ReviewFrontiers in molecular biosciences2022
Insights on Human Small Heat Shock Proteins and Their Alterations in Diseases.
Review in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
What it found
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Who cites it
47 citing papers in PubMed, 70 citations in OpenAlex.
- Caenorhabditis elegans small heat-shock protein HSP-12.6 has a highly specialized protective function towards muscle thick filaments in vivo.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Article
- αB-crystallin elastin-like polypeptides for sustained ocular drug delivery.Drug delivery and translational research · 2026Article
- Intermolecular disulfide bond formation promotes Hsp42 higher-order assembly and shapes client selection in yeast.bioRxiv : the preprint server for biology · 2026Article
- Article
- Heat Shock Protein 27 in Radiation-Induced Trismus: Mechanistic Insights and a Hypothesis-Generating Framework.Biomedicines · 2026Review
- Small heat shock proteins with two alpha-crystallin domains: a new set of proteins in the earthworm Eisenia fetida with differential transcriptional responses to stressors.Environmental science and pollution research international · 2026Article
- Small heat shock proteins HspB1 and HspB5 differentially alter the condensation and aggregation of the TDP-43 low-complexity domain.Protein science : a publication of the Protein Society · 2026Article
- Cardiomyocyte-derived HSPB1 regulates TGF-β1 maturation and inhibits endothelial-to-mesenchymal transition in myocardial fibrosis.iScience · 2026Article
- C-terminal extension of HSPB6 in a family with myopathy and cataract.Human molecular genetics · 2026Article
- Heat shock proteins in male infertility: recent advances and clinical implications.Frontiers in cell and developmental biology · 2026Review
- Heat shock proteins at the crossroads of endosomal trafficking pathways.Cell biology and toxicology · 2025Review
- Article
- Quantitative spatial analysis of crystallin proteins in human lens epithelial cells.Scientific reports · 2025Article
- Comparative Characterization of Plasmodium falciparum Small Heat Shock Proteins and Their Inhibition by Quercetin (3,3',4',5,7-Pentahydroxyflavone).The protein journal · 2025Article
- The sertraline metabolite, desmethylsertraline, may be implicated in adverse outcomes reported after gestational sertraline use: insights from a study in zebrafish.Pharmacological reports : PR · 2025Article
- Overexpression of the human heat shock protein B1 alters obesity-related metabolic changes in a sex-dependent manner in a mouse model of metabolic syndrome.Biology of sex differences · 2025Article
- Novel HSPB8 mutations in severe early-onset myopathy with involvement of respiratory and cardiac muscles cause proteostasis defects in cell models.European journal of human genetics : EJHG · 2025Article
- Autophagy induction by piplartine ameliorates axonal degeneration caused by mutant HSPB1 and HSPB8 in Charcot-Marie-Tooth type 2 neuropathies.Autophagy · 2025Article
- The Spectrum of Small Heat Shock Protein B8 (International journal of molecular sciences · 2025Review
- Small Heat Shock Proteins: Protein Aggregation Amelioration and Neuro- and Age-Protective Roles.International journal of molecular sciences · 2025Review
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The family of the human small Heat Shock Proteins (HSPBs) consists of ten members of chaperones (HSPB1-HSPB10), characterized by a low molecular weight and capable of dimerization and oligomerization forming large homo- or hetero-complexes. All HSPBs possess a highly conserved centrally located α-crystallin domain and poorly conserved N- and C-terminal domains. The main feature of HSPBs is to exert cytoprotective functions by preserving proteostasis, assuring the structural maintenance of the cytoskeleton and acting in response to cellular stresses and apoptosis. HSPBs take part in cell homeostasis by acting as holdases, which is the ability to interact with a substrate preventing its aggregation. In addition, HSPBs cooperate in substrates refolding driven by other chaperones or, alternatively, promote substrate routing to degradation. Notably, while some HSPBs are ubiquitously expressed, others show peculiar tissue-specific expression. Cardiac muscle, skeletal muscle and neurons show high expression levels for a wide variety of HSPBs. Indeed, most of the mutations identified in HSPBs are associated to cardiomyopathies, myopathies, and motor neuropathies. Instead, mutations in HSPB4 and HSPB5, which are also expressed in lens, have been associated with cataract. Mutations of HSPBs family members encompass base substitutions, insertions, and deletions, resulting in single amino acid substitutions or in the generation of truncated or elongated proteins. This review will provide an updated overview of disease-related mutations in HSPBs focusing on the structural and biochemical effects of mutations and their functional consequences.
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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 Socratic graph.