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Solution conditions define morphological homogeneity of α-synuclein fibrils.
The intrinsically disordered human α-synuclein (αSyn) protein exhibits considerable heterogeneity in in vitro fibrillization reactions. Using atomic force microscopy (AFM) we show that depending onExpand
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Distinct Mechanisms Determine α-Synuclein Fibril Morphology during Growth and Maturation.
Amyloid polymorphs have become one of the focal points of molecular studies of neurodegenerative diseases like Parkinson's disease. Due to their distinct biochemical properties and prion-likeExpand
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Conformational Compatibility Is Essential for Heterologous Aggregation of α-Synuclein.
Under aggregation-prone conditions, soluble amyloidogenic protein monomers can self-assemble into fibrils or they can fibrillize on preformed fibrillar seeds (seeded aggregation). Seeded aggregationsExpand
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Polymorph-specific distribution of binding sites determines thioflavin-T fluorescence intensity in α-synuclein fibrils
Abstract Thioflavin-T (ThT) is the most commonly used fluorescent dye for following amyloid formation semi-quantitatively in vitro, specifically probing the fibrillar cross-β-sheet content. In recentExpand
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Disease Related Point Mutations and Solution Conditions Determine Fibrillization Behavior of α-Synuclein
In vitro fibrillization of proteins into amyloid fibrils provides critical insights into the factors influencing protein aggregation and has a key role in understanding the molecular basis of severalExpand