CHITI, FABRIZIO

CHITI, FABRIZIO  

Scienze Biomediche, Sperimentali e Cliniche 'Mario Serio'  

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Risultati 1 - 20 di 203 (tempo di esecuzione: 0.038 secondi).
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 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
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
Amyloid formation from HypF-N under conditions in which the protein is initially in its native state 2005 G. MARCON; G. PLAKOUTSI; C. CANALE; A. RELINI; N. TADDEI; C.M. DOBSON; G. RAMPONI; F. CHITI
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
Amyloid-β oligomer synaptotoxicity is mimicked by oligomers of the model protein HypF-N 2013 Francesca Tatini; Anna Maria Pugliese; Chiara Traini; Sandra Niccoli; Giovanna Maraula; Teresa Ed Dami; Benedetta Mannini; Tania Scartabelli; Felicita Pedata; Fiorella Casamenti; Fabrizio Chiti
Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseases. 2008 V. BELLOTTI; 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
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
Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers 2018 Patel, Jayneil R.; Xu, Yingqi; Capitini, Claudia; Chiti, Fabrizio; De Simone, Alfonso*
Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases 2016 Evangelisti, Elisa; Cascella, Roberta; Becatti, Matteo; Marrazza, Giovanna; Dobson, Christopher M.; Chiti, Fabrizio; Stefani, Massimo; Cecchi, Cristina