Research Topics
| Fabrizio ChitiSummaryAffiliation: University of Florence Country: Italy Publications
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Detail Information
Publications
Capillary electrophoresis investigation of a partially unfolded conformation of beta(2)-microglobulinErsilia De Lorenzi
Department of Pharmaceutical Chemistry, University of Pavia, Viale Taramelli 12, I 27100 Pavia, Italy
Electrophoresis 23:918-25. 2002....- Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseasesAmol P Pawar
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
J Mol Biol 350:379-92. 2005.... 
Aggregation propensity of the human proteomeElodie Monsellier
Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, Florence, Italy
PLoS Comput Biol 4:e1000199. 2008..In particular, they emphasize the existence of a negative selection pressure that finely modulates protein sequences in order to adapt their aggregation propensity to their biological context...- Protein misfolding, functional amyloid, and human diseaseFabrizio Chiti
Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, I 50134 Firenze, Italy
Annu Rev Biochem 75:333-66. 2006.... 
Amyloid formation by globular proteins under native conditionsFabrizio Chiti
Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, Viale Morgagni 50, I 50134 Firenze, Italy
Nat Chem Biol 5:15-22. 2009..We review recent evidence on this topic and discuss its significance for understanding the onset and potential inhibition of protein aggregation in the context of diseases...- Structure and dynamics of a partially folded protein are decoupled from its mechanism of aggregationGiulia Calloni
Dipartimento di Scienze Biochimiche, Universita di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
J Am Chem Soc 130:13040-50. 2008..It is, by contrast, promoted by discrete protein regions that have the highest intrinsic propensity to aggregate because of their physicochemical properties... - Amyloid formation of a protein in the absence of initial unfolding and destabilization of the native stateGemma Soldi
Dipartimento di Scienze Biochimiche, Universita di Firenze, Firenze, Italy
Biophys J 89:4234-44. 2005.... - Agitation and high ionic strength induce amyloidogenesis of a folded PDZ domain in native conditionsAlessandro Sicorello
Dipartimento di Scienze Biochimiche, Universita di Firenze, Florence, Italy
Biophys J 96:2289-98. 2009..Such an approach offers new opportunities to investigate protein aggregation under conditions in which a globular protein is initially folded, and to elucidate the physical forces that promote amyloid fibril formation... - Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregatesGeorgia Plakoutsi
Dipartimento di Scienze Biochimiche, , Viale Morgagni 50, 50134 Firenze, Italy
J Mol Biol 351:910-22. 2005.... - Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphataseFrancesco Bemporad
Dipartimento di Scienze Biochimiche, , 50134, Firenze, Italy
Protein Sci 15:862-70. 2006..This suggests that aromatic residues favor aggregation because of these factors rather than for their aromaticity... - The folding process of acylphosphatase from Escherichia coli is remarkably accelerated by the presence of a disulfide bondClaudia Parrini
Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
J Mol Biol 379:1107-18. 2008..These results indicate that the presence of a disulfide bond in a protein is an important determinant of the folding rate and allows its contribution to be determined in quantitative terms... - Investigating the effects of mutations on protein aggregation in the cellGiulia Calloni
Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
J Biol Chem 280:10607-13. 2005..These results suggest that the principles being established to rationalize aggregation behavior in vitro have general validity for situations in vivo where aggregation has both biotechnological and medical relevance... - Kinetic analysis of amyloid formation in the presence of heparan sulfate: faster unfolding and change of pathwayNeda Motamedi-Shad
Department of Biochemistry, University of Florence, Viale Morgagni 50, 50134 Florence, Italy
J Biol Chem 284:29921-34. 2009..Two aggregation phases are generally observed when proteins aggregate in the presence of HS, underlying the importance of a detailed kinetic analysis to fully understand the effect of this glycosaminoglycan on amyloidogenesis... - Relative influence of hydrophobicity and net charge in the aggregation of two homologous proteinsMartino Calamai
Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
Biochemistry 42:15078-83. 2003.... - Conformational properties of the aggregation precursor state of HypF-NSilvia Campioni
Dipartimento di Scienze Biochimiche, Universita di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
