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Article

Energetic characteristics of the new transthyretin variant A25T may explain its atypical central nervous system pathology.

Laboratory investigation; a journal of technical methods and pathology - 1 Mar 2003

Sekijima Yoshiki, Hammarström Per, Matsumura Miyuki, Shimizu Yuko, Iwata Makoto, Tokuda Takahiko, Ikeda Shu-Ichi, Kelly Jeffery W

Abstract excerpt

Transthyretin (TTR) is a tetrameric protein that must misfold to form amyloid fibrils. Misfolding includes rate-limiting tetramer dissociation, followed by fast tertiary structural changes that enable aggregation. Amyloidogenesis of wild-type (WT) TTR causes a late-onset cardiac disease called senile systemic amyloidosis. The aggregation of one of > 80 TTR variants leads to familial amyloidosis encompassing a...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 12649341
DOI: 10.1097/01.lab.0000059937.11023.1f

Genes

TTR

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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