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Centre for Misfolding Diseases

Publications

Chaperones as Suppressors of Protein Misfolded Oligomer Toxicity.
B Mannini, F Chiti
– Frontiers in molecular neuroscience
(2017)
10,
98
Attenuating the Toxicity of Amyloid-Beta Aggregation with Specific Species
R Limbocker, B Mannini, M Perni, S Chia, G Heller, FS Ruggeri, J Habchi, G Meisl, PK Challa, M Zasloff, TPJ Knowles, M Vendruscolo, CM Dobson
– Biophysical Journal
(2017)
112,
494A
Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer’s disease
J Habchi, S Chia, R Limbocker, B Mannini, M Ahn, M Perni, O Hansson, P Arosio, JR Kumita, PK Challa, SIA Cohen, S Linse, CM Dobson, TPJ Knowles, M Vendruscolo
– Proceedings of the National Academy of Sciences
(2016)
114,
E200
Bis(indolyl)phenylmethane derivatives are effective small molecules for inhibition of amyloid fibril formation by hen lysozyme.
H Ramshini, B Mannini, K Khodayari, A Ebrahim-Habibi, AS Moghaddasi, R Tayebee, F Chiti
– European Journal of Medicinal Chemistry
(2016)
124,
361
Effect of molecular chaperones on aberrant protein oligomers in vitro: super-versus sub-stoichiometric chaperone concentrations
S Cappelli, A Penco, B Mannini, R Cascella, MR Wilson, H Ecroyd, X Li, JN Buxbaum, CM Dobson, C Cecchi, A Relini, F Chiti
– Biol Chem
(2016)
397,
401
SERS Detection of Amyloid Oligomers on Metallorganic-Decorated Plasmonic Beads
L Guerrini, R Arenal, B Mannini, F Chiti, R Pini, P Matteini, RA Alvarez-Puebla
– ACS applied materials & interfaces
(2015)
7,
9420
Toxicity of protein oligomers is rationalized by a function combining size and surface hydrophobicity
B Mannini, E Mulvihill, C Sgromo, R Cascella, R Khodarahmi, M Ramazzotti, CM Dobson, C Cecchi, F Chiti
– ACS chemical biology
(2014)
9,
2309
Transthyretin suppresses the toxicity of oligomers formed by misfolded proteins in vitro
R Cascella, S Conti, B Mannini, X Li, JN Buxbaum, B Tiribilli, F Chiti, C Cecchi
– Biochim Biophys Acta
(2013)
1832,
2302
Amyloid-β oligomer synaptotoxicity is mimicked by oligomers of the model protein HypF-N.
F Tatini, AM Pugliese, C Traini, S Niccoli, G Maraula, T Ed Dami, B Mannini, T Scartabelli, F Pedata, F Casamenti, F Chiti
– Neurobiol Aging
(2013)
34,
2100
Salt anions promote the conversion of HypF-N into amyloid-like oligomers and modulate the structure of the oligomers and the monomeric precursor state
S Campioni, B Mannini, JP López-Alonso, IN Shalova, A Penco, E Mulvihill, DV Laurents, A Relini, F Chiti
– Journal of molecular biology
(2012)
424,
132
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