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

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 condition...

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Dettagli Bibliografici
Pubblicato in:BMC Biol
Autori principali: Hervás, Rubén, del Carmen Fernández-Ramírez, María, Galera-Prat, Albert, Suzuki, Mari, Nagai, Yoshitaka, Bruix, Marta, Menéndez, Margarita, Laurents, Douglas V., Carrión-Vázquez, Mariano
Natura: Artigo
Lingua:Inglês
Pubblicazione: BioMed Central 2021
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC7953810/
https://ncbi.nlm.nih.gov/pubmed/33706787
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1186/s12915-021-00967-9
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