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Article

The congenital APOA1 K107del mutation disrupts the lipid-free conformation of monomeric APOA1 and impairs oligomerization.

Journal of lipid research - 1 Dec 2025

Díaz Ludovico Ivo, Gonzalez Marina C, Garda Horacio A, Vázquez Romina F, Maté Sabina, Tricerri María A, Ramella Nahuel A, Bedi Shimpi, Morris Jamie, Street Scott E, Geh Esmond, Clair Geremy C, Davidson W Sean, Melchior John T

Abstract excerpt

Apolipoprotein A-I (APOA1) oligomerization is thought to be essential for high-density lipoprotein (HDL) formation and metabolism. Naturally occurring mutations can disrupt normal APOA1 folding and self-association, leading to dysfunctional HDL formation and cardiovascular disease. The congenital APOA1 variant p.K131del (APOA1K107del) has been associated with cardiovascular pathologies such as low HDL-cholesterol...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 41167396
DOI: 10.1016/j.jlr.2025.100929
PMCID: PMC12686907

Genes

APOA1

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

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