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Fabrizio CHITI

Ruolo attuale:: Professore Ordinario
SSD:: BIOS-07/A - Biochimica
Afferenza organizzativa:: Dipartimento di Scienze Biomediche, Sperimentali e Cliniche 'Mario Serio'

Recapiti

	0552751220
	fabrizio.chiti(AT)unifi.it

Ulteriori Recapiti

http://www.fabriziochiti.it

Fabrizio CHITI

Curriculum

Personalia

Work address: Dipartimento di Scienze Biomediche Sperimentali e Cliniche, Sezione di Scienze Biohchimiche, Università di Firenze, Viale Morgagni 50, I-50134 Firenze
Phone (lab) +39-055-2751220
e-mail fabrizio.chiti/at/unifi.it
web page http://www.fabriziochiti.it
Place and Date of birth: Florence (Italy) on 7^th July 1971
Sex: Male
Nationality: Italian
Marital Status: Married to Giada Socci since 1999, two children.

Education

20/12/1995M.Sc. Degree (Laurea vecchio ordinamento) in Biological Sciences at the University of Florence (Italy). Final marks were 110/110 cum laude et encomium.
20/05/2000PhD degree (D.Phil) in Chemistry at the University of Oxford (United Kingdom) with a thesis titled “Folding Studies of Acylphosphatase”. Supervisor was Prof. Christopher M. Dobson. Examiners were Martin Karplus and Alan Fersht.

Research Experience

01/10/1996 - 31/01/2000Ph.D. student in the laboratory of the Prof. C. M. Dobson, Department of Chemistry, University of Oxford (United Kingdom)
01/02/2000 - 31/01/2002Post-doc in the laboratory of Prof. G. Ramponi, Department of Biochemistry, University of Florence (Italy)
01/02/2002 - 31/10/2002Post-doc in the laboratory of Prof. C. M. Dobson, Department of Chemistry, University of Cambridge (UK)
01/11/2002 – 30/12/2010Associate Professor of Biochemistry, affiliated to the Department of Biochemistry for research and to the Faculty of Medicine for teaching, University of Florence (Italy)
30/12/2010 - presentFull Professor of Biochemistry, affiliated to the Department of Biochemistry for research and to the Faculty of Medicine for teaching, University of Florence (Italy)

Academic Honours

7/10/1996 - 8/10/1998“Marie Curie” Fellowship from the European Commission (no. BI04CT965113)
9/10/1998 – 8/01/1999Research Prize (Premio di Ricerca) from the Italian Society of Biochemistry
01/02/1999 – 31/01/2000“Giuseppe Guelfi” Training Fellowship (Borsa di Perfezionamento) from the Accademia Nazionale dei Lincei (no. 33/cc)
01/05/1999 – 31/08/1999Training fellowship (Contributo per Attività di Formazione) from the Consorzio Interuniversitario Biotecnologie (no. 681/u/MM/cp/98)
01/02/2000 – 31/01/2002Research Fellowship from the Italian Telethon Foundation (no. 453.bi)
13/09/1999Prize from the publishing company McGraw-Hill at the 44^th Congress of the Italian Society of Biochemistry as “author of a significant paper published from 1998 to 1999”
23/09/2000Gold Medal from the Italian Society of Biochemistry as author of the most significant poster presented at the 45^th Congress of the Italian Society of Biochemistry
27/10/2003"Jean-Francois LeFèvre Lecture" at the Ecole Supérieure de Biotechnologie de Strasbourg (ESBS)
12/10/2005Membership to the EMBO Young Investigator Programme for years 2006-2008.
Year 2005Elected Member of the Editorial Board of Protein Engineering Design and Selection
Year 2005Elected Member of the Editorial Board of Amyloid
Year 2006ElectedMember of the Centre of Excellence DENOTHE (Faculty of Medicine, University of Florence, Italy)
25-28/03/2006Elected Main organiser of the “EMBO-FEBS workshop on amyloid formation” (Florence, Italy, 25-28 March 2006)
21-25/07/2007Elected as one of the two Meeting Chairs of the 21^st Annual Symposium of the Protein Society (Boston, Massachusetts, July 21-25, 2007)
Year 2006Elected member of the Editorial Board of The Open Structural Biology Journal
23-26/09/2008Elected a one of the four main organisers of the 53th Congress of the Italian Society of Biochemistry (Riccione, Italy, 23-26 September 2008)
Year 2008Elected member of the Italian Scholarship Advisory Committee of the Giovanni Armenise-Harvard Foundation for years 2008-2010
24/06/2010 “Roncaglia-Mari” Award for the year 2010 as a main contributor in Science (the Award was presented by the Accademia Nazionale dei Lincei in the presence of the President of the Italian Republic Giorgio Napolitano)

