ArticlePloS one2011
The thermal structural transition of α-crystallin inhibits the heat induced self-aggregation.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 1 of them a synthesis that pooled it.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Pooled it
- The interaction of Cu(II) and Zn(II) with peptide fragment of HSPB1 and its analogs.Frontiers in molecular biosciences · 2025Article
- Binding of βInternational journal of molecular sciences · 2023Article
- Heat shock proteins and metal ions - Reaction or interaction?Computational and structural biotechnology journal · 2023Review
- Alpha-Crystallin Association with the Model of Human and Animal Eye Lens-Lipid Membranes is Modulated by Surface Hydrophobicity of Membranes.Current eye research · 2022Article
- Association of Alpha-Crystallin with Fiber Cell Plasma Membrane of the Eye Lens Accompanied by Light Scattering and Cataract Formation.Membranes · 2021Review
- Article
- Heat shock protein concentration and clarity of porcine lenses incubated at elevated temperatures.Molecular vision · 2016Article
- Whole-depth change in bovine zona pellucida biomechanics after fertilization: how relevant in hindering polyspermy?PloS one · 2012Article
- The thermal structural transition of alpha-crystallin modulates subunit interactions and increases protein solubility.PloS one · 2012Article
- Temperature-dependent structural and functional properties of a mutant (F71L) αA-crystallin: molecular basis for early onset of age-related cataract.FEBS letters · 2011Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α-crystallin, the major constituent of human lens, is a member of the heat-shock proteins family and it is known to have a quaternary structural transition at . The presence of calcium ions and/or temperature changes induce supramolecular self-aggregation, a process of relevance in the cataractogenesis. Here we investigate the potential effect of the bovine α-crystallin's structural transition on the self-aggregation process. Along all the temperatures investigated, aggregation proceeds by forming intermediate molecular assemblies that successively aggregate in clusters. The final morphology of the aggregates, above and below Tc, is similar, but the aggregation kinetics are completely different. The size of the intermediate molecular assemblies, and their repulsive energy barrier show a marked increase while crossing . Our results highlight the key role of heat modified form of α-crystallin in protecting from aggregation and preserving the transparency of the lens under hyperthermic conditions.
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Registered trials
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