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Article

FAP mutations destabilize transthyretin facilitating conformational changes required for amyloid formation.

Ciba Foundation symposium - 1 Jan 1996

Colon W, Lai Z, McCutchen S L, Miroy G J, Strang C, Kelly J W

Abstract excerpt

Functional transthyretin (TTR) can be transformed into amyloid by partial acid denaturation yielding a monomeric amyloidogenic intermediate which self-associates. The amyloidogenic intermediate has substantial beta-sheet structure with non-native but defined tertiary structure. pH-dependent proteolysis sensitivity studies have identified portions of TTR which become disordered and solvent-exposed in the...

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Source

Identifiers

PMID: 8915613
DOI: 10.1002/9780470514924.ch14

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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FAP mutations destabilize transthyretin facilitating conformational changes required for amyloid formation.PMID 8915613Read ↗

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Transthyretin mutagenesis: impact on amyloidogenesis and disease.Semantic proximity Read ↗

Transthyretin can denature by an alternative pathway.Semantic proximity Read ↗

Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity.Semantic proximity Read ↗

Different disease-causing mutations in transthyretin trigger the same conformational conversion.Semantic proximity Read ↗

Review: TTR amyloidosis-structural features leading to protein aggregation and their implications on therapeutic strategies.Semantic proximity Read ↗

[Amyloid polyneuropathies--biochemical and genetic aspects].Semantic proximity Read ↗

Transthyretin: Its function and amyloid formation.Semantic proximity Read ↗

Intrinsic versus mutation dependent instability/flexibility: a comparative analysis of the structure and dynamics of wild-type transthyretin and its pathogenic variants.Semantic proximity Read ↗

Structural insight into pH-induced conformational changes within the native human transthyretin tetramer.Semantic proximity Read ↗

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