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Article

Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease.

Biochemistry - 17 Oct 1995

McCutchen S L, Lai Z, Miroy G J, Kelly J W, Colón W

Abstract excerpt

The role that transthyretin (TTR) mutations play in the amyloid disease familial amyloid polyneuropathy (FAP) has been probed by comparing the biophysical properties of several TTR variants as a function of pH. We have previously demonstrated that the partial acid denaturation of TTR is sufficient to effect amyloid fibril formation by self-assembly of a denaturation intermediate which appears to be monomeric....

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Source

Identifiers

PMID: 7577941
DOI: 10.1021/bi00041a032

Genes

TTR
FAP

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.

Related research

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Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease.PMID 7577941Read ↗

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Modulating conformational factors in transthyretin amyloid.Semantic proximity Read ↗

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Modifications of transthyretin in amyloid fibrils: analysis of amyloid from homozygous and heterozygous individuals with the Met30 mutation.Semantic proximity Read ↗

Tertiary structures of amyloidogenic and non-amyloidogenic transthyretin variants: new model for amyloid fibril formation.Semantic proximity Read ↗

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