Folding mechanisms steer the amyloid fibril formation propensity of highly homologous proteins

Significant advances in the understanding of the molecular determinants of fibrillogenesis can be expected from comparative studies of the aggregation propensities of proteins with highly homologous structures but different folding pathways. Here, we fully characterize, by means of stopped-flow, T-j...

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Detalles Bibliográficos
Autores principales: Malgieri, Gaetano, D'Abrosca, Gianluca, Pirone, Luciano, Toto, Angelo, Palmieri, Maddalena, Russo, Luigi, Sciacca, Michele Francesco Maria, Tatè, Rosarita, Sivo, Valeria, Baglivo, Ilaria, Majewska, Roksana, Coletta, Massimo, Pedone, Paolo Vincenzo, Isernia, Carla, De Stefano, Mario, Gianni, Stefano, Pedone, Emilia Maria, Milardi, Danilo, Fattorusso, Roberto
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2018
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5933289/
https://www.ncbi.nlm.nih.gov/pubmed/29780459
http://dx.doi.org/10.1039/c8sc00166a

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5933289/
https://www.ncbi.nlm.nih.gov/pubmed/29780459
http://dx.doi.org/10.1039/c8sc00166a

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