Recent Lectures at International Meetings (years 2002-2013)

15-20 June 2002, Snowmass, Colorado. Amyloids & other abnormal protein folding processes. Invited Lecture
3-5 October 2002, Verona, Italy. Horizon Symposium on "Protein Folding and Disease" organised by the Nature Publishing Group and Aventis. Invited Lecture.
27-29 November 2002, Saitama, Japan. First international workshop "Frontiers in Molecular Neuropathology", Invited Lecture.
29 march - 2 April 2003, Firenze, Italy. Fifth European Symposium of the Protein Society. Invited Lecture.
3-5 April 2003. Roma, Italy. International congress on Protein Folding and Misfolding. Invited Lecture.
5-16 May 2003. Trieste, Italy. International Workshop on Proteomics: Protein Structure, Function and Interactions. Invited Lecture.
9-12 September 2003. Lyon, France. CECAM workshop on Protein Folding: bringing theory and experiment closer together. InvitedLecture.
17-22 October 2003. Fondation des Treilles, France. Conference on "Disorders of Protein Folding". Invited Lecture.
27 October 2003. Strasbourg, France. Jean-Francois LeFèvre Lecture at the Ecole Supérieure de Biotechnologie de Strasbourg (ESBS). Invited Lecture.
9-11 February 2004. Boston, USA. Second ICAM workshop on physical principles of amyloid diseases. Invited Lecture.
18-22 April 2004. Tours, France. Xth International Symposium on Amyloid and Amyloidosis. Invited Lecture.
13-15 May 2004. Bedlewo, Poland. Workshop on Structure and Function of Biomolecules. Invited Lecture.
4-8 July 2004. Urbino, Italy. European School of Medicinal Chemistry. Invited Lecture.
14-16 October 2004. Berlin, Germany. Formation and Stability of b-sheets. Invited Lecture.
9-13 December 2004. Pavia, Italy. International Workshop on Dialysis related amyloidosis: from molecular mechanisms to therapies. Invited Lecture.
17-20 May 2005. Aalborg, Denmark. PhD course on protein aggregation and fibrillation. Invited Lecture.
28 May - 2 June 2005. Zakopane, Italy. EMBO–FEBS Workshop on Biology of Molecular Chaperones. Invited Lecture
18-23 June 2005. San Diego, California. 19^th American peptide Symposium. Invited Lecture.
16-20 July 2005.Lausanne, Switzerland. The First International ICAM Workshop on Protein Aggregation and Amyloid Formation in Systemic and Neurodegenerative Diseases. Invited Lecture.
23-30 August 2005. Firenze, Italy. XX Congress of the International Union of Crystallography. Invited Lecture.
4-8 October 2005.Rimini, Italy. First European Conference on Chemistry for Life Sciences. Invited Lecture.
2006. Henry Stewart Talks Series, Protein Folding, Aggregation and Design. Invited Audio-visual presentation.
25-28 March 2006. Firenze, Italy. EMBO-FEBS Workshop on Amyloid Formation. Invited Lecture and Main Organiser
3-6 May 2006. Vienna, Austria. EMBO YIP Meeting. Standard Short Presentation.
22-25 May 2006. Lyon, France. CECAM Workshop on Protein Aggregation. Invited Lecture.
10-15 June 2006. Snowmass Village, Colorado. FASEB Summer Research Conference: Amyloid fibril formation, protein misfolding & Disease. Chemistry, Physiology and disease. Invited Lecture.
19-22 September 2006. Lyon, France. CECAM Workshop on Protein Folding and misfolding: bringing theory to experiment and viceversa. Invited Lecture.
17-24 September 2006. Heidelberg, Germany. EMBO YIP PhD COURSE. Invited Lecture.
12-15 April 2007. Roscoff, France. Jaques-Monod Conference. Invited Lecture.
19-21 May 2007. Milan, Italy. 3^rd meeting on the Molecular mechanisms of neurodegeneration. Invited Lecture.
9-14 June 2007. Tomar, Portugal. EMBO-FEBS Workshop on Chaperones in Normal and Aberrant Protein Folding, Aging and Cancer. Invited Lecture.
7-12 July 2007. Vienna, Austria. 32^nd Annual FEBS Congress, Molecular Machines. Invited Lecture.
26-29 September 2007. Riva del Garda, Italy. 9^th Annual Congress of the FISV. Invited Lecture.
10 December 2007. Zurich, Switzerland. Encounter on protein aggregation at ETH. Invited Lecture
18-20 June 2008. Heidelberg, Germany. EMBO YIP Meeting. Standard Short Presentation.
14-15 September 2008. Cologne, Germany. Klenk Symposium on Protein misfolding and disease. Invited Lecture.
8-11 February 2009. Halle, Germany. Structure of amyloid fibrils and mechanisms of amyloid formation. Invited Lecture
23-28 May 2009. Dubrovnik, Croatia. The biology of molecular chaperones. Invited Lecture.
28 June-28 July 2009. Snowmass Village, Colorado, USA. FASEB SRC Amyloid Fibril Formation and Protein Misfolding: Molecular Mechanisms and Cellular Effects. Invited Lecture.
8-9 April 2010. Cambridge, UK. From Neuroscience to Nanoscience. Invited Lecture
18-21 April 2010. Rome, Italy. The XII International Symposium on Amyloidosis. Invited Lecture.
4-8 May 2010. Cold Spring Harbor Laboratory. New York. Molecular Chaperones and Stress Responses. Selected Abstract.
27-30 August 2010. Warsaw, Poland. Proteins: structures, folding and interactions. Invited Lecture.
3 September 2010. Liège, Belgium. Protein folding and stability. Invited Lecture.
15-17 November 2010. Julich, Germany. Expanding the frontiers of biomolecular sciences. Invited Lecture.
24-28 January 2011. Venice, Italy. Protein Stability and pathways of self-assembly. Invited Lecture.
19-24 May 2011. Grundlsee, Austria. The biology of molecular chaperones. Invited Lecture.
23-25 June 2011. Parma, Italy. 6th CLU workshop. Selected abstract.
16-21 July 2011. Paris, France. Alzheimer’s Association International Conference. Selected abstract.
11-16 September 2011, Lecce, Italy. XXIV Congresso Nazionale della Società Italiana di Chimica. Invited Lecture.
22 September 2011, Milan, Italy, 2nd CONVEGNO NAZIONALE ARiSLA, Invited Lecture.
16-18 February 2012 Bressanone, Italy, Physics Of Protein Folding And Aggregation. Invited Lecture.
10-14 June 2012, Monte Verità, Switzerland, International Conference on Molecular Crowding 2012. Invited Lecture
16-20 July 2012, Dresden, Germany, The Emerging Dynamic View of proteins: proteins plasticity in Allostery, Evolution, and Self-Assembly, Invited Lecture
24 October 2012, Milan, Italy. 3° Convegno Nazionale ARiSLA. Invited Lecture
28-30 November 2012, Wollongong, Australia, Proteostasis and Disease Symposium. Invited Lecture
18-20 September 2013, Ferrara, Italy. 57th meeting of the Italian Society of Biochemistry and Molecular Biology. Invited Lecture
4-5 November 2013, Cambridge, UK, 1st Annual meeting of the Centre for Misfolding Diseases. Invited Lecture

