High-avidity binding drives nucleation of amyloidogenic transthyretin monomer

Amyloidosis involves stepwise growth of fibrils assembled from soluble precursors. Transthyretin (TTR) naturally folds into a stable tetramer, whereas conditions and mutations that foster aberrant monomer formations facilitate TTR oligomeric aggregation and subsequent fibril extension. We investigat...

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Detalles Bibliográficos
Autores principales: Gao, Li, Xie, Xinfang, Liu, Pan, Jin, Jing
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Clinical Investigation 2022
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9057628/
https://www.ncbi.nlm.nih.gov/pubmed/35393947
http://dx.doi.org/10.1172/jci.insight.150131

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9057628/
https://www.ncbi.nlm.nih.gov/pubmed/35393947
http://dx.doi.org/10.1172/jci.insight.150131

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