Massimo Stefani

Summary

Affiliation: University of Florence
Country: Italy

Publications

  1. doi request reprint Structural features and cytotoxicity of amyloid oligomers: implications in Alzheimer's disease and other diseases with amyloid deposits
    Massimo Stefani
    Department of Biochemical Sciences and Research Centre on the Molecular Basis of Neurodegeneration, University of Florence, V le Morgagni 50, 50134 Florence, Italy
    Prog Neurobiol 99:226-45. 2012
  2. ncbi request reprint Biological surfaces as catalysts of amyloid aggregate nucleation and primary sites of amyloid toxicity
    Massimo Stefani
    Department of Biochemical Sciences, Research Centre on the Molecular Basis of Neurodegeneration, University of Florence, Florence, Italy
    Ital J Biochem 55:194-204. 2006
  3. ncbi request reprint Structural polymorphism of amyloid oligomers and fibrils underlies different fibrillization pathways: immunogenicity and cytotoxicity
    Massimo Stefani
    Department of Biochemical Sciences and Research Centre on the Molecular Basis of Neurodegeneration, University of Florence, Florence, Italy
    Curr Protein Pept Sci 11:343-54. 2010
  4. doi request reprint Biochemical and biophysical features of both oligomer/fibril and cell membrane in amyloid cytotoxicity
    Massimo Stefani
    Department of Biochemical Sciences, University of Florence, Florence, Italy
    FEBS J 277:4602-13. 2010
  5. ncbi request reprint Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution
    Massimo Stefani
    Department of Biochemical Sciences, University of Florence, Viale Morgagni 50, 50134 Florence, Italy
    J Mol Med (Berl) 81:678-99. 2003
  6. ncbi request reprint Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world
    Massimo Stefani
    Department of Biochemical Sciences, University of Florence, Viale Morgagni 50, 50134 Florence, Italy
    Biochim Biophys Acta 1739:5-25. 2004
  7. pmc Protein folding and misfolding on surfaces
    Massimo Stefani
    Department of Biochemical Sciences and Research Centre on the Molecular Basis of Neurodegeneration CIMN, University of Florence, Florence, Italy E Mail Tel 39 055 4398307
    Int J Mol Sci 9:2515-42. 2008
  8. ncbi request reprint Cholesterol in Alzheimer's disease: unresolved questions
    Massimo Stefani
    Department of Biochemical Sciences and Research Centre on Neurodegeneration CIMN, University of Florence, Florence, Italy
    Curr Alzheimer Res 6:15-29. 2009
  9. ncbi request reprint Generic cell dysfunction in neurodegenerative disorders: role of surfaces in early protein misfolding, aggregation, and aggregate cytotoxicity
    Massimo Stefani
    Department of Biochemical Sciences and Research Centre on the Molecular Basis of Neurodegeneration, University of Florence, Florence, Italy
    Neuroscientist 13:519-31. 2007
  10. ncbi request reprint What the use of disease-unrelated model proteins can tell us about the molecular basis of amyloid aggregation and toxicity
    Massimo Stefani
    Department of Biochemical Sciences, University of Florence
    Ital J Biochem 52:162-76. 2003

