Divergent CPEB prion-like domains reveal different assembly mechanisms for a generic amyloid-like fold

Divergent CPEB prion-like domains reveal different assembly mechanisms for a generic amyloid-like fold

Abstract Background Amyloids are ordered, insoluble protein aggregates, characterized by a cross-β sheet quaternary structure in which molecules in a β-strand conformation are stacked along the filament axis via intermolecular interactions. While amyloids are typically associated with pathological c...

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Bibliographic Details
Main Authors: Rubén Hervás, María del Carmen Fernández-Ramírez, Albert Galera-Prat, Mari Suzuki, Yoshitaka Nagai, Marta Bruix, Margarita Menéndez, Douglas V. Laurents, Mariano Carrión-Vázquez
Format: Article
Language:English
Published: BMC 2021-03-01
Series:BMC Biology
Subjects:
Cytoplasmic polyadenylation element binding protein (CPEB)
Functional amyloids
Prion-like protein
Memory persistence
Coiled coil
Online Access:https://doi.org/10.1186/s12915-021-00967-9

Internet

https://doi.org/10.1186/s12915-021-00967-9

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