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LonP1 chaperone-like activity is ATPase independent and is mediated by its N-domain

2026-05-08

Abstract excerpt

The mitochondrial Lon protease is essential for proteostasis through ATP-dependent proteolysis and suppression of protein aggregation through an unknown mechanism. Here we show in three independent aggregation systems that human Lon protease (LonP1) directly interacts with fibrillar aggregates to prevent further aggregation: LonP1 binds amyloid fibrils and inhibits their growth, independently of its protease and A...

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Identifiers and source

Literature Corpus work
1408cabd-bc68-503b-a60a-5ee20c0b9021
DOI
10.64898/2026.05.06.723147
Open publication

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LonP1 chaperone-like activity is ATPase independent and is mediated by its N-domainDOI 10.64898/2026.05.06.723147
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