J Mol Biol 379:554-67. 2008..In addition, the possibility of triggering aggregation by modulating the ionic strength of the solution provides one a unique opportunity to study both the initial precursor state and the aggregation process... - Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregationClaudia Parrini
Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
Structure 13:1143-51. 2005..Apart from the glycine at position 15, all other conserved glycine residues in this protein could have been maintained during evolution because of their ability to inhibit aggregation... - Comparison of the folding processes of distantly related proteins. Importance of hydrophobic content in foldingGiulia Calloni
Dipartimento di Scienze Biochimiche, Universita di Firenze, Viale Morgagni 50, 50134 Florence, Italy
J Mol Biol 330:577-91. 2003.... - The degree of structural protection at the edge beta-strands determines the pathway of amyloid formation in globular proteinsGemma Soldi
Dipartimento di Scienze Biochimiche, Universita di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
J Am Chem Soc 130:4295-302. 2008..The kinetic data show that formation of the latter species proceeds via an alternative mechanism that is independent of the transient formation of native-like aggregates... - Salt anions promote the conversion of HypF-N into amyloid-like oligomers and modulate the structure of the oligomers and the monomeric precursor stateSilvia Campioni
Department of Biochemical Sciences, University of Florence, Viale Morgagni 50, 50134 Florence, Italy
J Mol Biol 424:132-49. 2012..Overall, the data contribute to rationalize the effect of salts on amyloid-like oligomer formation and to explain the role of charged biological macromolecules in protein aggregation processes... - Low-level expression of a folding-incompetent protein in Escherichia coli: search for the molecular determinants of protein aggregation in vivoJulia Winkelmann
Department of Biochemical Sciences, University of Florence, Viale Morgagni 50, 50134 Firenze, Italy
J Mol Biol 398:600-13. 2010.... - Biological function in a non-native partially folded state of a proteinFrancesco Bemporad
Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, Firenze, Italy
EMBO J 27:1525-35. 2008..These results extend the spectrum of biological functions carried out in the absence of a folded state to include enzyme catalysis... - Amyloid formation from HypF-N under conditions in which the protein is initially in its native stateGiordana Marcon
Dipartimento di Scienze Biochimiche, Universita di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
J Mol Biol 347:323-35. 2005..This conclusion emphasises the importance for cells to constantly combat the propensity for even the most stable of these proteins to aggregate... - Protein aggregation starting from the native globular stateGiordana Marcon
, Dipartimento di Scienze Biochimiche, Firenze, Italy
Methods Enzymol 413:75-91. 2006.... - Studying the folding process of the acylphosphatase from Sulfolobus solfataricus. A comparative analysis with other proteins from the same superfamilyFrancesco Bemporad
Dipartimento di Scienze Biochimiche, , Viale Morgagni 50, 50134 Firenze, Italy
Biochemistry 43:9116-26. 2004.... - Glycosaminoglycans (GAGs) suppress the toxicity of HypF-N prefibrillar aggregatesTheodora Saridaki
Department of Biochemical Sciences, University of Florence, Viale Morgagni 50, 50134 Florence, Italy
J Mol Biol 421:616-30. 2012.... - Stabilization of a native protein mediated by ligand binding inhibits amyloid formation independently of the aggregation pathwayGemma Soldi
Dipartimento di Scienze Biochimiche, , Viale Morgagni 50, 50134 Firenze, Italy
J Med Chem 49:6057-64. 2006.... - Prevention of amyloid-like aggregation as a driving force of protein evolutionElodie Monsellier
Dipartimento di Scienze Biochimiche, Universita di Firenze, Viale Morgagni 50, I 50134, Firenze, Italy
EMBO Rep 8:737-42. 2007.... - Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseasesFabrizio Chiti
Dipartimento di Scienze Biochimiche, , Viale Morgagni 50, 50134 Florence, Italy
Proc Natl Acad Sci U S A 99:16419-26. 2002.... - Selection of antibody fragments specific for an alpha-helix region of acylphosphataseDonatella Degl'Innocenti
Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, Viale Morgagni 50, Firenze 50134, Italy
J Mol Recognit 17:62-6. 2004..This study shows that phage display libraries can be used to raise antibodies one can use as reagents able to target regions of a protein with a specific native-like secondary structure... - Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseasesMonica Bucciantini
Dipartimento di Scienze Biochimiche, Viale Morgagni 50, Universita degli Studi di Firenze, 50134 Firenze, Italy
Nature 416:507-11. 2002..This finding provides added evidence that avoidance of protein aggregation is crucial for the preservation of biological function and suggests common features in the origins of this family of protein deposition diseases... - A model for the aggregation of the acylphosphatase from Sulfolobus solfataricus in its native-like stateFrancesco Bemporad
