MANNINI, BENEDETTA

MANNINI, BENEDETTA  

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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.
Aβ oligomers dysregulate calcium homeostasis by mechanosensitive activation of AMPA and NMDA receptors. 2021 Giulia Fani, Benedetta Mannini, Giulia Vecchi, Roberta Cascella, Cristina Cecchi, Christopher M. Dobson, Michele Vendruscolo, Fabrizio Chiti
Bis(indolyl)phenylmethane derivatives are effective small molecules for inhibition of amyloid fibril formation by hen lysozyme 2016 Ramshini, Hassan; Mannini, Benedetta; Khodayari, Kaveh; Ebrahim-Habibi, Azadeh; Moghaddasi, Azam Sadat; Tayebee, Reza; Chiti, Fabrizio*
Chaperones as Suppressors of Protein Misfolded Oligomer Toxicity 2017 Mannini, Benedetta; Chiti, Fabrizio
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
Differential interactome and innate immune response activation of two structurally distinct misfolded protein oligomers 2019 Mannini, Benedetta; Vecchi, Giulia; Labrador-Garrido, Adahir; Fabre, Bertrand; Fani, Giulia; Munoz Franco, Jaime; Lilley, Kathryn S; Pozo, David; Vendruscolo, Michele; Chiti, Fabrizio; Dobson, Christopher M; Roodveldt, Cintia
Distinct responses of human peripheral blood cells to different misfolded protein oligomers 2021 Leal-Lasarte, Magdalena; Mannini, Benedetta; Chiti, Fabrizio; Vendruscolo, Michele; Dobson, Christopher M; Roodveldt, Cintia; Pozo, David
Early-forming aberrant aggregates in protein deposition diseases: structural characteristics, interaction with molecular chaperones, ability to trigger inflammation 2013 Benedetta Mannini
Effect of molecular chaperones on aberrant protein oligomers in vitro: super- versus sub-stoichiometric chaperone concentrations 2016 Cappelli, S; Penco, A; Mannini, Benedetta; Cascella, Roberta; Wilson, M; Ecroyd, H; Li, X; Buxbaum, J; Dobson, Cm; Cecchi, Cristina; Relini, A; Chiti, Fabrizio
Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegans 2021 Perni, Michele; Mannini, Benedetta; Xu, Catherine K; Kumita, Janet R; Dobson, Christopher M; Chiti, Fabrizio; Vendruscolo, Michele
Glycosaminoglycans (GAGs) Suppress the Toxicity of HypF-N Prefibrillar Aggregates 2012 T. Saridaki; M. Zampagni; B. Mannini; E. Evangelisti; N. Taddei; C. Cecchi; F. Chiti
Large proteins have a great tendency to aggregate but a low propensity to form amyloid fibrils 2011 H.Ramshini; C.Parrini; A.Relini; M.Zampagni; B.Mannini; A.Pesce; A.A.Saboury; M.Nemat-Gorgani; 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
Multistep Inhibition of α‑Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine 2018 Perni M, Flagmeier P, Limbocker R, Cascella R, Aprile FA, Galvagnion C, Heller GT, Meisl G, Chen SW, Kumita JR, Challa PK, Kirkegaard JB, Cohen SIA, Mannini B, Barbut D, Nollen EAA, Cecchi C, Cremades N, Knowles TPJ, Chiti F, Zasloff M, Vendruscolo M, Dobson CM
Rationally designed antibodies as research tools to study the structure–toxicity relationship of amyloid-β oligomers 2020 Limbocker R.; Mannini B.; Cataldi R.; Chhangur S.; Wright A.K.; Kreiser R.P.; Albright J.A.; Chia S.; Habchi J.; Sormanni P.; Kumita J.R.; Ruggeri F.S.; Dobson C.M.; Chiti F.; Aprile F.A.; Vendruscolo M.
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
SERS Detection of Amyloid Oligomers on Metallorganic-Decorated Plasmonic Beads 2015 Guerrini, Luca; Arenal, Raul; Mannini, Benedetta; Chiti, Fabrizio; Pini, Roberto; Matteini, Paolo; Alvarez-Puebla, Ramon A
Squalamine and its derivatives modulate the aggregation of amyloid-β and α-synuclein and suppress the toxicity of their oligomers 2021 Ryan Limbocker, Roxine Staats, Sean Chia, Francesco S Ruggeri, Benedetta Mannini, Catherine K Xu, Michele Perni, Roberta Cascella, Alessandra Bigi, Liam R Sasser, Natalie R Block, Aidan K Wright, Ryan P Kreiser, Edward T Custy, Georg Meisl, Silvia Errico, Johnny Habchi, Patrick Flagmeier, Tadas Kartanas, Jared E Hollows, Lam T Nguyen, Kathleen LeForte, Denise Barbut, Janet R Kumita, Cristina Cecchi, Michael Zasloff, Tuomas P J Knowles, Christopher M Dobson, Fabrizio Chiti, Michele Vendruscolo