Teaching

Academic years from 2002-2003 to 2007-2008. Ca. 80 hours of teaching per year (10 CFU/year), Course of Biochemistry, Faculty of Medicine, Univ. di Firenze. Ca. 340 hours of exams and tutorials.
Academic years 2008-2009 and 2009-2010. Ca. 16 hours of teaching per year (2 CFU/year), Course of Structure and function of proteins, Faculty of Medicine, Univ. di Firenze. Ca. 5 hours of exams.
Academic years 2008-2009 and 2009-2010. Ca. 20 hours of teaching per year (2 CFU/year), Course of Chemistry, Faculty of Medicine, Univ. di Firenze. Ca. 15 hours of exams.
Academic years 2009-2010 and 2010-2011. Ca. 16 hours of teaching per year (2 CFU/year), Course of Cellular Biochemistry, Faculty of Medicine, Univ. di Firenze. Ca. 20 hours of exams.
Year 2010-2011 and 2011-2012, Ca. 40 hours of teaching per year (4 CFU/year), Course of Chemistry, Faculty of Medicine, Univ. di Firenze. Ca. 200 hours of exams and tutorials per year.
Academic years 2011-2012. Ca. 24 hours of teaching per year (3 CFU/year), Course of protein homeostasis and associated diseases, Faculty of Medicine, Univ. di Firenze. Ca. 4 hours of exams.
Over 20 Invited seminars at Italian and Foreign Universities and Research Institutes.
Ca. 18 Invited Lectures at National Meetings

