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Article

Key charged residues influence the amyloidogenic propensity of the helix-1 region of serum amyloid A.

Biochimica et biophysica acta. General subjects - 1 Nov 2024

Bilog Marvin, Vedad Jayson, Capadona Charisse, Profit Adam A, Desamero Ruel Z B

Abstract excerpt

Increased plasma levels of serum amyloid A (SAA), an acute-phase protein that is secreted in response to inflammation, may lead to the accumulation of amyloid in various organs thereby obstructing their functions. Severe cases can lead to a systemic disorder called AA amyloidosis. Previous studies suggest that the N-terminal helix is the most amyloidogenic region of SAA. Moreover, computational studies implicated...

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Source

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Identifiers

PMID: 39117048
DOI: 10.1016/j.bbagen.2024.130690
PMCID: PMC11547331

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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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