International journal of biological macromoleculesPhosphorylationIntrinsically Disordered ProteinsHumansProtein AggregatesDNA-Binding Proteins
Unveiling the effect of phosphorylation and phosphomimetics on the structural and aggregation properties of the amyloidogenic intrinsically disordered protein DPF3a.
Tanguy Leyder, Julien Mignon, Emma Bongiovanni, Quentin Machiels, Jehan Waeytens, Vincent Raussens, Antonio Monari, Denis Mottet, Catherine Michaux
Published: 202610.1016/j.ijbiomac.2025.149393
Abstract
DPF3a is a human epigenetic regulator involved in chromatin remodelling, cell division, and ciliogenesis. This protein is deregulated in various cancers and neurodegenerative diseases. In our previous work, DPF3a has been described as an amyloidogeni…
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