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Article

Cryo-EM confirms a common fibril fold in the heart of four patients with ATTRwt amyloidosis.

Communications biology - 27 Jul 2024

Nguyen Binh An, Singh Virender, Afrin Shumaila, Singh Preeti, Pekala Maja, Ahmed Yasmin, Pedretti Rose, Canepa Jacob, Lemoff Andrew, Kluve-Beckerman Barbara, Wydorski Pawel M, Chhapra Farzeen, Saelices Lorena

Abstract excerpt

ATTR amyloidosis results from the conversion of transthyretin into amyloid fibrils that deposit in tissues causing organ failure and death. This conversion is facilitated by mutations in ATTRv amyloidosis, or aging in ATTRwt amyloidosis. ATTRv amyloidosis exhibits extreme phenotypic variability, whereas ATTRwt amyloidosis presentation is consistent and predictable. Previously, we found unique structural...

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Identifiers

PMID: 39068302
DOI: 10.1038/s42003-024-06588-6
PMCID: PMC11283564

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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