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Manipulating the aggregation activity of human prion-like proteins

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Pages 323-331 | Received 24 May 2017, Accepted 10 Jul 2017, Published online: 12 Oct 2017

Figures & data

FIGURE 1. Intracellular processes commonly affecting PrLD aggregation. Mutations, changes in protein concentration, or post-translational modifications in PrLDs can affect protein aggregation by altering intrinsic aggregation propensity (1); liquid-liquid phase separation/stress granule dynamics (2); conversion of granules to a pathological state (3); organism-, tissue-, or compartment-specific intermolecular interactions (4); proteasome-mediated degradation (5); or nucleocytoplasmic transport (6).

FIGURE 1. Intracellular processes commonly affecting PrLD aggregation. Mutations, changes in protein concentration, or post-translational modifications in PrLDs can affect protein aggregation by altering intrinsic aggregation propensity (1); liquid-liquid phase separation/stress granule dynamics (2); conversion of granules to a pathological state (3); organism-, tissue-, or compartment-specific intermolecular interactions (4); proteasome-mediated degradation (5); or nucleocytoplasmic transport (6).

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