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Charge and charge-pair mutations alter the rate of assembly and structural properties of apolipoprotein C-II amyloid fibrils.

Biochemistry - 17 Feb 2015

Mao Yu, Teoh Chai Lean, Yang Shuo, Zlatic Courtney O, Rosenes Zachary K, Gooley Paul R, Howlett Geoffrey J, Griffin Michael D W

Abstract excerpt

The misfolding, aggregation, and accumulation of proteins as amyloid fibrils is a defining characteristic of several debilitating diseases. Human apolipoprotein C-II (apoC-II) amyloid fibrils are representative of the fibrils formed by a number of plasma apolipoproteins implicated in amyloid-related disease. Previous structural analyses identified a buried charge pair between residues K30 and D69 within apoC-II...

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PMID: 25609257
DOI: 10.1021/bi5014535

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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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