Department of Biochemical Sciences, University of Florence, Viale Morgagni 50, Florence 50134, Italy
Biochim Biophys Acta 1784:1986-96. 2008..The obtained results allow the formulation of a model for the assembly of Sso AcP into amyloid-like aggregates at a molecular level... - Sequence and structural determinants of amyloid fibril formationFrancesco Bemporad
Dipartimento di Scienze Biochimiche, , Viale Morgagni 50, 50134 Firenze, Italy
Acc Chem Res 39:620-7. 2006.... - Exploring the mechanism of formation of native-like and precursor amyloid oligomers for the native acylphosphatase from Sulfolobus solfataricusGeorgia Plakoutsi
Dipartimento di Scienze Biochimiche, , Viale Morgagni 50, 50134 Firenze, Italy
Structure 14:993-1001. 2006.... - A computational approach for identifying the chemical factors involved in the glycosaminoglycans-mediated acceleration of amyloid fibril formationElodie Monsellier
Dipartimento di Scienze Biochimiche, Universita di Firenze, Firenze, Italy
PLoS ONE 5:e11363. 2010..The high number of data accumulated so far has created the grounds for the construction of a database on the effects of a number of GAGs on different proteins... - Large proteins have a great tendency to aggregate but a low propensity to form amyloid fibrilsHassan Ramshini
Dipartimento di Scienze Biochimiche, Universita di Firenze, Florence, Italy
PLoS ONE 6:e16075. 2011.... - Aggregation of the Acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursors for amyloid formationGeorgia Plakoutsi
Dipartimento di Scienze Biochimiche, Universita di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
J Biol Chem 279:14111-9. 2004..This conclusion has a biological relevance as globular proteins normally spend most of their lifetime in folded structures... - The distribution of residues in a polypeptide sequence is a determinant of aggregation optimized by evolutionElodie Monsellier
Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, Florence, Italy
Biophys J 93:4382-91. 2007.... - Amyloid formation by the model protein muscle acylphosphatase is accelerated by heparin and heparan sulphate through a scaffolding-based mechanismNeda Motamedi-Shad
Dipartimento di Scienze Biochimiche, Universita di Firenze, Viale Morgagni, 50, 50134 Firenze and Consorzio interuniversitario Istituto Nazionale Biostrutture e Biosistemi INBB, Viale delle Medaglie d Oro, 305, 00136 Roma, Italy
J Biochem 146:805-14. 2009.... - Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomersElisa Evangelisti
Department of Biochemical Sciences and Research Centre on the Molecular Basis of Neurodegeneration CIMN, University of Florence, Florence, Italy
J Cell Sci 125:2416-27. 2012..We identified that the degree of toxicity of the oligomeric species is the result of a complex interplay between the structural and physicochemical features of both the oligomers and the cell membrane... - Characterization of a novel Drosophila melanogaster acylphosphataseDonatella Degl'Innocenti
Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
FEBS Lett 535:171-4. 2003..Its activity on benzoylphosphate shows higher K(cat) but lower K(m) with respect to AcPDro. It is possible that AcPDro and AcPDro2 genes are not the direct ancestor of MT and CT vertebrate isoenzymes... - Kinetic partitioning of protein folding and aggregationFabrizio Chiti
Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
Nat Struct Biol 9:137-43. 2002.... - Structural and folding dynamic properties of the T70N variant of human lysozymeGennaro Esposito
Dipartimento di Scienze e Tecnologie Biomediche, Universita di Udine, 33100 Udine, Italy
J Biol Chem 278:25910-8. 2003..This is the opposite of the conformational variation shown by the amyloidogenic variant D67H, but it accounts for the reduced stability and catalytic performance of T70N... - Amyloid fibril formation can proceed from different conformations of a partially unfolded proteinMartino Calamai
Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom
Biophys J 89:4201-10. 2005..In addition, the structures of the resulting aggregates are largely independent of the conformational properties of their soluble precursors... - Prediction of aggregation-prone regions in structured proteinsGian Gaetano Tartaglia
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
J Mol Biol 380:425-36. 2008.... - The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation processMaria Monti
Dipartimento di Chimica Organica e Biochimica, , via Cinthia 6, 80126 Naples, Italy
J Mol Biol 336:253-62. 2004..This indicates that a considerable degree of solvent exposure is a feature of the portions of a protein that initiate the process of aggregation... - Reversal of protein aggregation provides evidence for multiple aggregated StatesMartino Calamai
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK
