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Article

Competition between inside-out unfolding and pathogenic aggregation in an amyloid-forming β-propeller.

Nature communications - 2 Jan 2024

Saccuzzo Emily G, Mebrat Mubark D, Scelsi Hailee F, Kim Minjoo, Ma Minh Thu, Su Xinya, Hill Shannon E, Rheaume Elisa, Li Renhao, Torres Matthew P, Gumbart James C, Van Horn Wade D, Lieberman Raquel L

Abstract excerpt

Studies of folded-to-misfolded transitions using model protein systems reveal a range of unfolding needed for exposure of amyloid-prone regions for subsequent fibrillization. Here, we probe the relationship between unfolding and aggregation for glaucoma-associated myocilin. Mutations within the olfactomedin domain of myocilin (OLF) cause a gain-of-function, namely cytotoxic intracellular aggregation, which...

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Identifiers

PMID: 38168102
DOI: 10.1038/s41467-023-44479-2
PMCID: PMC10762032

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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