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Article

Mutations can cause light chains to be too stable or too unstable to form amyloid fibrils.

Protein science : a publication of the Protein Society - 1 Nov 2015

Marin-Argany Marta, Güell-Bosch Jofre, Blancas-Mejía Luis M, Villegas Sandra, Ramirez-Alvarado Marina

Abstract excerpt

Light chain (AL) amyloidosis is an incurable human disease, where the amyloid precursor is a misfolding-prone immunoglobulin light-chain. Here, we identify the role of somatic mutations in the structure, stability and in vitro fibril formation for an amyloidogenic AL-12 protein by restoring four nonconservative mutations to their germline (wild-type) sequence. The single restorative mutations do not affect...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 26300552
DOI: 10.1002/pro.2790
PMCID: PMC4622216

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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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