Research Topics
| Massimo StefaniSummaryAffiliation: University of Florence Country: Italy Publications
| Collaborators
|
Detail Information
Publications
Structural features and cytotoxicity of amyloid oligomers: implications in Alzheimer's disease and other diseases with amyloid depositsMassimo 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....
Protein folding and misfolding on surfacesMassimo 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....
What the use of disease-unrelated model proteins can tell us about the molecular basis of amyloid aggregation and toxicityMassimo 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...- Biological surfaces as catalysts of amyloid aggregate nucleation and primary sites of amyloid toxicityMassimo 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... - Generic cell dysfunction in neurodegenerative disorders: role of surfaces in early protein misfolding, aggregation, and aggregate cytotoxicityMassimo 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... - Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolutionMassimo 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... - Structural polymorphism of amyloid oligomers and fibrils underlies different fibrillization pathways: immunogenicity and cytotoxicityMassimo 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... - Cholesterol in Alzheimer's disease: unresolved questionsMassimo 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... - Biochemical and biophysical features of both oligomer/fibril and cell membrane in amyloid cytotoxicityMassimo Stefani
Department of Biochemical Sciences, University of Florence, Florence, Italy
FEBS J 277:4602-13. 2010.... - Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein worldMassimo 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... - A causative link between the structure of aberrant protein oligomers and their toxicitySilvia 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... - Differentiation increases the resistance of neuronal cells to amyloid toxicityCristina 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... - 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... - Synthetic lipid vesicles recruit native-like aggregates and affect the aggregation process of the prion Ure2p: insights on vesicle permeabilization and charge selectivityLaura 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... - Replicating neuroblastoma cells in different cell cycle phases display different vulnerability to amyloid toxicityCristina 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... - 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.... - A protective role for lipid raft cholesterol against amyloid-induced membrane damage in human neuroblastoma cellsCristina 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... - 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 (1-63) region of the p53 transactivation domain aggregates in vitro into cytotoxic amyloid assembliesStefania Rigacci
Department of Biochemical Sciences, University of Florence, 50134 Florence, Italy
Biophys J 94:3635-46. 2008.... - 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... - 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.... - Differing molecular mechanisms appear to underlie early toxicity of prefibrillar HypF-N aggregates to different cell typesCristina Cecchi
Department of Biochemical Sciences, University of Florence, Italy
FEBS J 273:2206-22. 2006.... - The yeast prion Ure2p native-like assemblies are toxic to mammalian cells regardless of their aggregation stateLaura 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.... - 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.... - 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... - Aβ(1-42) aggregates into non-toxic amyloid assemblies in the presence of the natural polyphenol oleuropein aglyconStefania 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... - 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... - 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.... - Toxic effects of amyloid fibrils on cell membranes: the importance of ganglioside GM1Monica Bucciantini
Department of Biochemical Sciences, University of Florence, Florence, Italy
FASEB J 26:818-31. 2012.... - 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... - The intrachain disulfide bridge is responsible of the unusual stability properties of novel acylphosphatase from Escherichia coliMatteo 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... - Neuronal differentiation of human mesenchymal stromal cells increases their resistance to Aβ42 aggregate toxicityCristina 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... - 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... - 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... - Oleuropein aglycon prevents cytotoxic amyloid aggregation of human amylinStefania Rigacci
Department of Biochemical Sciences, University of Florence, Florence, Italy
J Nutr Biochem 21:726-35. 2010.... - Proteomic analysis of cells exposed to prefibrillar aggregates of HypF-NFrancesca 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... - 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.... - Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrilsAnnalisa 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... - 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... - 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.... - 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.... - Crystallization and preliminary X-ray characterization of the acylphosphatase-like domain from the Escherichia coli hydrogenase maturation factor HypFCamillo 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)... - Natively folded HypF-N and its early amyloid aggregates interact with phospholipid monolayers and destabilize supported phospholipid bilayersClaudio 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... - 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.... - Insights into the molecular basis of the differing susceptibility of varying cell types to the toxicity of amyloid aggregatesCristina 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... - 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... - Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphataseSimone 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... - Crystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domainCamillo 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... - Preliminary characterization of two different crystal forms of acylphosphatase from the hyperthermophile archaeon Sulfolobus solfataricusSimone 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...