Amyloidogenic 60–71 deletion/ValThr insertion mutation of apolipoprotein A-I generates a new aggrega...
Amyloidogenic 60–71 deletion/ValThr insertion mutation of apolipoprotein A-I generates a new aggregation-prone segment that promotes nucleation through entropic effects
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London: Nature Publishing Group UK
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English
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London: Nature Publishing Group UK
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The N-terminal fragment of apolipoprotein A-I (apoA-I), comprising residues 1–83, contains three segments prone to aggregation: residues 14–22, 53–58, and 67–72. We previously demonstrated that residues 14–22 are critical in apoA-I fibril formation while residues 53–58 entropically drove the nucleation process. Here, we investigated the impact of a...
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Amyloidogenic 60–71 deletion/ValThr insertion mutation of apolipoprotein A-I generates a new aggregation-prone segment that promotes nucleation through entropic effects
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TN_cdi_doaj_primary_oai_doaj_org_article_21de3cc37573420ebf053c4f5b2d5d94
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_21de3cc37573420ebf053c4f5b2d5d94
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2045-2322
E-ISSN
2045-2322
DOI
10.1038/s41598-023-45803-y