Invited Reviews and Book Chapters

Chiti F and Dobson CM (2006). Invited review titled “Protein misfolding, functional amyloid, and human disease”. Ann. Rev. Biochem. 75, 333-366.
Chiti F (2006). Chapter titled “The influence of hydrophobicity, secondary structure propensity and charge in protein aggregation” for the book Protein Misfolding, Aggregation, and Conformational Diseases. Vladimir N. Uversky and Anthony L. Fink Editors, Kluwer Academic / Plenum Publishers, pp. 43-59
Plakoutsi G, Marcon G and Chiti F (2006). Chapter titled “Investigation of amyloid formation by globular proteins under conditions in which they are in their native state”. In “Amyloid, Prions and other Protein Aggregates” Methods in Enzymology 413, 75-91.
Bemporad F, Calloni G, Campioni S, Plakoutsi G, Taddei N and Chiti F (2006). Invited review titled “Sequence and Structural Determinants of amyloid fibril formation” Accounts of Chemical Research 39, 620-627.
Monsellier E and Chiti F (2007). Invited review titled “Prevention of amyloid-like aggregation as a driving force of protein evolution”. EMBO Reports 8, 737-742.
Bellotti V and Chiti F (2008). Invited review titled “Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseases” Curr. Op. Struct. Biol. 18, 771-779.
Chiti F and Dobson CM (2009). Invited review titled “Amyloid formation by globular proteins under native conditions”. Nature Chem. Biol. 5, 15-22.
Bemporad F and Chiti F (2009). “Native-like aggregation” of the acylphosphatase from Sulfolobus solfataricus and its biological implications. FEBS Lett. 583, 2630-2638.
Campioni S, Monsellier E and Chiti F (2010). Chapter titled “Why proteins misfold?” for the book “Protein Misfolding Diseases: Current and Emerging Principles and Therapies” Marina Ramirez-Alvarado, Chris Dobson, Jeff Kelly editors, John Wiley and Sons, pp 3-20.
Belli M, Ramazzotti M, Chiti F. (2011). Prediction of amyloid aggregation in vivo. EMBO Rep. 12, 657-663.
Bemporad F, Chiti F (2012). Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships.Chem. Biol. 19, 315-327.
Bemporad F, Chiti F (2012). Chapter titled “Pathways of amyloid formation” for the book “Amyloid Fibrils and Prefibrillar Aggregates: Molecular and Biological Properties” Daniel Otzen editor, Wiley-VCH, pp. 151-166.

Publications of original articles (excluding reviews)

