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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Bibliografiske detaljer
Udgivet i:Chem Sci
Main Authors: 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
Sprog:Inglês
Udgivet: Royal Society of Chemistry 2018
Fag:
Chemistry
Online adgang: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
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