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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Detaylı Bibliyografya
Yayımlandı:Chem Sci
Asıl Yazarlar: 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
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: Royal Society of Chemistry 2018
Konular:
Chemistry
Online Erişim: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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