Modesti A., Taddei N., Chiti F., Bucciantini M., Magherini F., Rigacci S., Stefani M., Raugei G. and Ramponi G. (1996). Properties of Cys21 mutated muscle acylphosphatases. J. Prot. Chem. 15, 27-34.
Taddei N., Magherini F., Chiti F., Bucciantini M., Raugei G., Stefani M. and Ramponi G. (1996). C-terminal region contributes to muscle acylphosphatase three-dimensional structure stabilization. FEBS Lett. 384, 172-176.
Taddei N., Stefani M., Magherini F., Chiti F., Modesti A., Raugei G. and Ramponi G. (1996). Looking for residues involved in muscle acylphosphatase catalytic mechanism and structural stabilization: the role of Asn41, Thr42 and Thr46. Biochemistry, 35, 7077-7083.
Taddei N., Chiti F., Magherini F., Stefani M., Thunnissen M.M.G.M., Nordlund P. and Ramponi G. (1997). Structural and kinetic investigations on the 15-21 and 42-45 loops of muscle acylphosphatase: evidence for their involvement in enzyme catalysis and conformational stabilisation. Biochemistry, 36, 7217-7224.
Chiti F., van Nuland N.A.J., Taddei N., Magherini F., Stefani M., Ramponi G. and Dobson C.M. (1998). Conformational stability of muscle acylphosphatase. The role of temperature, denaturant concentration and pH. Biochemistry, 37, 1447-1455.
Bucciantini M., Stefani M., Taddei N., Chiti F., Rigacci S. and Ramponi G. (1998). Sequence-specific recognition of peptide substrates by the low M-r phosphotyrosine protein phosphatase isoforms. FEBS Lett., 422, 213-217.
Modesti A., Marzocchini R., Raugei G., Chiti F., Sereni A., Magherini F. and Ramponi G. (1998). Cloning, expression and characterization of a new human LMW-PTP isoform originating by alternative splicing. FEBS Lett. 431, 111-115.
Chiti F., Magherini F., Taddei N., Ilardi C., Stefani M., Bucciantini M., Dobson C.M. and Ramponi G. (1998). Studies of enzymatic activity and conformational stability of muscle acylphosphatase mutated at conserved lysine residues. Protein Eng. 11, 557-561.
van Nuland N.A.J., Chiti F., Taddei N., Raugei G., Ramponi G. and Dobson C.M. (1998). Slow folding of muscle acylphosphatase in the absence of intermediates. J. Mol. Biol. 283, 883-891.
Chiti F., Taddei N., van Nuland N.A.J., Magherini F., StefaniM., RamponiG. and DobsonC.M.(1998). Structural characterisation of the transition state for folding of muscle acylphosphatase. J. Mol. Biol. 283, 893-903.
Taddei N., Chiti F., Paoli P. Fiaschi T., Bucciantini M., Stefani M., Dobson C.M. and Ramponi G. (1999). Thermodynamics and kinetics of folding of common-type acylphosphatase: comparison to the highly homologous muscle isoenzyme. Biochemistry 38, 2135-2142.
Paoli P., Taddei N., Fiaschi T., Veggi D., Camici G., Manao G., Raugei G., Chiti F. and Ramponi G. (1999). The contribution of acidic residues to the conformational stability of common-type acylphosphatase. Arch. Biochem. Biophys. 363, 349-355.
Chiti F., Webster M., Taddei N., Clark, A., Stefani M., Ramponi G. and Dobson C.M. (1999). Designing conditions for in vitro formation of amyloid fibrils. Proc. Natl. Acad. Sci. USA 96, 3590-3594.
Chiti F., Taddei N., Webster P., Hamada D., Fiaschi T., Ramponi G. and Dobson C.M. (1999). Acceleration of the folding of acylphosphatase by stabilisation of local secondary structure. Nature Struct. Biol. 6, 380-387.
Chiti F., Taddei N., Giannoni E., van Nuland N.A.J., Ramponi G. and Dobson C.M. (1999). Development of enzymatic activity during protein folding. J. Biol. Chem. 274, 20151-20158.
Chiti F., Taddei N., White P.M., Bucciantini M., Magherini F., Stefani M. and Dobson C.M. (1999). Mutational analysis of acylphosphatase reveals the importance of topology and contact order in protein folding.Nature Struct. Biol. 6, 1005-1009.
Hamada D., Chiti F., Guijarro J.I., Kataoka M., Taddei N. and Dobson C.M. (2000). Evidence concerning rate-limiting steps in protein folding from the effects of trifluoroethanol. Nature Struct. Biol. 7, 58-61.
