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Niccolò Taddei
Niccolò Taddei
Professore di Biochimica, Università di Firenze
Verified email at unifi.it
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Cited by
Cited by
Year
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
29862002
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
13721999
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
12632003
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
5082002
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
3522002
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
3521999
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
3002006
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
2922000
The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase
XD Su, N Taddei, M Stefani, G Ramponi, P Nordlund
Nature 370 (6490), 575-578, 1994
2581994
Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N‐terminal domain
F Chiti, M Bucciantini, C Capanni, N Taddei, CM Dobson, M Stefani
Protein Science 10 (12), 2541-2547, 2001
1652001
Cadmium-induced oxidative stress: focus on the central nervous system
JJV Branca, C Fiorillo, D Carrino, F Paternostro, N Taddei, M Gulisano, ...
Antioxidants 9 (6), 492, 2020
1582020
Nature and significance of the interactions between amyloid fibrils and biological polyelectrolytes
M Calamai, JR Kumita, J Mifsud, C Parrini, M Ramazzotti, G Ramponi, ...
Biochemistry 45 (42), 12806-12815, 2006
1532006
Relative influence of hydrophobicity and net charge in the aggregation of two homologous proteins
M Calamai, N Taddei, M Stefani, G Ramponi, F Chiti
Biochemistry 42 (51), 15078-15083, 2003
1532003
Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates
G Plakoutsi, F Bemporad, M Calamai, N Taddei, CM Dobson, F Chiti
Journal of molecular biology 351 (4), 910-922, 2005
1512005
SIRT1 modulates MAPK pathways in ischemic–reperfused cardiomyocytes
M Becatti, N Taddei, C Cecchi, N Nassi, PA Nassi, C Fiorillo
Cellular and Molecular Life Sciences 69, 2245-2260, 2012
1502012
Neutrophil activation promotes fibrinogen oxidation and thrombus formation in Behçet disease
M Becatti, G Emmi, E Silvestri, G Bruschi, L Ciucciarelli, D Squatrito, ...
Circulation 133 (3), 302-311, 2016
1432016
Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase
F Bemporad, N Taddei, M Stefani, F Chiti
Protein science 15 (4), 862-870, 2006
1392006
Detection of two partially structured species in the folding process of the amyloidogenic protein β2-microglobulin
F Chiti, P Mangione, A Andreola, S Giorgetti, M Stefani, CM Dobson, ...
Journal of molecular biology 307 (1), 379-391, 2001
1312001
Sequence and structural determinants of amyloid fibril formation
F Bemporad, G Calloni, S Campioni, G Plakoutsi, N Taddei, F Chiti
Accounts of chemical research 39 (9), 620-627, 2006
1282006
Aggregation of the acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursors for amyloid formation
G Plakoutsi, N Taddei, M Stefani, F Chiti
Journal of Biological Chemistry 279 (14), 14111-14119, 2004
1252004
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