|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
|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
|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
|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
|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
|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
|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 the propensity for amyloid formation by a globular protein|
F Chiti, N Taddei, M Bucciantini, P White, G Ramponi, CM Dobson
The EMBO journal 19 (7), 1441-1449, 2000
|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
|Prevention of amyloid‐like aggregation as a driving force of protein evolution|
E Monsellier, F Chiti
EMBO reports 8 (8), 737-742, 2007
|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
|Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two‐state proteins|
KL Maxwell, D Wildes, A Zarrine‐Afsar, MA De Los Rios, AG Brown, ...
Protein Science 14 (3), 602-616, 2005
|Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships|
F Bemporad, F Chiti
Chemistry & biology 19 (3), 315-327, 2012