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Article

Dimeric transthyretin variant assembles into spherical neurotoxins.

Biochemistry - 8 Mar 2005

Matsubara Kimiaki, Mizuguchi Mineyuki, Igarashi Kouhei, Shinohara Yoshinori, Takeuchi Makoto, Matsuura Atsushi, Saitoh Takayuki, Mori Yoshihiro, Shinoda Hiroyuki, Kawano Keiichi

Abstract excerpt

Familial amyloidotic polyneuropathy is a hereditary autosomal-dominant disease in which the deposited transthyretin fibrils are derived from amyloidogenic mutation. We investigated structure and stability of a human Ser112Ile transthyretin variant and showed that the Ser112Ile variant exists as a dimer having nonnative tertiary structure at physiological pH. In addition, the dimeric Ser112Ile assembles into a...

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PMID: 15736938
DOI: 10.1021/bi048838c

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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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