Collaborators

Detail Information

Publications53

  1. doi request reprint Structural features and cytotoxicity of amyloid oligomers: implications in Alzheimer's disease and other diseases with amyloid deposits
    Massimo Stefani
    Department of Biochemical Sciences and Research Centre on the Molecular Basis of Neurodegeneration, University of Florence, V le Morgagni 50, 50134 Florence, Italy
    Prog Neurobiol 99:226-45. 2012
    ....
  2. ncbi request reprint Biological surfaces as catalysts of amyloid aggregate nucleation and primary sites of amyloid toxicity
    Massimo Stefani
    Department of Biochemical Sciences, Research Centre on the Molecular Basis of Neurodegeneration, University of Florence, Florence, Italy
    Ital J Biochem 55:194-204. 2006
    ..Each of these steps is most likely influenced by the physicochemical and biochemical features of the membrane(s) themselves in ways that are still under investigation. This review summarizes the most recent advances in these fields...
  3. ncbi request reprint Structural polymorphism of amyloid oligomers and fibrils underlies different fibrillization pathways: immunogenicity and cytotoxicity
    Massimo Stefani
    Department of Biochemical Sciences and Research Centre on the Molecular Basis of Neurodegeneration, University of Florence, Florence, Italy
    Curr Protein Pept Sci 11:343-54. 2010
    ..Important clues into the structure-toxicity relation of amyloids, the role performed by natural surfaces in oligomer growth and the molecular basis of oligomer-membrane interaction are also emerging...
  4. doi request reprint Biochemical and biophysical features of both oligomer/fibril and cell membrane in amyloid cytotoxicity
    Massimo Stefani
    Department of Biochemical Sciences, University of Florence, Florence, Italy
    FEBS J 277:4602-13. 2010
    ....
  5. ncbi request reprint Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution
    Massimo Stefani
    Department of Biochemical Sciences, University of Florence, Viale Morgagni 50, 50134 Florence, Italy
    J Mol Med (Berl) 81:678-99. 2003
    ..It also suggests some intriguing new factors that could be of great significance in the evolution of biological molecules and the mechanisms that regulate their behaviour...
  6. ncbi request reprint Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world
    Massimo Stefani
    Department of Biochemical Sciences, University of Florence, Viale Morgagni 50, 50134 Florence, Italy
    Biochim Biophys Acta 1739:5-25. 2004
    ..The present review focuses the most recent reports supporting these ideas and discusses their clinical and biological significance...
  7. pmc Protein folding and misfolding on surfaces
    Massimo Stefani
    Department of Biochemical Sciences and Research Centre on the Molecular Basis of Neurodegeneration CIMN, University of Florence, Florence, Italy E Mail Tel 39 055 4398307
    Int J Mol Sci 9:2515-42. 2008
    ....
  8. ncbi request reprint Cholesterol in Alzheimer's disease: unresolved questions
    Massimo Stefani
    Department of Biochemical Sciences and Research Centre on Neurodegeneration CIMN, University of Florence, Florence, Italy
    Curr Alzheimer Res 6:15-29. 2009
    ..The aim of this review is to critically discuss some of the main results reported in the recent years in this field supporting a role of cholesterol either as a susceptibility factor or as a protective agent in AD...
  9. ncbi request reprint Generic cell dysfunction in neurodegenerative disorders: role of surfaces in early protein misfolding, aggregation, and aggregate cytotoxicity
    Massimo Stefani
    Department of Biochemical Sciences and Research Centre on the Molecular Basis of Neurodegeneration, University of Florence, Florence, Italy
    Neuroscientist 13:519-31. 2007
    ..Recent research has highlighted the involvement of surfaces as protein-misfolding chaperones and aggregation catalysts and their effects in these phenomena...
  10. ncbi request reprint What the use of disease-unrelated model proteins can tell us about the molecular basis of amyloid aggregation and toxicity
    Massimo Stefani
    Department of Biochemical Sciences, University of Florence
    Ital J Biochem 52:162-76. 2003
    ..In addition, it rises intriguing considerations on protein and cell evolution as well as on amyloid disease pathogenesis...
  11. doi request reprint A causative link between the structure of aberrant protein oligomers and their toxicity
    Silvia Campioni
    Department of Biochemical Sciences, University of Florence, Florence, Italy
    Nat Chem Biol 6:140-7. 2010
    ..Our findings suggest that structural flexibility and hydrophobic exposure are primary determinants of the ability of oligomeric assemblies to cause cellular dysfunction and its consequences, such as neurodegeneration...
  12. doi request reprint Differentiation increases the resistance of neuronal cells to amyloid toxicity
    Cristina Cecchi
    Department of Biochemical Sciences, University of Florence, Viale Morgagni 50, 50134, Florence, Italy
    Neurochem Res 33:2516-31. 2008
    ..Finally, increasing the content of membrane cholesterol resulted in a remarkable reduction of vulnerability and ability to bind the aggregates in either undifferentiated and differentiated cells...
  13. pmc Synthetic lipid vesicles recruit native-like aggregates and affect the aggregation process of the prion Ure2p: insights on vesicle permeabilization and charge selectivity
    Laura Pieri
    Department of Biochemical Sciences, University of Florence, Italy Research Centre on the Molecular Basis of Neurodegeneration, University of Florence, Italy
    Biophys J 96:3319-30. 2009
