Abilities of the BRICHOS domain to prevent neurotoxicity and fibril formation are dependent on a highly conserved Asp residue

Proteins can self-assemble into amyloid fibrils or amorphous aggregates and thereby cause disease. Molecular chaperones can prevent both these types of protein aggregation, but to what extent the respective mechanisms are overlapping is not fully understood. The BRICHOS domain constitutes a disease-...

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Detalles Bibliográficos
Autores principales: Chen, Gefei, Andrade-Talavera, Yuniesky, Zhong, Xueying, Hassan, Sameer, Biverstål, Henrik, Poska, Helen, Abelein, Axel, Leppert, Axel, Kronqvist, Nina, Rising, Anna, Hebert, Hans, Koeck, Philip J. B., Fisahn, André, Johansson, Jan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: RSC 2022
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9627735/
https://www.ncbi.nlm.nih.gov/pubmed/36349220
http://dx.doi.org/10.1039/d2cb00187j

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9627735/
https://www.ncbi.nlm.nih.gov/pubmed/36349220
http://dx.doi.org/10.1039/d2cb00187j

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