CHITI, FABRIZIO
CHITI, FABRIZIO
Scienze Biomediche, Sperimentali e Cliniche 'Mario Serio'
(1)H, (13)C and (15)N resonance assignments of human muscle acylphosphatase
2011 G.Fusco; A. De Simone; S.T.Hsu; F.Bemporad; M.Vendruscolo; F.Chiti; C.M.Dobson
A Brain-Permeable Aminosterol Regulates Cell Membranes to Mitigate the Toxicity of Diverse Pore-Forming Agents
2022 Kreiser, Ryan P; Wright, Aidan K; Sasser, Liam R; Rinauro, Dillon J; Gabriel, Justus M; Hsu, Claire M; Hurtado, Jorge A; McKenzie, Tristan L; Errico, Silvia; Albright, J Alex; Richardson, Lance; Jaffett, Victor A; Riegner, Dawn E; Nguyen, Lam T; LeForte, Kathleen; Zasloff, Michael; Hollows, Jared E; Chiti, Fabrizio; Vendruscolo, Michele; Limbocker, Ryan
A causative link between the structure of aberrant protein oligomers and their toxicity
2010 S.Campioni;B.Mannini;M.Zampagni;A.Pensalfini;C.Parrini;E.Evangelisti;A.Relini;M.Stefani;C.M.Dobson;C.Cecchi;F.Chiti
A comparison of the biochemical modifications caused by toxic and non-toxic protein oligomers in cells
2011 Zampagni M; Cascella R; Casamenti F; Grossi C; Evangelisti E; Wright D; Becatti M; Liguri G; Mannini B; Campioni S; Chiti F; Cecchi C.
A Complex Equilibrium among Partially Unfolded Conformations in Monomeric Transthyretin
2014 Conti S; Li X; Gianni S; Ghadami SA; Buxbaum JN; Cecchi C; Chiti F; and Bemporad F.
A computational approach for identifying the chemical factors involved in the glycosaminoglycans-mediated acceleration of amyloid fibril formation
2010 E. Monsellier; M. Ramazzotti; N. Taddei; F. Chiti
A model for the aggregation of the acylphosphatase from Sulfolobus solfataricus in its native-like state.
2008 F. BEMPORAD; T. VANNOCCI; L. VARELA; A. AZUAGA; F. CHITI
A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity
2017 Perni, Michele; Galvagnion, Céline; Maltsev, Alexander; Meisl, Georg; Müller, Martin B. D.; Challa, Pavan K.; Kirkegaard, Julius B.; Flagmeier, Patrick; Cohen, Samuel I. A.; Cascella, Roberta; Chen, Serene W.; Limboker, Ryan; Sormanni, Pietro; Heller, Gabriella T.; Aprile, Francesco A.; Cremades, Nunilo; Cecchi, Cristina; Chiti, Fabrizio; Nollen, Ellen A. A.; Knowles, Tuomas P. J.; Vendruscolo, Michele; Bax, Adriaan; Zasloff, Michael; M. Dobson, Christopher
A partially structured species of beta 2-microglobulin is significantly populated under physiological conditions and involved in fibrillogenesis.
2001 F. CHITI; E. DE LORENZI; S. GROSSI; P. MANGIONE; S. GIORGETTI; G. CACCIALANZA; C.M.DOBSON; G. MERLINI; G. RAMPONI; V. BELLOTTI
A quantitative biology approach correlates neuronal toxicity with the largest inclusions of TDP-43
2022 Roberta Cascella, Alessandra Bigi, Dylan Giorgino Riffert, Maria Cristina Gagliani, Emilio Ermini, Matteo Moretti, Katia Cortese, Cristina Cecchi, Fabrizio Chiti
Acceleration of the folding of acylphosphatase by stabilization of local secondary structure.