J Mol Biol 346:603-16. 2005.... - Rationalization of the effects of mutations on peptide and protein aggregation ratesFabrizio Chiti
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
Nature 424:805-8. 2003.... - Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricusAlessandra Corazza
Dipartimento di Scienze e Tecnologie Biomediche, Universita di Udine, Udine, Italy
Proteins 62:64-79. 2006.... - Patterns of cell death triggered in two different cell lines by HypF-N prefibrillar aggregatesMonica Bucciantini
Department of Biochemical Sciences, University of Florence, Florence, Italy
FASEB J 19:437-9. 2005.... - Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) caseSalvador Ventura
Institut de Biotecnologia i de Biomedicina and Departament de Bioquimica i Biologia Molecular, Universitat Autonoma de Barcelona, 08193 Bellaterra, Spain
Proc Natl Acad Sci U S A 101:7258-63. 2004.... - Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysisPatrizia Polverino De Laureto
CRIBI Biotechnology Centre, University of Padua, Viale G. Colombo 3, 35121, Padua, Italy
J Mol Biol 334:129-41. 2003..In addition, the disordered and non-native character of the polypeptide chains in the early aggregates could be important in determining the high cytotoxicity that has been revealed in previous studies of these species... - Prefibrillar amyloid protein aggregates share common features of cytotoxicityMonica Bucciantini
Department of Biochemical Sciences, University of Florence, Italy
J Biol Chem 279:31374-82. 2004..They also support the idea that a higher number of degenerative pathologies than previously known might be considered as protein deposition diseases... - Prefibrillar amyloid aggregates could be generic toxins in higher organismsSerena Baglioni
Department of Biochemical Sciences, University of Florence, 50134 Florence, Italy
J Neurosci 26:8160-7. 2006..These findings support the hypothesis that neurodegenerative disorders result primarily from a generic cell dysfunction caused by early misfolded species in the aggregation process... - Nature and significance of the interactions between amyloid fibrils and biological polyelectrolytesMartino Calamai
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK
Biochemistry 45:12806-15. 2006.... - Rational design of aggregation-resistant bioactive peptides: reengineering human calcitoninSusan B Fowler
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom
Proc Natl Acad Sci U S A 102:10105-10. 2005..The results suggest that this approach could be used successfully to enhance the solubility and efficacy of a wide range of other peptide and protein therapeutics... - Prediction of the absolute aggregation rates of amyloidogenic polypeptide chainsKateri F DuBay
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
J Mol Biol 341:1317-26. 2004..These results indicate that the formation of protein aggregates can be rationalised to a considerable extent in terms of simple physico-chemical parameters that describe the properties of polypeptide chains and their environment... - Insight into the structure of amyloid fibrils from the analysis of globular proteinsAntonio Trovato
Consorzio Nazionale Interuniversitario per le Scienze Fisiche della Materia, Unità di Padova, Padua, Italy
PLoS Comput Biol 2:e170. 2006..They also suggest that side chain-side chain interaction across neighbouring beta-strands is a key determinant of amyloid fibril formation and of their self-propagating ability... - Systematic in vivo analysis of the intrinsic determinants of amyloid Beta pathogenicityLeila M Luheshi
Department of Chemistry, University of Cambridge, Cambridge, United Kingdom
PLoS Biol 5:e290. 2007.... - Amyloid fibril formation and disaggregation of fragment 1-29 of apomyoglobin: insights into the effect of pH on protein fibrillogenesisPaola Picotti
CRIBI Biotechnology Centre, University of Padua, Viale G Colombo 3, 35121 Padua, Italy
J Mol Biol 367:1237-45. 2007..The results observed here for apoMb(1-29) provide an experimental basis for explaining the effect of charge and pH on amyloid fibril formation by both unfolded and folded protein systems... - Equilibrium collapse and the kinetic 'foldability' of proteinsIan S Millet
Department of Applied Physics, Stanford University, Stanford, California 92343, USA
Biochemistry 41:321-5. 2002..Thus, while sigma approximately 0 may be a necessary condition to ensure rapid folding, differences in sigma do not account for the wide range of rates and mechanisms with which naturally occurring proteins fold... - Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteinsKaren L Maxwell
Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada
Protein Sci 14:602-16. 2005..The goal of our efforts is to set uniform standards for the experimental community and to initiate an accumulating, self-consistent data set that will aid ongoing efforts to understand the folding process...