Fabrizio Chiti
Cited by
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Protein misfolding, functional amyloid, and human disease
F Chiti, CM Dobson
Annu. Rev. Biochem. 75, 333-366, 2006
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
M Bucciantini, E Giannoni, F Chiti, F Baroni, L Formigli, J Zurdo, N Taddei, ...
nature 416 (6880), 507-511, 2002
Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade
F Chiti, CM Dobson
Annual review of biochemistry 86, 27-68, 2017
Designing conditions for in vitro formation of amyloid protofilaments and fibrils
F Chiti, P Webster, N Taddei, A Clark, M Stefani, G Ramponi, CM Dobson
Proceedings of the National Academy of Sciences 96 (7), 3590-3594, 1999
Rationalization of the effects of mutations on peptide andprotein aggregation rates
F Chiti, M Stefani, N Taddei, G Ramponi, CM Dobson
Nature 424 (6950), 805-808, 2003
Amyloid formation by globular proteins under native conditions
F Chiti, CM Dobson
Nature chemical biology 5 (1), 15-22, 2009
Prediction of “aggregation-prone” and “aggregation-susceptible” regions in proteins associated with neurodegenerative diseases
AP Pawar, KF Dubay, J Zurdo, F Chiti, M Vendruscolo, CM Dobson
Journal of molecular biology 350 (2), 379-392, 2005
A causative link between the structure of aberrant protein oligomers and their toxicity
S Campioni, B Mannini, M Zampagni, A Pensalfini, C Parrini, ...
Nature chemical biology 6 (2), 140-147, 2010
Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers
G Fusco, SW Chen, PTF Williamson, R Cascella, M Perni, JA Jarvis, ...
Science 358 (6369), 1440-1443, 2017
Kinetic partitioning of protein folding and aggregation
F Chiti, N Taddei, F Baroni, C Capanni, M Stefani, G Ramponi, ...
Nature structural biology 9 (2), 137-143, 2002
Prediction of aggregation-prone regions in structured proteins
GG Tartaglia, AP Pawar, S Campioni, CM Dobson, F Chiti, M Vendruscolo
Journal of molecular biology 380 (2), 425-436, 2008
Prefibrillar amyloid protein aggregates share common features of cytotoxicity
M Bucciantini, G Calloni, F Chiti, L Formigli, D Nosi, CM Dobson, ...
Journal of Biological Chemistry 279 (30), 31374-31382, 2004
Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains
KF DuBay, AP Pawar, F Chiti, J Zurdo, CM Dobson, M Vendruscolo
Journal of molecular biology 341 (5), 1317-1326, 2004
Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases
F Chiti, M Calamai, N Taddei, M Stefani, G Ramponi, CM Dobson
Proceedings of the National Academy of Sciences 99 (suppl_4), 16419-16426, 2002
Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding
F Chiti, N Taddei, PM White, M Bucciantini, F Magherini, M Stefani, ...
Nature structural biology 6 (11), 1005-1009, 1999
Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships
F Bemporad, F Chiti
Chemistry & biology 19 (3), 315-327, 2012
A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity
M Perni, C Galvagnion, A Maltsev, G Meisl, MBD Müller, PK Challa, ...
Proceedings of the National Academy of Sciences 114 (6), E1009-E1017, 2017
Prefibrillar amyloid aggregates could be generic toxins in higher organisms
S Baglioni, F Casamenti, M Bucciantini, LM Luheshi, N Taddei, F Chiti, ...
Journal of Neuroscience 26 (31), 8160-8167, 2006
Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case
S Ventura, J Zurdo, S Narayanan, M Parreño, R Mangues, B Reif, F Chiti, ...
Proceedings of the National Academy of Sciences 101 (19), 7258-7263, 2004
Mutational analysis of the propensity for amyloid formation by a globular protein
F Chiti, N Taddei, M Bucciantini, P White, G Ramponi, CM Dobson
The EMBO journal, 2000
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