    ..These data suggest that soluble Ure2p oligomers and native-like fibrils, but not amyloid fibrils, interact intimately with negatively charged lipid membranes, where they allow selective cation influx...
  14. ncbi request reprint 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...
  15. ncbi request reprint Replicating neuroblastoma cells in different cell cycle phases display different vulnerability to amyloid toxicity
    Cristina Cecchi
    Department of Biochemical Sciences, University of Florence, Viale Morgagni 50, 50134, Florence, Italy
    J Mol Med (Berl) 86:197-209. 2008
    ..The high vulnerability of S cells to aggregate toxicity extends previous data suggesting that neuronal loss in AD could result from mitotic reactivation of terminally differentiated neurons with arrest in the S phase...
  16. ncbi request reprint 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
    ....
  17. doi request reprint A protective role for lipid raft cholesterol against amyloid-induced membrane damage in human neuroblastoma cells
    Cristina Cecchi
    Department of Biochemical Sciences, University of Florence, Viale Morgagni 50, 50134 Florence, Italy
    Biochim Biophys Acta 1788:2204-16. 2009
    ..Our data suggest that cholesterol reduces amyloid-induced membrane modifications at the lipid raft level by altering raft physicochemical features...
  18. ncbi request reprint 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
    ....
  19. ncbi request reprint 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...
  20. ncbi request reprint 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
    ....
  21. pmc The (1-63) region of the p53 transactivation domain aggregates in vitro into cytotoxic amyloid assemblies
    Stefania Rigacci
    Department of Biochemical Sciences, University of Florence, 50134 Florence, Italy
    Biophys J 94:3635-46. 2008
    ....
  22. ncbi request reprint The yeast prion Ure2p native-like assemblies are toxic to mammalian cells regardless of their aggregation state
    Laura Pieri
    Department of Biochemical Sciences, Interuniversity Centre for the Study of the Molecular Basis of Neurodegenerative Diseases, University of Florence, Florence 50134, Italy
    J Biol Chem 281:15337-44. 2006
    ....
  23. ncbi request reprint Differing molecular mechanisms appear to underlie early toxicity of prefibrillar HypF-N aggregates to different cell types
    Cristina Cecchi
    Department of Biochemical Sciences, University of Florence, Italy
    FEBS J 273:2206-22. 2006
    ....
  24. ncbi request reprint 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 request reprint 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...
  26. ncbi request reprint Aβ(1-42) aggregates into non-toxic amyloid assemblies in the presence of the natural polyphenol oleuropein aglycon
    Stefania Rigacci
    Department of Biochemical Sciences, University of Florence, Viale Morgagni 50, 50134 Florence, Italy
    Curr Alzheimer Res 8:841-52. 2011
    ..The possible use of this polyphenol as anti-aggregation molecule is discussed in the light of these data...
  27. 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
    ....
  28. ncbi request reprint 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...
  29. doi request reprint Toxic effects of amyloid fibrils on cell membranes: the importance of ganglioside GM1
    Monica Bucciantini
    Department of Biochemical Sciences, University of Florence, Florence, Italy
    FASEB J 26:818-31. 2012
    ....
  30. ncbi request reprint 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...
  31. ncbi request reprint The intrachain disulfide bridge is responsible of the unusual stability properties of novel acylphosphatase from Escherichia coli
    Matteo Ramazzotti
    Department of Biochemical Sciences, University of Florence, V le Morgagni 50, 50134 Firenze, Italy
    FEBS Lett 580:6763-8. 2006
    ..Site directed mutagenesis suggests that, together with other structural features, the intrachain S-S bridge in EcoAcP is involved in a remarkable thermal and chemical stabilization of the protein without affecting its catalytic activity...
  32. doi request reprint Neuronal differentiation of human mesenchymal stromal cells increases their resistance to Aβ42 aggregate toxicity
    Cristina Cecchi
    Department of Biochemical Sciences, and Research Centre on the Molecular Basis of Neurodegeneration CIMN, Florence, Italy
    J Alzheimers Dis 27:651-64. 2011
    ..These findings extend our knowledge of stem cell vulnerability to amyloid species, which remains a controversial issue, and confirm that amyloid-GM1 interactions play an important role in cell impairment...
  33. ncbi request reprint 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...
  34. ncbi request reprint 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...
  35. doi request reprint Oleuropein aglycon prevents cytotoxic amyloid aggregation of human amylin
    Stefania Rigacci
    Department of Biochemical Sciences, University of Florence, Florence, Italy
    J Nutr Biochem 21:726-35. 2010
    ....
  36. doi request reprint Oleuropein aglycone counteracts Aβ42 toxicity in the rat brain
    Ilaria Luccarini
    Department of Neuroscience, Psychology, Drug Research and Child Health, Division of Pharmacology and Toxicology, University of Florence, 50139 Florence, Italy
    Neurosci Lett 558:67-72. 2014
    ..Altogether, these data provide additional support to the anti-aggregation, neuroprotective and anti-inflammatory activities of this natural phenol, confirming its beneficial properties against neurodegeneration. ..
  37. doi request reprint Proteomic analysis of cells exposed to prefibrillar aggregates of HypF-N