Chiti F., Taddei N., Bucciantini M., White P., Ramponi G. and Dobson C.M. (2000). Mutational analysis of the propensity for amyloid formation by a globular protein. EMBO J. 19, 1441-1449.
Verzola B., Chiti F., Manao G. and Righetti P.G. (2000). Monitoring equilibria and kinetics of protein folding/unfolding reactions by capillary zone electrophoresis. Anal. Biochem. 282, 239-244.
Taddei N., Chiti F., Fiaschi T., Bucciantini M., Capanni C., Stefani M., Serrano L., Dobson C.M. and Ramponi G. (2000). Stabilisation of alpha-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatase folding. J. Mol. Biol. 300, 633-647.
Pertinhez T.A., Hamada D., Smith L.J., Chiti F., Taddei N., Stefani M. and Dobson C.M. (2000). Initial denaturing conditions influence the slow folding phase of acylphosphatase associated with proline isomerization. Protein Sci. 9, 1466-1473.
Chiti F., Mangione P., Andreola A., Giorgetti S., Stefani M., Dobson C.M., Bellotti V. and Taddei N. (2001). Detection of two partially structured species in the folding process of the amyloidogenic protein b2-microglobulin. J. Mol. Biol. 307, 379-391.
Chiti F., Taddei N., Stefani M., Dobson C.M. and Ramponi G. (2001). Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation. Protein Sci. 10, 879-886.
Taddei N., Capanni C., Chiti F., Stefani M., Dobson C.M. and Ramponi G. (2001). Folding and aggregation are selectively influenced by the conformational preferences of the a-helices of muscle acylphosphatase. J. Biol. Chem., 276, 37149-37154.
Chiti F., De Lorenzi E., Grossi S., Mangione P., Giorgetti S., Caccialanza G., Dobson C.M., Merlini G., Ramponi G. and Bellotti V. (2001). A partially structured species of b2-microglobulin is significantly populated under physiological conditions and involved in fibrillogenesis. J. Biol. Chem. 276, 46714-46721.
Chiti F., Bucciantini M., Capanni C., Taddei N., Dobson C.M. and Stefani M. (2001). Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain. Protein Sci. 10, 2541-2547.
Millet I.S., Townsley L.E., Chiti F., Doniach S. and Plaxco K.W. (2002). Equilibrium collapse and the kinetic 'foldability' of proteins. Biochemistry 41, 321-325.
Chiti F., Taddei N., Baroni F., Capanni C., Stefani M., Ramponi G. and Dobson C.M. (2002). Kinetic partitioning of protein folding and aggregation. Nature Struct. Biol. 9, 137-143.
De Lorenzi E., Grossi S., Massolini G., Giorgetti S., Mangione P., Andreola A., Chiti F., Bellotti V. and Caccialanza G. (2002). Capillary electrophoresis investigation of a partially unfolded conformation of b2-microglobulin. Electrophoresis 23, 918-925.
Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., Zurdo J., Taddei N., Ramponi G., Dobson C.M. and Stefani M. (2002). Inherent toxicity of aggregates implies a common origin for protein misfolding diseases. Nature 416, 507-511.*
Chiti F, Calamai M, Taddei N, Stefani M, Ramponi G, Dobson CM. (2002). Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases. Proc. Natl. Acad. Sci. USA 99, 16419-16426.
Degl'Innocenti D, Ramazzotti M, Marzocchini R, Chiti F, Raugei G, Ramponi G. (2003). Characterization of a novel Drosophila melanogaster acylphosphatase. FEBS Lett. 30, 171-174.
Esposito G, Garcia J, Mangione P, Giorgetti S, Corazza A, Viglino P, Chiti F, Andreola A, Dumy P, Booth D, Hawkins PN, Bellotti V. (2003). Structural and folding dynamics properties of T70N variant of human lysozyme. J. Biol. Chem. 278, 25910-25918
Calloni G, Taddei N, Plaxco KW, Ramponi G, Stefani M, Chiti F (2003). Comparison of the folding processes of distantly related proteins. Importance of hydrophobic content in folding. J. Mol. Biol. 330, 577-591.
Chiti F, Stefani M, Taddei N, Ramponi G, Dobson CM. (2003). Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424, 805-808.
Polverino de Laureto P, Taddei N, Frare E, Capanni C, Costantini S, Zurdo J, Chiti F, Dobson CM, Fontana A. (2003). Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis. J. Mol. Biol. 334, 129-141.
