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Article

Native state hydrogen exchange study of suppressor and pathogenic variants of transthyretin.

Journal of molecular biology - 19 Jul 2002

Liu Kai, Kelly Jeffery W, Wemmer David E

Abstract excerpt

Transthyretin (TTR) is an amyloidogenic protein whose aggregation is responsible for numerous familial amyloid diseases, the exact phenotype being dependent on the sequence deposited. Many familial disease variants display decreased stability in vitro, and early onset pathology in vivo. Only subtle structural differences were observed upon crystallographic comparison of the disease-associated variants to the...

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Share to Amino Acid Substitution
Share to Amyloid Neuropathies, Familial
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 12095258
DOI: 10.1016/s0022-2836(02)00471-0

Genes

TTR
FAP

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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Native state hydrogen exchange study of suppressor and pathogenic variants of transthyretin.PMID 12095258Read ↗

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