CAMPIONI, SILVIA
CAMPIONI, SILVIA
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.
Chaperones suppress protein oligomer toxicity: Insight into the molecular mechanism of action
2011 B. Mannini; S. Campioni; M. Boninsegna; E. Palagano; R. Cascella; M. Zampagni; A. Penco; M. Wilson; S. Meehan; C. Roodveldt; A. Relini; C. Cecchi; F. Chiti
Chaperones suppress the toxicity of aberrant protein aggregates. Molecular insight into the mechanism of action
2012 B. Mannini; S. Campioni; M. Boninsegna; A. Penco; R. Cascella; M. Zampagni; M. Wilson; S. Meehan; C. Roodveldt; C. Dobson; A. Relini; C. Cecchi; F. Chiti
Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers
2012 B. Mannini; R. Cascella; M. Zampagni; M. van Waarde-Verhagen; S. Meehan; C. Roodveldt; S. Campioni; M. Boninsegna; A. Penco; A. Relini; H.H. Kampinga; C.M. Dobson; M.R. Wilson; C. Cecchi; F. Chiti
Salt anions promote the conversion of HypF-N into amyloid-like oligomers and modulate the structure of the oligomers and the monomeric precursor state.
2012 Campioni S;Mannini B;López-Alonso JP;Shalova IN;Penco A;Mulvihill E;Laurents DV;Relini A;Chiti F
Sequence and structural determinants of amyloid fibril formation
2006 F. BEMPORAD; G. CALLONI; S. CAMPIONI; G. PLAKOUTSI; N. TADDEI; F. CHITI
Study of the early stages of HypN-N conversion intoamyloid-like aggregates: from the monomeric state tothe early-forming pre-fibrillar aggregates
2008 S.Campioni
The induction of α-helical structure in partially unfolded HypF-N does not affect its aggregation propensity
2011 B.Ahmad; I.Vigliotta; F.Tatini; S.Campioni; B.Mannini; J.Winkelmann; B.Tiribilli; F.Chiti
Why proteins misfold?
2010 Campioni S; Monsellier E; Chiti F
Titolo | Data di pubblicazione | Autore(i) | File |
---|---|---|---|
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. | |
Chaperones suppress protein oligomer toxicity: Insight into the molecular mechanism of action | 2011 | B. Mannini; S. Campioni; M. Boninsegna; E. Palagano; R. Cascella; M. Zampagni; A. Penco; M. Wilson; S. Meehan; C. Roodveldt; A. Relini; C. Cecchi; F. Chiti | |
Chaperones suppress the toxicity of aberrant protein aggregates. Molecular insight into the mechanism of action | 2012 | B. Mannini; S. Campioni; M. Boninsegna; A. Penco; R. Cascella; M. Zampagni; M. Wilson; S. Meehan; C. Roodveldt; C. Dobson; A. Relini; C. Cecchi; F. Chiti | |
Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers | 2012 | B. Mannini; R. Cascella; M. Zampagni; M. van Waarde-Verhagen; S. Meehan; C. Roodveldt; S. Campioni; M. Boninsegna; A. Penco; A. Relini; H.H. Kampinga; C.M. Dobson; M.R. Wilson; C. Cecchi; F. Chiti | |
Salt anions promote the conversion of HypF-N into amyloid-like oligomers and modulate the structure of the oligomers and the monomeric precursor state. | 2012 | Campioni S;Mannini B;López-Alonso JP;Shalova IN;Penco A;Mulvihill E;Laurents DV;Relini A;Chiti F | |
Sequence and structural determinants of amyloid fibril formation | 2006 | F. BEMPORAD; G. CALLONI; S. CAMPIONI; G. PLAKOUTSI; N. TADDEI; F. CHITI | |
Study of the early stages of HypN-N conversion intoamyloid-like aggregates: from the monomeric state tothe early-forming pre-fibrillar aggregates | 2008 | S.Campioni | |
The induction of α-helical structure in partially unfolded HypF-N does not affect its aggregation propensity | 2011 | B.Ahmad; I.Vigliotta; F.Tatini; S.Campioni; B.Mannini; J.Winkelmann; B.Tiribilli; F.Chiti | |
Why proteins misfold? | 2010 | Campioni S; Monsellier E; Chiti F |