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- W2085642283 abstract "Most amyloids are pathological. Pmel17 is a functional amyloid, promoting melanin deposition and possibly protecting cells from adverse effects of the reactive groups that comprise this important pigment. Here, we show that at the mildly acidic pH (4 - 5.5) typical of melanosomes, organelles where melanin is synthesized, the repeat domain (RPT) of human Pmel17 can form amyloid in vitro. Combined with the known presence of RPT in the melanosomal filaments and the requirement of this domain for fibril formation, we propose that RPT may constitute the amyloid core in vivo. While most of the amino acid sequence of Pmel17 is highly conserved across a broad range of vertebrates, the RPT domain length and sequence varies. To address RPT aggregation propensities, we have investigated mouse and zebrafish sequences as well as a smaller truncated variant of human Pmel17. Although there is no sequence conservation amongst RPT domains, amyloid formation at acidic pH is preserved." @default.
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- W2085642283 date "2011-02-01" @default.
- W2085642283 modified "2023-09-26" @default.
- W2085642283 title "The Repeat Domain of Pmel17 Orthologs Form Amyloid Fibrils at the Acidic Melanosomal pH" @default.
- W2085642283 doi "https://doi.org/10.1016/j.bpj.2010.12.3150" @default.
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