1999 F. CHITI ; N. TADDEI; P. WEBSTER; D. HAMADA; T. FIASCHI; G. RAMPONI; C. DOBSON
Aggregation of the acylphosphatase from S. solfataricus. The folded and partially unfolded states can be both precursors for amyloid formation.
2004 G. PLAKOUTSI; N. TADDEI; M. STEFANI; F. CHITI
Aggregation propensity of the human proteome
2008 E. Monsellier*; M. Ramazzotti*; N. Taddei; F. Chiti
Agitation and high ionic strength induce amyloidogenesis of a folded PDZ domain in native conditions
2009 A.Sicorello; S.Torrassa; G.Soldi; S.Gianni; C.Travaglini-Allocatelli; N.Taddei; A.Relini; F.Chiti
Amyloid fibril formation and disaggregation of fragment 1-29 of apomyoglobin: insights into the effect of pH on protein fibrillogenesis
2007 P. PICOTTI; G. DE FRANCESCHI; E. FRARE; B. SPOLAORE; M. ZAMBONIN; F. CHITI; P. POLVERINO DE LAURETO; A. FONTANA
Amyloid fibril formation by a normally folded protein in the absence of denaturants and agitation.
2013 Monsef Shokri M;Ahmadian S;Bemporad F;Khajeh K;Chiti F
Amyloid Fibril Formation can Proceed from Different Conformations of a Partially Unfolded Protein
2005 M. CALAMAI; F. CHITI; C.M. DOBSON
Amyloid fibrils act as a reservoir of soluble oligomers, the main culprits in protein deposition diseases
2022 Alessandra Bigi, Roberta Cascella, Fabrizio Chiti, Cristina Cecchi
Amyloid formation by globular proteins under native conditions
2009 F.CHITI; C.M.DOBSON
Amyloid formation by the model protein muscle acylphosphatase is accelerated by heparin and heparan sulphate through a scaffolding-based mechanism
2009 N.Motamedi-Shad; E.Monsellier; F.Chiti
| Titolo | Data di pubblicazione | Autore(i) | File |
|---|---|---|---|
| (1)H, (13)C and (15)N resonance assignments of human muscle acylphosphatase | 2011 | G.Fusco; A. De Simone; S.T.Hsu; F.Bemporad; M.Vendruscolo; F.Chiti; C.M.Dobson | |
| A Brain-Permeable Aminosterol Regulates Cell Membranes to Mitigate the Toxicity of Diverse Pore-Forming Agents | 2022 | Kreiser, Ryan P; Wright, Aidan K; Sasser, Liam R; Rinauro, Dillon J; Gabriel, Justus M; Hsu, Claire M; Hurtado, Jorge A; McKenzie, Tristan L; Errico, Silvia; Albright, J Alex; Richardson, Lance; Jaffett, Victor A; Riegner, Dawn E; Nguyen, Lam T; LeForte, Kathleen; Zasloff, Michael; Hollows, Jared E; Chiti, Fabrizio; Vendruscolo, Michele; Limbocker, Ryan | |
| A causative link between the structure of aberrant protein oligomers and their toxicity | 2010 | S.Campioni;B.Mannini;M.Zampagni;A.Pensalfini;C.Parrini;E.Evangelisti;A.Relini;M.Stefani;C.M.Dobson;C.Cecchi;F.Chiti | |
| A comparison of the biochemical modifications caused by toxic and non-toxic protein oligomers in cells | 2011 | Zampagni M; Cascella R; Casamenti F; Grossi C; Evangelisti E; Wright D; Becatti M; Liguri G; Mannini B; Campioni S; Chiti F; Cecchi C. | |
| A Complex Equilibrium among Partially Unfolded Conformations in Monomeric Transthyretin | 2014 | Conti S; Li X; Gianni S; Ghadami SA; Buxbaum JN; Cecchi C; Chiti F; and Bemporad F. | |
| A computational approach for identifying the chemical factors involved in the glycosaminoglycans-mediated acceleration of amyloid fibril formation | 2010 | E. Monsellier; M. Ramazzotti; N. Taddei; F. Chiti | |
