It exploits the highly significant correlation between the scores obtained from a parameterized linear function, that balances the contribution of both PrLDs composition and amyloid propensity [ 13 ], and the intracellular aggregation of hnRNPA2 variants; the unique prion-like protein for which a large set of mutations, both natural and artificial have been experimentally validated (Fig. 1 a).
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AMYCO: evaluation of mutational impact on prion-like proteins aggregation propensity.
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