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Article

Transthyretin can denature by an alternative pathway.

Proceedings of the National Academy of Sciences of the United States of America - 15 Sept 2026

Jäger Marcus, Schäfer Jan-Hannes, Lander Gabriel C, Powers Evan T, Gruebele Martin, Kelly Jeffery W

Abstract excerpt

Transthyretin (TTR) is a kinetically stable protein in the bloodstream, cerebrospinal fluid, and in the eye, whose aggregation causes a prominent human amyloid disease, TTR amyloidosis (ATTR). Dissociation of the wild-type TTR tetramer into metastable dimers is rate-limiting for aggregation at acidic pH and unfolding in denaturant solutions at neutral pH. However, this "canonical dimer" pathway of denaturation is...

Read the complete abstract on PubMed

Topics

Prealbumin
Protein Denaturation
Humans
Hydrogen-Ion Concentration
Kinetics
Mutation

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

Urea

Models, Molecular

Protein Unfolding

Source

Open in PubMed Open full text

Identifiers

PMID: 42709794
DOI: 10.1073/pnas.2536532123
PMCID: PMC13578799

Genes

TTR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 22 Oct 2026.

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Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

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