    Francesca Magherini
    Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, Italy
    Biochim Biophys Acta 1794:1243-50. 2009
    ..The levels of some of the differently expressed proteins were modified also in similar studies carried out on cells exposed to Abeta or alpha-synuclein aggregates, supporting the existence of shared features of amyloid cytotoxicity...
  38. pmc The polyphenol oleuropein aglycone protects TgCRND8 mice against Aß plaque pathology
    Cristina Grossi
    Department of Neuroscience, Psychology, Drug Research and Child Health, Division of Pharmacology and Toxicology, University of Florence, Florence, Italy
    PLoS ONE 8:e71702. 2013
    ..Our results support, and provide mechanistic insights into, the beneficial effects against Alzheimer-associated neurodegeneration of a polyphenol enriched in the extra virgin olive oil, a major component of the Mediterranean diet. ..
  39. ncbi request reprint 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
    ....
  40. doi request reprint The amyloid-cell membrane system. The interplay between the biophysical features of oligomers/fibrils and cell membrane defines amyloid toxicity
    Cristina Cecchi
    Department of Biomedical Experimental and Clinical Sciences and Research Centre on the Molecular Basis of Neurodegeneration, University of Florence, Florence, Italy
    Biophys Chem 182:30-43. 2013
    ..Finally, a recent view describes amyloid toxicity as an emerging property dependent on a complex interplay between the biophysical features of early aggregates and the interacting cell membranes taken as a whole system. ..
  41. pmc Protein folding and aggregation into amyloid: the interference by natural phenolic compounds
    Massimo Stefani
    Department of Experimental and Clinical Biomedical Sciences, University of Florence, Viale Morgagni 50, Florence 50134, Italy
    Int J Mol Sci 14:12411-57. 2013
    ....
  42. ncbi request reprint 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
    ....
  43. ncbi request reprint Crystallization and preliminary X-ray characterization of the acylphosphatase-like domain from the Escherichia coli hydrogenase maturation factor HypF
    Camillo Rosano
    Advanced Biotechnology Center IST, Largo Rosanna Benzi 10, 16132 Genoa, Italy
    Acta Crystallogr D Biol Crystallogr 58:524-5. 2002
    ..5, b = 59.8, c = 87.6 A) and to the rhombohedral space group R32 (unit-cell parameters a = b = 58.1, c = 155.6 A in the hexagonal setting)...
  44. pmc Natively folded HypF-N and its early amyloid aggregates interact with phospholipid monolayers and destabilize supported phospholipid bilayers
    Claudio Canale
    Department of Physics, University of Genoa, Genoa, Italy
    Biophys J 91:4575-88. 2006
    ..These results support the idea that, at least in most cases, early amyloid aggregates of different peptides and proteins produce similar effects on the integrity of membrane assembly and hence on cell viability...
  45. 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...
  46. ncbi request reprint Crystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domain
    Camillo Rosano
    National Institute for Cancer Research, IST Largo R Benzi, 10, I 16132 Genova, Italy
    J Mol Biol 321:785-96. 2002
    ..The crystallographic analyses here reported were undertaken to shed light on the molecular bases of inactivity, folding, misfolding and aggregation of the HypF N-terminal acylphosphatase domain...
  47. ncbi request reprint Insights into the molecular basis of the differing susceptibility of varying cell types to the toxicity of amyloid aggregates
    Cristina Cecchi
    Department of Biochemical Sciences
    J Cell Sci 118:3459-70. 2005
    ..Our data depict membrane destabilization and the subsequent early derangement of ion balance and intracellular redox status as key events in targeting exposed cells to apoptotic death...
  48. pmc Preliminary characterization of two different crystal forms of acylphosphatase from the hyperthermophile archaeon Sulfolobus solfataricus
    Simone Zuccotti
    Department of Physics INFM, Center of Excellence for Biomedical Research, University of Genova, Via Dodecaneso 33, 16132 Genova, Italy
    Acta Crystallogr Sect F Struct Biol Cryst Commun 61:144-6. 2005
    ..Here, the growth and characterization of a triclinic and a monoclinic crystal form of the hyperthermophilic enzyme are reported; X-ray diffraction data have been collected to 1.27 and 1.90 A resolution, respectively...
  49. ncbi request reprint Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils
    Annalisa Relini
    National Institute for the Physics of Matter and Department of Physics, University of Genoa, Genoa 16146, Italy
    J Mol Biol 338:943-57. 2004
    ..These data complement previously reported findings, and support the idea that protein aggregation, aggregate structure and toxicity are generic properties of polypeptide chains...
  50. 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...
  51. ncbi request reprint 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
    ....
  52. ncbi request reprint Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase
    Simone Zuccotti
    Department of Physics INFM and Center of Excellence for Biomedical Research, University of Genova, Via Dodecaneso 33, 16132 Genova, Italy
    Acta Crystallogr D Biol Crystallogr 60:1177-9. 2004
    ..8, c = 98.6 angstroms, gamma = 120 degrees, allowed the solution of the protein structure by molecular replacement and its refinement to 1.5 angstroms resolution. The AcPDro2 active-site structure is discussed...
  53. ncbi request reprint 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
    ....