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...

Descripció completa

Guardat en:
Dades bibliogràfiques
Publicat a:Chem Sci
Autors principals: 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
Format: Artigo
Idioma:Inglês
Publicat: Royal Society of Chemistry 2018
Matèries:
Chemistry
Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC5933289/
https://ncbi.nlm.nih.gov/pubmed/29780459
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1039/c8sc00166a
Etiquetes: Afegir etiqueta
Sense etiquetes, Sigues el primer a etiquetar aquest registre!

Ítems similars