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Article

Decreased amyloidogenicity caused by mutational modulation of surface properties of the immunoglobulin light chain BRE variable domain.

Biochemistry - 12 Aug 2014

Kobayashi Yuta, Tsutsumi Hirotaka, Abe Tetsuyuki, Ikeda Kyohei, Tashiro Yuki, Unzai Satoru, Kamikubo Hironari, Kataoka Mikio, Hiroaki Hidekazu, Hamada Daizo

Abstract excerpt

Amyloid formation by immunoglobulin light chain (LC) proteins is associated with amyloid light chain (AL) amyloidosis. Destabilization of the native state of the variable domain of the LC (VL) is known to be one of the critical factors in promoting the formation of amyloid fibrils. However, determining the key residues involved in this destabilization remains challenging, because of the existence of a number of...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 25062800
DOI: 10.1021/bi5007892

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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