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Article

Investigating transthyretin variants H88R and I107V in amyloid priming: From destabilization to complete dissociation.

The FEBS journal - 1 Aug 2026

Bódy István L, Fazekas Zsolt, Wágner Nóra, Kiss-Szemán Anna J, Harmat Veronika, Pozsonyi Zoltán, Menyhárd Dóra K, Perczel András

Abstract excerpt

The destabilization of transthyretin (TTR) tetramers underlies the pathogenesis of ATTR amyloidosis, a disease manifesting in form of toxic amyloid deposits. Here we investigate two clinically relevant TTR variants, H88R and I107V, found among ATTR patients in the Carpathian Basin. While the I107V mutation exerts only a mild effect on tetramer assembly and monomer stability, it decreases the denaturation midpoint...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 41830400
DOI: 10.1111/febs.70485
PMCID: PMC13440615

Genes

TTR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

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Investigating transthyretin variants H88R and I107V in amyloid priming: From destabilization to complete dissociation.PMID 41830400Read ↗

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