Gonzalo R. Lamberto

Structural characterization of the intrinsically unfolded protein β-synuclein, a natural negative regulator of α-synuclein aggregation

C. Griesinger, A. Binolfi, C. Bertoncini, 2007 .

Phosphorylation at S87 Is Enhanced in Synucleinopathies, Inhibits α-Synuclein Oligomerization, and Influences Synuclein-Membrane Interactions

E. Masliah, P. Aebischer, H. Lashuel, 2010, The Journal of Neuroscience.

Phosphorylation at Ser-129 but Not the Phosphomimics S129E/D Inhibits the Fibrillation of α-Synuclein*

P. Lansbury, H. Lashuel, D. Eliezer, 2008, Journal of Biological Chemistry.

Toward the Discovery of Effective Polycyclic Inhibitors of α-Synuclein Amyloid Assembly*

X. Salvatella, C. Griesinger, C. Bertoncini, 2011, The Journal of Biological Chemistry.

Structural and mechanistic basis behind the inhibitory interaction of PcTS on α-synuclein amyloid fibril formation

C. Griesinger, A. Binolfi, C. Bertoncini, 2009, Proceedings of the National Academy of Sciences.

Structural characterization of the intrinsically unfolded protein beta-synuclein, a natural negative regulator of alpha-synuclein aggregation.

C. Griesinger, A. Binolfi, C. Bertoncini, 2007, Journal of molecular biology.

Site-specific interactions of Cu(II) with alpha and beta-synuclein: bridging the molecular gap between metal binding and aggregation.

C. Griesinger, A. Binolfi, C. Bertoncini, 2008, Journal of the American Chemical Society.