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ATF6 Activation Reduces Amyloidogenic Transthyretin Secretion Through Increased Interactions with Endoplasmic Reticulum Proteostasis Factors

2022-04-13

Abstract excerpt

<h4>SUMMARY</h4> The extracellular aggregation of destabilized transthyretin (TTR) variants is implicated in the onset and pathogenesis of familial TTR-related amyloid diseases. One strategy to reduce toxic, extracellular aggregation of TTR is to decrease the population of aggregation-prone protein secreted from mammalian cells. Stress-independent activation of the unfolded protein response (UPR)-associated trans...

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Literature Corpus work
b915ad13-1750-5694-8df9-84ed10eaa42d
DOI
10.1101/2022.04.13.488200
Open publication

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ATF6 Activation Reduces Amyloidogenic Transthyretin Secretion Through Increased Interactions with Endoplasmic Reticulum Proteostasis FactorsDOI 10.1101/2022.04.13.488200
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