Fabrizio Chiti

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Aggregation Propensity of the Human Proteome

Niccolò Taddei, Elodie Monsellier, Matteo Ramazzotti, 2008, PLoS Comput. Biol..

Insight into the Structure of Amyloid Fibrils from the Analysis of Globular Proteins

Flavio Seno, Antonio Trovato, Amos Maritan, 2006, PLoS Comput. Biol..

Investigating the Effects of Mutations on Protein Aggregation in the Cell*

Fabrizio Chiti, Christopher M Dobson, C. Dobson, 2005, Journal of Biological Chemistry.

Amyloid formation by globular proteins under native conditions.

Fabrizio Chiti, Christopher M Dobson, C. Dobson, 2009, Nature chemical biology.

A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity

Michele Vendruscolo, Gabriella T Heller, Pietro Sormanni, 2017, Proceedings of the National Academy of Sciences.

Equilibrium collapse and the kinetic 'foldability' of proteins.

Kevin W Plaxco, Sebastian Doniach, Fabrizio Chiti, 2002, Biochemistry.

Exploring the mechanism of formation of native-like and precursor amyloid oligomers for the native acylphosphatase from Sulfolobus solfataricus.

Fabrizio Chiti, F. Chiti, F. Bemporad, 2006, Structure.

Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case.

Salvador Ventura, Fabrizio Chiti, Francesc X Aviles, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Comparison of the folding processes of distantly related proteins. Importance of hydrophobic content in folding.

Kevin W Plaxco, Niccolò Taddei, Fabrizio Chiti, 2003, Journal of molecular biology.

Edge strand engineering prevents native‐like aggregation in Sulfolobus solfataricus acylphosphatase

Fabrizio Chiti, Martino Bolognesi, Sara Pellegrino, 2014, The FEBS journal.

Low-level expression of a folding-incompetent protein in Escherichia coli: search for the molecular determinants of protein aggregation in vivo.

Niccolò Taddei, Fabrizio Chiti, Silvia Campioni, 2010, Journal of molecular biology.

Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase

Niccolò Taddei, Fabrizio Chiti, F. Chiti, 2006, Protein science : a publication of the Protein Society.

Protein folding: Defining a “standard” set of experimental conditions and a preliminary kinetic data set of two‐state proteins

Kevin W Plaxco, Ingo Ruczinski, Fabrizio Chiti, 2005, Protein science : a publication of the Protein Society.

Prefibrillar Amyloid Protein Aggregates Share Common Features of Cytotoxicity*

Fabrizio Chiti, Daniele Nosi, Lucia Formigli, 2004, Journal of Biological Chemistry.

Prediction of amyloid aggregation in vivo

Matteo Ramazzotti, Fabrizio Chiti, Mattia Belli, 2011, EMBO reports.

The distribution of residues in a polypeptide sequence is a determinant of aggregation optimized by evolution.

Michele Vendruscolo, Niccolò Taddei, Angelo Fontana, 2007, Biophysical journal.

Amyloid fibril formation and disaggregation of fragment 1-29 of apomyoglobin: insights into the effect of pH on protein fibrillogenesis.

Angelo Fontana, Fabrizio Chiti, Paola Picotti, 2007, Journal of molecular biology.

Kinetic partitioning of protein folding and aggregation

Christopher M. Dobson, Niccolò Taddei, Fabrizio Chiti, 2002, Nature Structural Biology.

Salt anions promote the conversion of HypF-N into amyloid-like oligomers and modulate the structure of the oligomers and the monomeric precursor state.

Fabrizio Chiti, Silvia Campioni, D. Laurents, 2012, Journal of molecular biology.

Prevention of amyloid‐like aggregation as a driving force of protein evolution

Fabrizio Chiti, F. Chiti, Elodie Monsellier, 2007, EMBO reports.

Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding

Christopher M. Dobson, Niccolò Taddei, Fabrizio Chiti, 1999, Nature Structural Biology.

Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases.

Michele Vendruscolo, Fabrizio Chiti, Christopher M Dobson, 2005, Journal of molecular biology.

Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases

Fabrizio Chiti, Christopher M Dobson, C. Dobson, 2002, Proceedings of the National Academy of Sciences of the United States of America.

1H, 13C and 15N resonance assignments of human muscle acylphosphatase

Michele Vendruscolo, Fabrizio Chiti, Alfonso De Simone, 2012, Biomolecular NMR assignments.

A causative link between the structure of aberrant protein oligomers and their toxicity.

Fabrizio Chiti, Christopher M Dobson, Silvia Campioni, 2010, Nature chemical biology.

Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility

Michele Vendruscolo, Fabrizio Chiti, Shang-Te Danny Hsu, 2011, Proceedings of the National Academy of Sciences.

The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process.

Fabrizio Chiti, F. Chiti, M. Monti, 2004, Journal of molecular biology.

Systematic In Vivo Analysis of the Intrinsic Determinants of Amyloid β Pathogenicity

Michele Vendruscolo, Fabrizio Chiti, Damian C Crowther, 2007, PLoS biology.

Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains.

Michele Vendruscolo, Fabrizio Chiti, Christopher M Dobson, 2004, Journal of molecular biology.

Prediction of aggregation-prone regions in structured proteins.

Michele Vendruscolo, Fabrizio Chiti, Gian Gaetano Tartaglia, 2008, Journal of molecular biology.

Prefibrillar Amyloid Aggregates Could Be Generic Toxins in Higher Organisms

Christopher M. Dobson, Fabrizio Chiti, Leila M. Luheshi, 2006, The Journal of Neuroscience.

Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus

Alessandra Corazza, Gennaro Esposito, Paolo Viglino, 2005, Proteins.

Biological function in a non‐native partially folded state of a protein

Michele Vendruscolo, Niccolò Taddei, Fabrizio Chiti, 2008, The EMBO journal.

Stabilization of a native protein mediated by ligand binding inhibits amyloid formation independently of the aggregation pathway.

Fabrizio Chiti, F. Chiti, N. Taddei, 2006, Journal of medicinal chemistry.

Sequence and structural determinants of amyloid fibril formation.

Fabrizio Chiti, Silvia Campioni, F. Chiti, 2006, Accounts of chemical research.

Large Proteins Have a Great Tendency to Aggregate but a Low Propensity to Form Amyloid Fibrils

Ali Akbar Saboury, Fabrizio Chiti, Alessandra Pesce, 2011, PloS one.

Characterizing intermolecular interactions that initiate native-like protein aggregation.

Fabrizio Chiti, Christopher M Dobson, C. Dobson, 2012, Biophysical journal.