Calamai M, Taddei N, Stefani M, Ramponi G, Chiti F (2003). Relative Influence of Hydrophobicity and Net Charge in the Aggregation of two Homologous Proteins. Biochemistry 42, 15078-15083.
Degl’Innocenti D, Taddei N, Ramazzotti M, Stefani M, Chiti F and Ramponi G. Selection of antibody fragments specific for an a-helix region of acylphosphatase. (2004). J. Mol. Recognit. 17, 62-66.
Monti M., Lelj Garolla Di Bard B, Calloni G, Chiti F, Amoresano A, Ramponi G and Pucci P. (2004). The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process. J. Mol. Biol. 336, 253-262.
Plakoutsi G, Stefani M, Taddei N and Chiti F. (2004). Aggregation of the acylphosphatase from S. solfataricus. The folded and partially unfolded states can be both precursors for amyloid formation. J. Biol. Chem. 279, 14111-14119.
CapanniC, Taddei N, Gabrielli S, Messori L, OrioliP, ChitiF, Stefani M and Ramponi G (2004). Investigation of the effects of copper ions on protein aggregation using a model system. Cell. Mol. Life. Sci. 61, 982-991.
ReliniA, CanaleC, TorrassaS, RolandiR, Gliozzi A, Rosano C, Bolognesi M, Plakoutsi G, Bucciantini M, Chiti F and Stefani M. (2004). Monitoring the process of HypF-N fibrillization and liposome permeabilization by fibril precursors. J. Mol. Biol. 338, 943-957.
Ventura S, Zurdo J, Narayanan S, Parreño M. Mangues R, Reif B, Chiti F, Giannoni E, Dobson CM, Aviles FX. and Serrano L. (2004). Short amino acid stretches play an important role in protein amyloid formation. The SH3 case. Proc. Natl. Acad. Sci. USA, 101, 7258-63.
Bucciantini M, Calloni G, Chiti F, Formigli L, Nosi D, Dobson CM and Stefani M. (2004). Pre-fibrillar amyloid protein aggregates share common features of cytotoxicity. J. Biol. Chem. 279, 31374-31382.
Bemporad F, Capanni C, Calamai M, Tutino ML, Stefani M and Chiti F. (2004). Studying the folding process of the acylphosphatase from S. solfataricus. A comparative analysis with other proteins from the same superfamily. Biochemistry 43, 9116-9126.
DuBay KF, Pawar AP, Chiti F, Zurdo J, Dobson CM and Vendruscolo M. (2004). Predicting Absolute Aggregation Rates of amyloidogenic polypeptide chains. J. Mol. Biol. 341, 1317-1326.
Bucciantini M, Rigacci S, Berti A, Pieri L, Cecchi C, Nosi D, Formigli L, Chiti F and Stefani M (2005). Patterns of cell death triggered in two different cell lines by HypF-N pre-fibrillar aggregates. FASEB J. 19, 437-439
Calloni G, Zoffoli S, Stefani M, Dobson CM, Chiti F. (2005). Investigating the effects of mutations on protein aggregation in the cell. J. Biol. Chem. 280, 10607-10613.
Maxwell KL., Wildes D, Zarrine-Afsar A, de los Rios MA, Brown AG, Friel CT, Hedberg L, Horng J-C, Bona D, Miller EJ, Valle-Blisle A, Main ERG, Bemporad F, Qiu L, Teilum K, Vu N-D, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai Y, Hagen SJ, Serrano L, Oliveberg M, Raleigh DP, Wittung-Stafshede P, Radford SE, Jackson SE, Sosnick TR, Marqusee S, Davidson AR and Plaxco KW (2005). Protein folding: defining a standard set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602-616.
Calamai M, Canale C, Relini A, Stefani M, Chiti F and Dobson CM (2005). Reversal of Protein Aggregation Provides Evidence for Multiple Aggregated States. J. Mol. Biol. 346, 603-616.
Marcon G, Plakoutsi G, Canale C, Relini A., Taddei N., Dobson CM, Ramponi G and Chiti F (2005). Amyloid formation from HypF-N under conditions in which the protein is initially in its native state. J. Mol. Biol. 347, 323-35.
Pawar AP, DuBay KF, Zurdo J, Chiti F, Vendruscolo M and Dobson CM (2005). Prediction of “aggregation-prone” and “aggregation-susceptible” regions in proteins associated with neurodegenerative diseases. J. Mol. Biol. 350, 379-392.
Fowler SB, Poon S, Muff R, Chiti F, Dobson CM, Zurdo J. (2005). Rational design of aggregation-resistant bioactive peptides: reengineering human calcitonin. Proc. Natl. Acad. Sci. USA 102, 10105-10110.
