ReviewCell stress & chaperones2020
Structural aspects of the human small heat shock proteins related to their functional activities.
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 27 papers.
What it found
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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, 47 citations in OpenAlex.
- 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 and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026Review
- 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
- Potential new biomarkers in pig saliva for differentiating between the effects of different conditions of mixing and density at pre-slaughter: A preliminary proteomicstudy.Animal welfare (South Mimms, England) · 2026Article
- Impact of N-terminal domain on the sHSP Lo18 function.Scientific reports · 2025Article
- Anti-aggregation Properties of the Mini-Peptides Derived from Alpha Crystallin Domain of the Small Heat Shock Protein, Tpv HSP 14.3.Molecular biotechnology · 2025Article
- Regulatory role of serine 59 in the oligomeric dynamics and chaperone function of αB-crystallin.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
- Small HSPs at the crossroad between protein aggregation, autophagy and unconventional secretion: clinical implications and potential therapeutic opportunities in the context of neurodegenerative diseases.Frontiers in cell and developmental biology · 2025Review
- Article
- α-Crystalline Domains and Intrinsically Disordered Regions Can Work in Parallel to Induce Accumulation of MBD6 at Chromocenters inEpigenomes · 2024Article
- Identification of Alternatively Spliced Novel Isoforms of Human HSPB8 Gene.The protein journal · 2024Article
- Review
- A method for the analysis of the oligomerization profile of the Huntington's disease-associated, aggregation-prone mutant huntingtin protein by isopycnic ultracentrifugation.Frontiers in molecular biosciences · 2024Article
- ACD15, ACD21, and SLN regulate the accumulation and mobility of MBD6 to silence genes and transposable elements.Science advances · 2023Article
- Mature human induced pluripotent stem cell-derived cardiomyocytes promote angiogenesis through alpha-B crystallin.Stem cell research & therapy · 2023Article
- Homo-oxidized HSPB1 protects H9c2 cells against oxidative stress via activation of KEAP1/NRF2 signaling pathway.iScience · 2023Article
- HSPB8 frameshift mutant aggregates weaken chaperone-assisted selective autophagy in neuromyopathies.Autophagy · 2023Article
- The HSPB1-p62/SQSTM1 functional complex regulates the unconventional secretion and transcellular spreading of the HD-associated mutant huntingtin protein.Human molecular genetics · 2023Article
- Evaluation of the Small Heat Shock Protein Family MembersInternational journal of molecular sciences · 2023Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Small heat shock proteins function as chaperones by binding unfolding substrate proteins in an ATP-independent manner to keep them in a folding-competent state and to prevent irreversible aggregation. They play crucial roles in diseases that are characterized by protein aggregation, such as neurodegenerative and neuromuscular diseases, but are also involved in cataract, cancer, and congenital disorders. For this reason, these proteins are interesting therapeutic targets for finding molecules that could affect the chaperone activity or compensate specific mutations. This review will give an overview of the available knowledge on the structural complexity of human small heat shock proteins, which may aid in the search for such therapeutic molecules.
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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.