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Article

Biophysical analyses of the transthyretin variants, Tyr114His and Tyr116Ser, associated with familial amyloidotic polyneuropathy.

Biochemistry - 30 Dec 2003

Shinohara Yoshinori, Mizuguchi Mineyuki, Matsubara Kimiaki, Takeuchi Makoto, Matsuura Atsushi, Aoki Takahiro, Igarashi Kouhei, Nagadome Hatsumi, Terada Yoshihiro, Kawano Keiichi

Abstract excerpt

The familial amyloidotic polyneuropathy is strictly associated with point mutations in the coding region of the transthyretin gene. Here, we focused on the mutations in the monomer-monomer and dimer-dimer interaction site of the transthyretin tetramer. The naturally occurring amyloidogenic Tyr114His (Y114H) and Tyr116Ser (Y116S) variants formed more amyloid fibrils than the wild-type transthyretin,...

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Identifiers

PMID: 14690414
DOI: 10.1021/bi0353528

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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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