ArticleMolecular biotechnology2016
Trehalose-Induced Structural Transition Accelerates Aggregation of α-Synuclein.
Article in Molecular biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed.
- In situ analysis of osmolyte mechanisms of proteome thermal stabilization.Nature chemical biology · 2024Article
- Natural and engineered mediators of desiccation tolerance stabilize Human Blood Clotting Factor VIII in a dry state.Scientific reports · 2023Article
- Protein Fibrillation under Crowded Conditions.Biomolecules · 2022Review
- Polyol and sugar osmolytes can shorten protein hydrogen bonds to modulate function.Communications biology · 2020Article
- Trehalose as a promising therapeutic candidate for the treatment of Parkinson's disease.British journal of pharmacology · 2019Review
- Heat shock promotes inclusion body formation of mutant huntingtin (mHtt) and alleviates mHtt-induced transcription factor dysfunction.The Journal of biological chemistry · 2018Article
- Osmolyte Induced Tumorigenesis and Metastasis: Interactions With Intrinsically Disordered Proteins.Frontiers in oncology · 2018Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fibrillation of α-synuclein proceeds through distinct stages, with oligomers combining to form the seed or the nucleus, followed by exponential and saturation phases. Osmolytes are considered to act as protein stabilizers by virtue of their ability to inhibit protein aggregation. Trehalose, a non-reducing disaccharide which is conventionally used as a stabilizer, was found to order α-synuclein, a natively disordered protein, into a non-native conformation such that the protein folding pathway is driven towards aggregation. Thus, by ordering the pathway intermediates, the osmolyte trehalose exerts variable effect on an intrinsically disordered protein when compared with its effect on natively folded proteins.
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Registered trials
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