Fabrizio Chiti

Summary

Affiliation: University of Florence
Country: Italy

Publications

  1. ncbi Capillary electrophoresis investigation of a partially unfolded conformation of beta(2)-microglobulin
    Ersilia De Lorenzi
    Department of Pharmaceutical Chemistry, University of Pavia, Viale Taramelli 12, I 27100 Pavia, Italy
    Electrophoresis 23:918-25. 2002
  2. ncbi Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases
    Amol P Pawar
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    J Mol Biol 350:379-92. 2005
  3. pmc Aggregation propensity of the human proteome
    Elodie Monsellier
    Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, Florence, Italy
    PLoS Comput Biol 4:e1000199. 2008
  4. doi Amyloid formation by globular proteins under native conditions
    Fabrizio Chiti
    Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, Viale Morgagni 50, I 50134 Firenze, Italy
    Nat Chem Biol 5:15-22. 2009
  5. ncbi Protein misfolding, functional amyloid, and human disease
    Fabrizio Chiti
    Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, I 50134 Firenze, Italy
    Annu Rev Biochem 75:333-66. 2006
  6. doi Structure and dynamics of a partially folded protein are decoupled from its mechanism of aggregation
    Giulia Calloni
    Dipartimento di Scienze Biochimiche, Universita di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
    J Am Chem Soc 130:13040-50. 2008
  7. pmc Amyloid formation of a protein in the absence of initial unfolding and destabilization of the native state
    Gemma Soldi
    Dipartimento di Scienze Biochimiche, Universita di Firenze, Firenze, Italy
    Biophys J 89:4234-44. 2005
  8. pmc Agitation and high ionic strength induce amyloidogenesis of a folded PDZ domain in native conditions
    Alessandro Sicorello
    Dipartimento di Scienze Biochimiche, Universita di Firenze, Florence, Italy
    Biophys J 96:2289-98. 2009
  9. ncbi Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates
    Georgia Plakoutsi
    Dipartimento di Scienze Biochimiche, Universita di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
    J Mol Biol 351:910-22. 2005
  10. pmc Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase
    Francesco Bemporad
    Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, 50134, Firenze, Italy
    Protein Sci 15:862-70. 2006

