Cavity filling mutations at the thyroxine-binding site dramatically increase transthyretin stability and prevent its aggregation

More than a hundred different Transthyretin (TTR) mutations are associated with fatal systemic amyloidoses. They destabilize the protein tetrameric structure and promote the extracellular deposition of TTR as pathological amyloid fibrils. So far, only mutations R104H and T119M have been shown to sta...

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Detalles Bibliográficos
Autores principales: Sant’Anna, Ricardo, Almeida, Maria Rosário, Varejāo, Nathalia, Gallego, Pablo, Esperante, Sebastian, Ferreira, Priscila, Pereira-Henriques, Alda, Palhano, Fernando L., de Carvalho, Mamede, Foguel, Debora, Reverter, David, Saraiva, Maria João, Ventura, Salvador
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5364509/
https://www.ncbi.nlm.nih.gov/pubmed/28338000
http://dx.doi.org/10.1038/srep44709

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5364509/
https://www.ncbi.nlm.nih.gov/pubmed/28338000
http://dx.doi.org/10.1038/srep44709

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