Rationalization of the effects of mutations on peptide andprotein aggregation rates

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

Monica Bucciantini, Elisa Giannoni, Fabrizio Chiti et al. · Nature · 2002 · 2.4K citations

Life Sciences, Biochemistry, Molecular Biology +17

Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy

Kelly A. Conway, Seung‐Jae Lee, Jean‐Christophe Rochet et al. · Proceedings of the National Academy of Sciences · 2000 · 1.5K citations

Life Sciences, Neurobiology, Neuroscience +17

The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation

Camilla Nilsberth, Anita Westlind‐Danielsson, Christopher B. Eckman et al. · Nature Neuroscience · 2001 · 1.2K citations

Life Sciences, Genetics, Neuroscience +14

A Hydrophobic Stretch of 12 Amino Acid Residues in the Middle of α-Synuclein Is Essential for Filament Assembly

Benoit I. Giasson, Ian Murray, John Q. Trojanowski et al. · Journal of Biological Chemistry · 2001 · 1.1K citations · Full text

Life Sciences, Biochemistry, Neuroscience +17

Prevention of Transthyretin Amyloid Disease by Changing Protein Misfolding Energetics

Per Hammarström, R. Luke Wiseman, Evan T. Powers et al. · Science · 2003 · 522 citations

Life Sciences, Biochemistry, Molecular Biology +17