BEMPORAD, FRANCESCO

BEMPORAD, FRANCESCO  

Scienze Biomediche, Sperimentali e Cliniche 'Mario Serio'  

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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 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 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 single amino acid mutation affects elicitor and expansins-like activities of cerato-platanin, a non-catalytic fungal protein. 2017 Luti, S; Martellini, F; Bemporad, F; Mazzoli, L; Paoli, P; Pazzagli, L.
Amyloid Aggregation Is Potently Slowed Down by Osmolytes Due to Compaction of Partially Folded State 2023 Garfagnini, Tommaso; Bemporad, Francesco; Harries, Daniel; Chiti, Fabrizio; Friedler, Assaf
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 formation of a protein in the absence of unfolding and destabilization of the native state 2005 G. Soldi; F. Bemporad; S. Torassa; A. Relini; M. Ramazzotti; N. Taddei; F. Chiti
Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase 2006 F. BEMPORAD; N. TADDEI; M. STEFANI; F. CHITI
Biological function in a non-native partially folded state of a protein. 2008 F. BEMPORAD; J. GSPONER; H.I. HOPEHARUOHO; G. PLAKOUTSI; G. STATI; M. STEFANI; N. TADDEI; M. VENDRUSCOLO; F. CHITI
Capturing Aβ42 aggregation in the cell 2019 Francesco Bemporad, Cristina Cecchi, Fabrizio Chiti
Characterization of the aggregation competent state of the acylphosphatase from Sulfolobus solfataricus 2010 Bemporad, Francesco; De Simone, Alfonso; Chiti, Fabrizio; Dobson, Christopher Martin
Characterizing intermolecular interactions that initiate native-like protein aggregation. 2012 Bemporad F;De Simone A;Chiti F;Dobson CM
Characterizing the amyloidogenic state of the acylphosphatase from Sulfolobus solfataricus 2011 Bemporad, Francesco; De Simone, Alfonso; Chiti, Fabrizio; Dobson, Christopher Martin
Conversion of the Native N-Terminal Domain of TDP-43 into a Monomeric Alternative Fold with Lower Aggregation Propensity 2022 Moretti, Matteo; Marzi, Isabella; Cantarutti, Cristina; Vivoli Vega, Mirella; Mandaliti, Walter; Mimmi, Maria Chiara; Bemporad, Francesco; Corazza, Alessandra; Chiti, Fabrizio
Direct Conversion of an Enzyme from Native-like to Amyloid-like Aggregates within Inclusion Bodies 2017 Elia, Francesco; Cantini, Francesca; Chiti, Fabrizio; Dobson, Christopher Martin; Bemporad, Francesco
Edge strand engineering prevents native-like aggregation in Sulfolobus solfataricus acylphosphatase. 2014 de Rosa M;Bemporad F;Pellegrino S;Chiti F;Bolognesi M;Ricagno S
Enzymatic activity outside the folded states of proteins 2009 Bemporad, Francesco; Chiti, Fabrizio
Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates 2005 G. PLAKOUTSI; F. BEMPORAD; M. CALAMAI; N. TADDEI; C.M. DOBSON; F. CHITI
Exploring the mechanism of formation of native-like and precursor amyloid oligomers for the native acylphosphatase from Sulfolobus solfataricus. 2006 Plakoutsi G;Bemporad F;Monti M;Pagnozzi D;Pucci P;Chiti F
Folding and aggregation studies in the acylphosphatase-like family 2009 Bemporad, Francesco