ArticleCell stress & chaperones2017
The functional roles of the unstructured N- and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins.
Article in Cell stress & chaperones, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 54 citations in OpenAlex.
- Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026Review
- High density-lipoprotein regulates liquid-liquid phase separation of heat shock protein β-1 by lncRNA HDRACA to affect vascular inflammation and atherosclerosis.International journal of biological sciences · 2026Article
- TXSelect: A multi-task learning model to identify secretory effectors.PLoS computational biology · 2025Article
- Mini-αA-crystallin protects a client lens protein from catastrophic aggregation due to heat stress.Protein science : a publication of the Protein Society · 2025Article
- The inhibitory action of the chaperone BRICHOS against the α-Synuclein secondary nucleation pathway.Nature communications · 2024Article
- Aquaporin-0-protein interactions elucidated by crosslinking mass spectrometry.Biochemical and biophysical research communications · 2024Article
- The major inducible small heat shock protein HSP20-3 in the tardigrade Ramazzottius varieornatus forms filament-like structures and is an active chaperone.Cell stress & chaperones · 2024Article
- HSPB8 frameshift mutant aggregates weaken chaperone-assisted selective autophagy in neuromyopathies.Autophagy · 2023Article
- Heat shock proteins and metal ions - Reaction or interaction?Computational and structural biotechnology journal · 2023Review
- The Common Bean Small Heat Shock Protein Nodulin 22 fromMolecules (Basel, Switzerland) · 2022Article
- Effects of Molecular Crowding and Betaine on HSPB5 Interactions, with Target Proteins Differing in the Quaternary Structure and Aggregation Mechanism.International journal of molecular sciences · 2022Article
- Article
- Insights Into the Role of Heat Shock Protein 27 in the Development of Neurodegeneration.Frontiers in molecular neuroscience · 2022Review
- Whole-exome sequencing identification of a recurrentExperimental and therapeutic medicine · 2021Article
- Effect of Structural Changes Induced by Deletion ofInternational journal of molecular sciences · 2021Article
- α-Crystallins in the Vertebrate Eye Lens: Complex Oligomers and Molecular Chaperones.Annual review of physical chemistry · 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
- The Effect of Oxidized Dopamine on the Structure and Molecular Chaperone Function of the Small Heat-Shock Proteins, αB-Crystallin and Hsp27.International journal of molecular sciences · 2021Article
- Chaperone-Like Activity of HSPB5: The Effects of Quaternary Structure Dynamics and Crowding.International journal of molecular sciences · 2020Article
- Structural aspects of the human small heat shock proteins related to their functional activities.Cell stress & chaperones · 2020Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Small heat-shock proteins (sHsps), such as αB-crystallin, are one of the major classes of molecular chaperone proteins. In vivo, under conditions of cellular stress, sHsps are the principal defence proteins that prevent large-scale protein aggregation. Progress in determining the structure of sHsps has been significant recently, particularly in relation to the conserved, central and β-sheet structured α-crystallin domain (ACD). However, an understanding of the structure and functional roles of the N- and C-terminal flanking regions has proved elusive mainly because of their unstructured and dynamic nature. In this paper, we propose functional roles for both flanking regions, based around three properties: (i) they act in a localised crowding manner to regulate interactions with target proteins during chaperone action, (ii) they protect the ACD from deleterious amyloid fibril formation and (iii) the flexibility of these regions, particularly at the extreme C-terminus in mammalian sHsps, provides solubility for sHsps under chaperone and non-chaperone conditions. In the eye lens, these properties are highly relevant as the crystallin proteins, in particular the two sHsps αA- and αB-crystallin, are present at very high concentrations.
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