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Article

Thyroxine binding to transthyretin (TTR) variants--two variants (TTR Pro 55 and TTR Met 111) with a particularly low binding affinity.

European journal of endocrinology - 1 Aug 1996

Almeida M R, Saraiva M J

Abstract excerpt

Thyroxine (T4) binding is a well-characterized function of transthyretin (TTR) and has been used to assess structural alterations of TTR variants. Most TTR variants deposit as amyloid fibrils originating different forms of hereditary amyloidosis. It has been hypothesized that amino acid substitutions in the TTR variants induce structural alterations that may be responsible for the amyloidogenicity of the mutant...

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Share to Amino Acid Sequence
Share to Binding, Competitive
Share to Chromatography, High Pressure Liquid

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

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Source

Identifiers

PMID: 8810738
DOI: 10.1530/eje.0.1350226

Genes

TTR

Provenance

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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Thyroxine binding to transthyretin (TTR) variants--two variants (TTR Pro 55 and TTR Met 111) with a particularly low binding affinity.PMID 8810738Read ↗

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