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Article

Polymorphism in disease-related apolipoprotein C-II amyloid fibrils: a structural model for rod-like fibrils.

The FEBS journal - 1 Aug 2018

Zlatic Courtney O, Mao Yu, Todorova Nevena, Mok Yee-Foong, Howlett Geoffrey J, Yarovsky Irene, Gooley Paul R, Griffin Michael D W

Abstract excerpt

Human apolipoprotein (apo) C-II is one of several plasma apolipoproteins that form amyloid deposits in vivo and is an independent risk factor for cardiovascular disease. Lipid-free apoC-II readily self-assembles into twisted-ribbon amyloid fibrils but forms straight, rod-like amyloid fibrils in the presence of low concentrations of micellar phospholipids. Charge mutations exerted significantly different effects...

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Identifiers

PMID: 29791776
DOI: 10.1111/febs.14517

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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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