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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Bibliographic Details
Published in: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
Language:Inglês
Published: Royal Society of Chemistry 2018
Subjects:
Chemistry
Online Access: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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