Collaborators

Detail Information

Publications61

  1. ncbi Capillary electrophoresis investigation of a partially unfolded conformation of beta(2)-microglobulin
    Ersilia De Lorenzi
    Department of Pharmaceutical Chemistry, University of Pavia, Viale Taramelli 12, I 27100 Pavia, Italy
    Electrophoresis 23:918-25. 2002
    ....
  2. ncbi Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases
    Amol P Pawar
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    J Mol Biol 350:379-92. 2005
    ....
  3. pmc Aggregation propensity of the human proteome
    Elodie 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...
  4. doi Amyloid formation by globular proteins under native conditions
    Fabrizio 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...
  5. ncbi Protein misfolding, functional amyloid, and human disease
    Fabrizio Chiti
    Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, I 50134 Firenze, Italy
    Annu Rev Biochem 75:333-66. 2006
    ....
  6. doi Structure and dynamics of a partially folded protein are decoupled from its mechanism of aggregation
    Giulia 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...
  7. pmc Amyloid formation of a protein in the absence of initial unfolding and destabilization of the native state
    Gemma Soldi
    Dipartimento di Scienze Biochimiche, Universita di Firenze, Firenze, Italy
    Biophys J 89:4234-44. 2005
    ....
  8. pmc Agitation and high ionic strength induce amyloidogenesis of a folded PDZ domain in native conditions
    Alessandro 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...
  9. ncbi Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates
    Georgia Plakoutsi
    Dipartimento di Scienze Biochimiche, Universita di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
    J Mol Biol 351:910-22. 2005
    ....
  10. pmc Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase
    Francesco Bemporad
    Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, 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...
  11. doi The folding process of acylphosphatase from Escherichia coli is remarkably accelerated by the presence of a disulfide bond
    Claudia 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...
  12. ncbi Investigating the effects of mutations on protein aggregation in the cell
    Giulia 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...
  13. ncbi Relative influence of hydrophobicity and net charge in the aggregation of two homologous proteins
    Martino Calamai
    Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
    Biochemistry 42:15078-83. 2003
    ....
  14. pmc Kinetic analysis of amyloid formation in the presence of heparan sulfate: faster unfolding and change of pathway
    Neda 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...
  15. ncbi Comparison of the folding processes of distantly related proteins. Importance of hydrophobic content in folding
    Giulia Calloni
    Dipartimento di Scienze Biochimiche, Universita di Firenze, Viale Morgagni 50, 50134 Florence, Italy
    J Mol Biol 330:577-91. 2003
    ....
  16. ncbi Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregation
    Claudia 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...
  17. doi Conformational properties of the aggregation precursor state of HypF-N
    Silvia 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...
  18. doi The degree of structural protection at the edge beta-strands determines the pathway of amyloid formation in globular proteins
    Gemma 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...
  19. doi Salt anions promote the conversion of HypF-N into amyloid-like oligomers and modulate the structure of the oligomers and the monomeric precursor state
    Silvia 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...
  20. doi Low-level expression of a folding-incompetent protein in Escherichia coli: search for the molecular determinants of protein aggregation in vivo
    Julia Winkelmann
    Department of Biochemical Sciences, University of Florence, Viale Morgagni 50, 50134 Firenze, Italy
    J Mol Biol 398:600-13. 2010
    ....
  21. ncbi Amyloid formation from HypF-N under conditions in which the protein is initially in its native state
    Giordana 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...
  22. pmc Biological function in a non-native partially folded state of a protein
    Francesco 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...
  23. ncbi Protein aggregation starting from the native globular state
    Giordana Marcon
    Universita di Firenze, Dipartimento di Scienze Biochimiche, Firenze, Italy
    Methods Enzymol 413:75-91. 2006
    ....
  24. ncbi Studying the folding process of the acylphosphatase from Sulfolobus solfataricus. A comparative analysis with other proteins from the same superfamily
    Francesco Bemporad
    Dipartimento di Scienze Biochimiche, Universita di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
    Biochemistry 43:9116-26. 2004
    ....
  25. doi Glycosaminoglycans (GAGs) suppress the toxicity of HypF-N prefibrillar aggregates
    Theodora Saridaki
    Department of Biochemical Sciences, University of Florence, Viale Morgagni 50, 50134 Florence, Italy
    J Mol Biol 421:616-30. 2012
    ....
  26. ncbi Stabilization of a native protein mediated by ligand binding inhibits amyloid formation independently of the aggregation pathway
    Gemma Soldi
    Dipartimento di Scienze Biochimiche, Universita di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
    J Med Chem 49:6057-64. 2006
    ....
  27. pmc Prevention of amyloid-like aggregation as a driving force of protein evolution
    Elodie Monsellier
    Dipartimento di Scienze Biochimiche, Universita di Firenze, Viale Morgagni 50, I 50134, Firenze, Italy
    EMBO Rep 8:737-42. 2007
    ....
  28. pmc Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases
    Fabrizio Chiti
    Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, Viale Morgagni 50, 50134 Florence, Italy
    Proc Natl Acad Sci U S A 99:16419-26. 2002
    ....
  29. ncbi Selection of antibody fragments specific for an alpha-helix region of acylphosphatase
