|
Representative papers:
[1] Perni M, Galvagnion C, Maltsev A, Meisl G, Müller MB, Challa PK, Kirkegaard JB, Flagmeier P, Cohen SI, Cascella R, Chen SW, Limboker R, Sormanni P, Heller GT, Aprile FA, Cremades N, Cecchi C, Chiti F, Nollen EA, Knowles TP, Vendruscolo M, Bax A, Zasloff M, Dobson CM. A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity. Proc. Natl. Acad. Sci. USA. 2017, 114, E1009-E1017.
[2] Fusco G, Chen SW, Williamson PTF, Cascella R, Perni M, Jarvis JA, Cecchi C, Vendruscolo M, Chiti F, Cremades N, Ying L, Dobson CM, De Simone A. Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers. Science. 2017, 358:1440-1443.
[3] Chiti F, Dobson CM. Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. Annu. Rev. Biochem. 2017, 86, 27-68.
D'Andrea C, Foti A, Cottat M, Banchelli M, Capitini C, Barreca F, Canale C, de Angelis M, Relini A, Maragò OM, Pini R, Chiti F, Gucciardi PG, Matteini P. Small. Nanoscale Discrimination between Toxic and Nontoxic Protein Misfolded Oligomers with Tip-Enhanced Raman Spectroscopy. Small, 2018, 14 |
