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Article

Structural stabilization of transthyretin by a new compound, 6-benzoyl-2-hydroxy-1H-benzo[de]isoquinoline-1,3(2H)-dione.

Journal of pharmacological sciences - 1 Dec 2015

Yokoyama Takeshi, Takaki Shun, Chosa Keisuke, Sato Takashi, Suico Mary Ann, Teranishi Yuriko, Shuto Tsuyoshi, Mizuguchi Mineyuki, Kai Hirofumi

Abstract excerpt

Familial amyloid polyneuropathy (FAP) is a genetic, adult-onset, neurodegenerative disorder caused by amyloid formation of transthyretin (TTR), a thyroxine-binding protein. Mutation in TTR causes a propensity of TTR tetramer to dissociate to monomer, which is the first step to amyloidosis. Thus, a drug that can stabilize the tetramer structure will have therapeutic benefit. Here, by virtual screening and...

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Share to Amyloid Neuropathies, Familial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 26639444
DOI: 10.1016/j.jphs.2015.09.006

Genes

TTR
FAP

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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