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Article

Molecular simulation unravels the amyloidogenic misfolding of nascent ApoA1 protein, driven by deleterious point mutations occurring in between 170-178 hotspot region.

Journal of biomolecular structure & dynamics - 1 Jan 2022

Chandrasekhar G, Chandra Sekar P, Srinivasan E, Amarnath A, Pengyong H, Rajasekaran R

Abstract excerpt

Protein ApoA1 is extensively studied for its role in lipid metabolism. Its seedy dark side of amyloid formulation remains relatively understudied yet. Due to genetic mutations, the protein pathologically misshapes into its amyloid form that gets accumulated in various organs, including the heart. To contrive effective therapeutics against this debilitating congenital disorder, it is imperative to comprehend the...

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Identifiers

PMID: 34613891
DOI: 10.1080/07391102.2021.1986134

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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