    Donatella 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...
  30. ncbi Exploring the mechanism of formation of native-like and precursor amyloid oligomers for the native acylphosphatase from Sulfolobus solfataricus
    Georgia Plakoutsi
    Dipartimento di Scienze Biochimiche, Universita di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
    Structure 14:993-1001. 2006
    ....
  31. doi A model for the aggregation of the acylphosphatase from Sulfolobus solfataricus in its native-like state
    Francesco 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...
  32. ncbi Sequence and structural determinants of amyloid fibril formation
    Francesco Bemporad
    Dipartimento di Scienze Biochimiche, Universita di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
    Acc Chem Res 39:620-7. 2006
    ....
  33. ncbi Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    Monica 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...
  34. pmc Large proteins have a great tendency to aggregate but a low propensity to form amyloid fibrils
    Hassan Ramshini
    Dipartimento di Scienze Biochimiche, Universita di Firenze, Florence, Italy
    PLoS ONE 6:e16075. 2011
    ....
  35. pmc A computational approach for identifying the chemical factors involved in the glycosaminoglycans-mediated acceleration of amyloid fibril formation
    Elodie 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...
  36. ncbi Aggregation of the Acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursors for amyloid formation
    Georgia 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...
  37. doi Amyloid formation by the model protein muscle acylphosphatase is accelerated by heparin and heparan sulphate through a scaffolding-based mechanism
    Neda 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
    ....
  38. pmc The distribution of residues in a polypeptide sequence is a determinant of aggregation optimized by evolution
    Elodie Monsellier
    Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, Florence, Italy
    Biophys J 93:4382-91. 2007
    ....
  39. doi Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomers
    Elisa 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...
  40. ncbi Characterization of a novel Drosophila melanogaster acylphosphatase
    Donatella 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...
  41. ncbi Kinetic partitioning of protein folding and aggregation
    Fabrizio Chiti
    Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
    Nat Struct Biol 9:137-43. 2002
    ....
  42. ncbi The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process
    Maria Monti
    Dipartimento di Chimica Organica e Biochimica, Universita di Napoli Federico II, 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...
  43. ncbi Patterns of cell death triggered in two different cell lines by HypF-N prefibrillar aggregates
    Monica Bucciantini
    Department of Biochemical Sciences, University of Florence, Florence, Italy
    FASEB J 19:437-9. 2005
    ....
  44. pmc Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case
    Salvador 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
    ....
  45. ncbi Reversal of protein aggregation provides evidence for multiple aggregated States
    Martino Calamai
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK
    J Mol Biol 346:603-16. 2005
    ....
  46. doi Prediction of aggregation-prone regions in structured proteins
    Gian Gaetano Tartaglia
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    J Mol Biol 380:425-36. 2008
    ....
  47. ncbi Structural and folding dynamic properties of the T70N variant of human lysozyme
    Gennaro 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...
  48. ncbi Rationalization of the effects of mutations on peptide and protein aggregation rates
    Fabrizio Chiti
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    Nature 424:805-8. 2003
    ....
  49. ncbi Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus
    Alessandra Corazza
    Dipartimento di Scienze e Tecnologie Biomediche, Universita di Udine, Udine, Italy
    Proteins 62:64-79. 2006
    ....
  50. pmc Amyloid fibril formation can proceed from different conformations of a partially unfolded protein
    Martino 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...
  51. ncbi Equilibrium collapse and the kinetic 'foldability' of proteins
    Ian 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...
  52. pmc Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins
    Karen 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...
  53. ncbi Amyloid fibril formation and disaggregation of fragment 1-29 of apomyoglobin: insights into the effect of pH on protein fibrillogenesis
    Paola 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...
  54. ncbi Prefibrillar amyloid aggregates could be generic toxins in higher organisms
    Serena 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...
  55. pmc Rational design of aggregation-resistant bioactive peptides: reengineering human calcitonin
    Susan 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...
  56. ncbi Nature and significance of the interactions between amyloid fibrils and biological polyelectrolytes
    Martino Calamai
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK
    Biochemistry 45:12806-15. 2006
    ....
  57. ncbi Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis
    Patrizia 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...
  58. pmc Systematic in vivo analysis of the intrinsic determinants of amyloid Beta pathogenicity
    Leila M Luheshi
    Department of Chemistry, University of Cambridge, Cambridge, United Kingdom
    PLoS Biol 5:e290. 2007
    ....
  59. pmc Insight into the structure of amyloid fibrils from the analysis of globular proteins
    Antonio 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...
  60. ncbi Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains
    Kateri 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...
  61. ncbi Prefibrillar amyloid protein aggregates share common features of cytotoxicity
    Monica 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...