular sciences · 2023Article
- Review
- Human HspB1, HspB3, HspB5 and HspB8: Shaping these disease factors during vertebrate evolution.Cell stress & chaperones · 2022Article
- The role of BAG3 in dilated cardiomyopathy and its association with Charcot-Marie-Tooth disease type 2.Acta myologica : myopathies and cardiomyopathies : official journal of the Mediterranean Society of Myology · 2022Review
- Association of SORD mutation with autosomal recessive asymmetric distal hereditary motor neuropathy.BMC medical genomics · 2022Article
- Insights Into the Role of Heat Shock Protein 27 in the Development of Neurodegeneration.Frontiers in molecular neuroscience · 2022Review
- Brain transcriptomic profiling reveals common alterations across neurodegenerative and psychiatric disorders.Computational and structural biotechnology journal · 2022Article
- Bioinformatics and System Biology Techniques to Determine Biomolecular Signatures and Pathways of Prion Disorder.Bioinformatics and biology insights · 2022Article
- The chaperone HSPB1 prepares protein aggregates for resolubilization by HSP70.Scientific reports · 2021Article
- Early and late manifestations of neuropathy due to HSPB1 mutation in the Jewish Iranian population.Annals of clinical and translational neurology · 2021Article
- Small Hsps as Therapeutic Targets of Cystic Fibrosis Transmembrane Conductance Regulator Protein.International journal of molecular sciences · 2021Review
- A weakened interface in the P182L variant of HSP27 associated with severe Charcot-Marie-Tooth neuropathy causes aberrant binding to interacting proteins.The EMBO journal · 2021Article
- [Rare variants of HSPB1 are probably associated with amyotrophic lateral sclerosis].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2021Article
- Homeostatic Roles of the Proteostasis Network in Dendrites.Frontiers in cellular neuroscience · 2020Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Charcot-Marie-Tooth (CMT) disease is major hereditary neuropathy. CMT has been linked to mutations in a range of proteins, including the small heat shock protein HspB1. Here we review the properties of several HspB1 mutants associated with CMT. In vitro, mutations in the N-terminal domain lead to a formation of larger HspB1 oligomers when compared with the wild-type (WT) protein. These mutants are resistant to phosphorylation-induced dissociation and reveal lower chaperone-like activity than the WT on a range of model substrates. Mutations in the α-crystallin domain lead to the formation of yet larger HspB1 oligomers tending to dissociate at low protein concentration and having variable chaperone-like activity. Mutations in the conservative IPV motif within the C-terminal domain induce the formation of very large oligomers with low chaperone-like activity. Most mutants interact with a partner small heat shock protein, HspB6, in a manner different from that of the WT protein. The link between the altered physico-chemical properties and the pathological CMT phenotype is a subject of discussion. Certain HspB1 mutations appear to have an effect on cytoskeletal elements such as intermediate filaments and/or microtubules, and by this means damage the axonal transport. In addition, mutations of HspB1 can affect the metabolism in astroglia and indirectly modulate the viability of motor neurons. While the mechanisms of pathological mutations in HspB1 are likely to vary greatly across different mutations, further in vitro and in vivo studies are required for a better understanding of the CMT disease at molecular level.
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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.