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Article

The importance of a gatekeeper residue on the aggregation of transthyretin: implications for transthyretin-related amyloidoses.

The Journal of biological chemistry - 10 Oct 2014

Sant'Anna Ricardo, Braga Carolina, Varejão Nathalia, Pimenta Karinne M, Graña-Montes Ricardo, Alves Aline, Cortines Juliana, Cordeiro Yraima, Ventura Salvador, Foguel Debora

Abstract excerpt

Protein aggregation into β-sheet-enriched amyloid fibrils is associated with an increasing number of human disorders. The adoption of such amyloid conformations seems to constitute a generic property of polypeptide chains. Therefore, during evolution, proteins have adopted negative design strategies to diminish their intrinsic propensity to aggregate, including enrichment of gatekeeper charged residues at the...

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Source

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Identifiers

PMID: 25086037
DOI: 10.1074/jbc.M114.563981
PMCID: PMC4192486

Genes

TTR

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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Research trail→

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The importance of a gatekeeper residue on the aggregation of transthyretin: implications for transthyretin-related amyloidoses.PMID 25086037Read ↗

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The crystal structure of amyloidogenic Leu55 --> Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils.Semantic proximity Read ↗

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