The chaperonin CCT inhibits assembly of α-synuclein amyloid fibrils by a specific, conformation-dependent interaction

The eukaryotic chaperonin CCT (chaperonin containing TCP-1) uses cavities built into its double-ring structure to encapsulate and to assist folding of a large subset of proteins. CCT can inhibit amyloid fibre assembly and toxicity of the polyQ extended mutant of huntingtin, the protein responsible f...

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Detalles Bibliográficos
Autores principales: Sot, Begoña, Rubio-Muñoz, Alejandra, Leal-Quintero, Ahudrey, Martínez-Sabando, Javier, Marcilla, Miguel, Roodveldt, Cintia, Valpuesta, José M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5244355/
https://www.ncbi.nlm.nih.gov/pubmed/28102321
http://dx.doi.org/10.1038/srep40859

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5244355/
https://www.ncbi.nlm.nih.gov/pubmed/28102321
http://dx.doi.org/10.1038/srep40859

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