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The Journal of Physical Chemistry. B|November 26, 2009
Conformational properties of unfolded HypF-NYujie Chen, Claudia Parrini, Niccolò Taddei, et al.FEBS Letters|December 1, 2006
The intrachain disulfide bridge is responsible of the unusual stability properties of novel acylphosphatase from Escherichia coliMatteo Ramazzotti, Claudia Parrini, Massimo Stefani, et al.Structure (London, England : 1993)|August 9, 2005
Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregationClaudia Parrini, Niccolò Taddei, Matteo Ramazzotti, et al.Journal of Molecular Biology|May 23, 2008
The folding process of acylphosphatase from Escherichia coli is remarkably accelerated by the presence of a disulfide bondClaudia Parrini, Francesco Bemporad, Alessio Baroncelli, et al.Plos One|January 21, 2011
Large proteins have a great tendency to aggregate but a low propensity to form amyloid fibrilsHassan Ramshini, Claudia Parrini, Annalisa Relini, et al.Biochemistry|October 18, 2006
Nature and significance of the interactions between amyloid fibrils and biological polyelectrolytesMartino Calamai, Janet R Kumita, John Mifsud, et al.Nature Chemical Biology|January 19, 2010
A causative link between the structure of aberrant protein oligomers and their toxicitySilvia Campioni, Benedetta Mannini, Mariagioia Zampagni, et al.Pageof 1