| A model for the aggregation of the acylphosphatase from Sulfolobus solfataricus in its native-like state. | 2008 | F. BEMPORAD; T. VANNOCCI; L. VARELA; A. AZUAGA; F. CHITI | |
| A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity | 2017 | Perni, Michele; Galvagnion, Céline; Maltsev, Alexander; Meisl, Georg; Müller, Martin B. D.; Challa, Pavan K.; Kirkegaard, Julius B.; Flagmeier, Patrick; Cohen, Samuel I. A.; Cascella, Roberta; Chen, Serene W.; Limboker, Ryan; Sormanni, Pietro; Heller, Gabriella T.; Aprile, Francesco A.; Cremades, Nunilo; Cecchi, Cristina; Chiti, Fabrizio; Nollen, Ellen A. A.; Knowles, Tuomas P. J.; Vendruscolo, Michele; Bax, Adriaan; Zasloff, Michael; M. Dobson, Christopher | |
| A partially structured species of beta 2-microglobulin is significantly populated under physiological conditions and involved in fibrillogenesis. | 2001 | F. CHITI; E. DE LORENZI; S. GROSSI; P. MANGIONE; S. GIORGETTI; G. CACCIALANZA; C.M.DOBSON; G. MERLINI; G. RAMPONI; V. BELLOTTI | |
| A quantitative biology approach correlates neuronal toxicity with the largest inclusions of TDP-43 | 2022 | Roberta Cascella, Alessandra Bigi, Dylan Giorgino Riffert, Maria Cristina Gagliani, Emilio Ermini, Matteo Moretti, Katia Cortese, Cristina Cecchi, Fabrizio Chiti | |
| Acceleration of the folding of acylphosphatase by stabilization of local secondary structure. | 1999 | F. CHITI ; N. TADDEI; P. WEBSTER; D. HAMADA; T. FIASCHI; G. RAMPONI; C. DOBSON | |
| Aggregation of the acylphosphatase from S. solfataricus. The folded and partially unfolded states can be both precursors for amyloid formation. | 2004 | G. PLAKOUTSI; N. TADDEI; M. STEFANI; F. CHITI | |
| Aggregation propensity of the human proteome | 2008 | E. Monsellier*; M. Ramazzotti*; N. Taddei; F. Chiti | |
| Agitation and high ionic strength induce amyloidogenesis of a folded PDZ domain in native conditions | 2009 | A.Sicorello; S.Torrassa; G.Soldi; S.Gianni; C.Travaglini-Allocatelli; N.Taddei; A.Relini; F.Chiti | |
| Amyloid fibril formation and disaggregation of fragment 1-29 of apomyoglobin: insights into the effect of pH on protein fibrillogenesis | 2007 | P. PICOTTI; G. DE FRANCESCHI; E. FRARE; B. SPOLAORE; M. ZAMBONIN; F. CHITI; P. POLVERINO DE LAURETO; A. FONTANA | |
| Amyloid fibril formation by a normally folded protein in the absence of denaturants and agitation. | 2013 | Monsef Shokri M;Ahmadian S;Bemporad F;Khajeh K;Chiti F | |
| Amyloid Fibril Formation can Proceed from Different Conformations of a Partially Unfolded Protein | 2005 | M. CALAMAI; F. CHITI; C.M. DOBSON | |
| Amyloid fibrils act as a reservoir of soluble oligomers, the main culprits in protein deposition diseases | 2022 | Alessandra Bigi, Roberta Cascella, Fabrizio Chiti, Cristina Cecchi | |
| Amyloid formation by globular proteins under native conditions | 2009 | F.CHITI; C.M.DOBSON | |
| Amyloid formation by the model protein muscle acylphosphatase is accelerated by heparin and heparan sulphate through a scaffolding-based mechanism | 2009 | N.Motamedi-Shad; E.Monsellier; F.Chiti |