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Article

Heat-induced native dimerization prevents amyloid formation by variable domain from immunoglobulin light-chain REI.

The FEBS journal - 1 Sept 2017

Nawata Marina, Tsutsumi Hirotaka, Kobayashi Yuta, Unzai Satoru, Mine Shouhei, Nakamura Tsutomu, Uegaki Koichi, Kamikubo Hironari, Kataoka Mikio, Hamada Daizo

Abstract excerpt

Amyloid light-chain (AL) amyloidosis is a protein-misfolding disease characterized by accumulation of immunoglobulin light chains (LCs) into amyloid fibrils. Dimerization of a full length or variable domain (VL ) of LC serves to stabilize the native state and prevent the formation of amyloid fibrils. We here analyzed the thermodynamic properties of dimerization and unfolding reactions by nonamyloidogenic VL from...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 28736891
DOI: 10.1111/febs.14181

Provenance

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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