ArticleScientific reports2019
In vitro study of interaction of 17β-hydroxysteroid dehydrogenase type 10 and cyclophilin D and its potential implications for Alzheimer's disease.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- MAMs and Mitochondrial Quality Control: Overview and Their Role in Alzheimer's Disease.Neurochemical research · 2024Review
- Involvement of Type 10 17β-Hydroxysteroid Dehydrogenase in the Pathogenesis of Infantile Neurodegeneration and Alzheimer's Disease.International journal of molecular sciences · 2023Review
- Ionic Environment Affects Biomolecular Interactions of Amyloid-β: SPR Biosensor Study.International journal of molecular sciences · 2020Article
- Study of Biomolecular Interactions of Mitochondrial Proteins Related to Alzheimer's Disease: Toward Multi-Interaction Biomolecular Processes.Biomolecules · 2020Article
- Interactions of 17β-Hydroxysteroid Dehydrogenase Type 10 and Cyclophilin D in Alzheimer's Disease.Neurochemical research · 2020Article
- Senescence as an Amyloid Cascade: The Amyloid Senescence Hypothesis.Frontiers in cellular neuroscience · 2020Review
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4 authors.
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Abstract
In early stages of Alzheimer's disease (AD), amyloid-β (Aβ) accumulates in neuronal mitochondria where it interacts with a number of biomolecules including 17beta-hydroxysteroide dehydrogenase 10 (17β-HSD10) and cyclophilin D (cypD). It has been hypothesized that 17β-HSD10 interacts with cypD preventing it from opening mitochondrial permeability transition pores and that its regulation during AD may be affected by the accumulation of Aβ. In this work, we demonstrate for the first time that 17β-HSD10 and cypD form a stable complex in vitro. Furthermore, we show that factors, such as pH, ionic environment and the presence of Aβ, affect the ability of 17β-HSD10 to bind cypD. We demonstrate that K
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