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• W2593248800 abstract "Abstract PMEL is a pigment cell protein that forms physiological amyloid in melanosomes. Many amyloids and/or their oligomeric precursors are toxic, causing or contributing to severe, incurable diseases including Alzheimer’s and prion diseases. Striking similarities in intracellular formation pathways between PMEL and various pathological amyloids including Aβ and PrP Sc suggest PMEL is an excellent model system to study endocytic amyloid. Learning how PMEL fibrils assemble without apparent toxicity may help developing novel therapies for amyloid diseases. Here we identify the critical PMEL domain that forms the melanosomal amyloid core (CAF). An unbiased alanine-scanning screen covering the entire region combined with quantitative electron microscopy analysis of the full set of mutants uncovers numerous essential residues. Many of these rely on aromaticity for function suggesting a role for π-stacking in melanosomal amyloid assembly. Various mutants are defective in amyloid nucleation. This extensive data set informs the first structural model of the CAF and provides insights into how the melanosomal amyloid core forms." @default.
• W2593248800 created "2017-03-16" @default.
• W2593248800 creator A5000054664 @default.
• W2593248800 creator A5071481483 @default.
• W2593248800 creator A5079978421 @default.
• W2593248800 creator A5089839962 @default.
• W2593248800 date "2017-03-08" @default.
• W2593248800 modified "2023-10-18" @default.
• W2593248800 title "Melanosomal formation of PMEL core amyloid is driven by aromatic residues" @default.
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• W2593248800 doi "https://doi.org/10.1038/srep44064" @default.
• W2593248800 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5341037" @default.
• W2593248800 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28272432" @default.
• W2593248800 hasPublicationYear "2017" @default.
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