ArticleCell stress & chaperones2014
Effect of disulfide crosslinking on thermal transitions and chaperone-like activity of human small heat shock protein HspB1.
Article in Cell stress & chaperones, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Review
- Review
- Homo-oxidized HSPB1 protects H9c2 cells against oxidative stress via activation of KEAP1/NRF2 signaling pathway.iScience · 2023Article
- Insights on Human Small Heat Shock Proteins and Their Alterations in Diseases.Frontiers in molecular biosciences · 2022Review
- Oligomeric Structural Transition of HspB1 from Chinese Hamster.International journal of molecular sciences · 2021Article
- AlphaB-crystallin and breast cancer: role and possible therapeutic strategies.Cell stress & chaperones · 2021Review
- Bmal1 Regulates the Redox Rhythm of HSPB1, and Homooxidized HSPB1 Attenuates the Oxidative Stress Injury of Cardiomyocytes.Oxidative medicine and cellular longevity · 2021Article
- Neuromuscular Diseases Due to Chaperone Mutations: A Review and Some New Results.International journal of molecular sciences · 2020Review
- Functional and structural characterization of HspB1/Hsp27 from Chinese hamster ovary cells.FEBS open bio · 2019Article
- Local unfolding of the HSP27 monomer regulates chaperone activity.Nature communications · 2019Article
- The role of αB-crystallin in skeletal and cardiac muscle tissues.Cell stress & chaperones · 2018Review
- The Chaperone Activity and Substrate Spectrum of Human Small Heat Shock Proteins.The Journal of biological chemistry · 2017Article
- Structure of the α-crystallin domain from the redox-sensitive chaperone, HSPB1.Journal of biomolecular NMR · 2015Article
- A first line of stress defense: small heat shock proteins and their function in protein homeostasis.Journal of molecular biology · 2015Review
- Article
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5 authors.
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Abstract
Temperature-induced conformational changes of reduced and oxidized HspB1 crosslinked by disulfide bond between single Cys137 of neighboring monomers were analyzed by means of different techniques. Heating of reduced HspB1 was accompanied by irreversible changes of Trp fluorescence, whereas oxidized HspB1 underwent completely reversible changes of fluorescence. Increase of the temperature in the range of 20-70 °C was accompanied by self-association of both reduced and oxidized protein. Further increase of the temperature led to formation of heterogeneous mixture of large self-associated complexes of reduced HspB1 and to formation of smaller and less heterogeneous complexes of oxidized HspB1. Heat-induced changes of oligomeric state of reduced HspB1 were only partially reversible, whereas the corresponding changes of oligomeric state of oxidized HspB1 were almost completely reversible. Oxidation resulted in decrease of chaperone-like activity of HspB1. It is concluded that oxidative stress, inducing formation of disulfide bond, can affect stability and conformational mobility of human HspB1.
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