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- W2805870520 abstract "Proteins containing EF-hand helix-loop-helix-binding motifs play essential roles in calcium homeostasis and signaling pathways. These proteins have considerable structural and functional diversity by virtue of their cation-binding properties, and occur as either Ca2+-bound or Ca2+-free states with distinct aggregation propensities. That is the case among β-parvalbumins and S100 proteins, which under certain conditions undergo Ca2+-dependent self-assembly reactions with the formation of oligomers, amyloid-type aggregates and fibrils. These phenomena may be particularly relevant in human S100A6 protein and in fish Gad m 1 allergenic protein, which are implicated in human disease processes. Here, we describe detailed methods to generate and monitor the formation of amyloidogenic assemblies and aggregates of these two EF-hand proteins in vitro." @default.
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- W2805870520 date "2018-01-01" @default.
- W2805870520 modified "2023-09-30" @default.
- W2805870520 title "Preparation of Amyloidogenic Aggregates from EF-Hand β-Parvalbumin and S100 Proteins" @default.
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- W2805870520 doi "https://doi.org/10.1007/978-1-4939-7816-8_11" @default.
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