Plakoutsi G, Bemporad F, Calamai M, Taddei N, Dobson CM, Chiti F. (2005). Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates. J. Mol. Biol. 351, 910-922.
Parrini C, Taddei N, Ramazzotti M, Degl'Innocenti D, Ramponi G, Dobson CM, Chiti F. (2005). Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregation. Structure 13, 1143-1151.
Calamai M, Chiti F, Dobson CM. (2005). Amyloid Fibril Formation can Proceed from Different Conformations of a Partially Unfolded Protein. Biophys. J. 89, 4201-4210
Soldi G, Bemporad F, Torrassa S, Relini A, Ramazzotti M, Taddei N, Chiti F (2005). Amyloid formation of a protein in the absence of unfolding and destabilisation of the native state. Biophys. J. 89, 4234-4244.
Corazza A, Rosano C, Pagano K, Alverdi V, Esposito G, Capanni C, Bemporad F, Plakoutsi G, Stefani M, Chiti F, Zuccotti S, Bolognesi M, Viglino P. (2006). Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus. Proteins 62, 64-79.
Bemporad F, Taddei N, Stefani M, Chiti F (2006). Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase. Protein Sci. 15, 862-870.
Plakoutsi G, Bemporad F, Monti M, Pagnozzi D, Pucci P, Chiti F. (2006). Exploring the mechanism of formation of native-like and precursor amyloid oligomers for the native acylphosphatase from Sulfolobus solfataricus. Structure 14, 993-1001.
Baglioni S, Casamenti F, Bucciantini M, Luheshi LM, Taddei N, Chiti F, Dobson CM, Stefani M. (2006). Prefibrillar amyloid aggregates could be generic toxins in higher organisms. J. Neurosci. 26, 8160-8167.
Soldi G, Plakoutsi G, Taddei N, Chiti F (2006). Stabilization of a native protein mediated by ligand binding inhibits amyloid formation independently of the aggregation pathway. J. Med. Chem. 49, 6057-6064.
Calamai M, Kumita JR, Mifsud J, Parrini C, Ramazzotti M, Ramponi G, Taddei N, Chiti F, Dobson CM. (2006). Nature and Significance of the Interactions between Amyloid Fibrils and Biological Polyelectrolytes. Biochemistry 45, 12806-12815.
Trovato A, Chiti F, Maritan A, Seno F. (2006). Insight into the Structure of Amyloid Fibrils from the Analysis of Globular Proteins. PLoS Comput. Biol. 2, e170.
Picotti P, De Franceschi G, Frare E, Spolaore B, Zambonin M, Chiti F, de Laureto PP, Fontana A. (2007). J. Mol. Biol. 367, 1237-45.
Monsellier E, Ramazzotti M, de Laureto PP, Tartaglia GG, Taddei N, Fontana A, Vendruscolo M, Chiti F. (2007). The distribution of residues in a polypeptide sequence is a determinant of aggregation optimized by evolution. Biophys J. 93, 4382-4891.
Luheshi LM, Tartaglia GG, Brorsson AC, Pawar AP, Watson IA, Vendruscolo M, Lomas DA, Dobson CM, Crowther DC (2007). Systematic in vivo Analysis of the Intrinsic Determinants of Amyloid b Pathogenicity. PloS Biol. 5, e290.
Soldi G, Bemporad F, Chiti F (2008). The Degree of Structural Protection at the Edge ‚-Strands Determines the Pathway of Amyloid Formation in Globular Proteins. J. Am. Chem. Soc. 130, 4295-302.
Bemporad F, Gsponer J, Hopeharuoho HI, Plakoutsi G, Stati G, Stefani M, Taddei N, Vendruscolo M, Chiti F (2008). Biological function in a non-native partially folded state of a protein. EMBO J. 27, 1525-1535.
Campioni S, Mossuto MF, Torrassa S, Calloni G, de Laureto PP, Relini A, Fontana A, Chiti F. (2008). Conformational properties of the aggregation precursor state of HypF-N. J. Mol. Biol. 379, 554-567.
Parrini C, Bemporad F, Baroncelli A, Gianni S, Travaglini-Allocatelli C, Kohn JE, Ramazzotti M, Chiti F, Taddei N. (2008). The folding process of acylphosphatase from Escherichia coli is remarkably accelerated by the presence of a disulfide bond. J. Mol. Biol. 379, 1107-1118.
Tartaglia GG, Pawar AP, Campioni S, Dobson CM, Chiti F, Vendruscolo M (2008). Prediction of Aggregation-Prone Regions in Structured Proteins. J. Mol. Biol. 380, 425-436.
Calloni G, Lendel C, Campioni S, Giannini S, Gliozzi A, Relini A, Vendruscolo M, Dobson CM, Salvatella X, Chiti F. (2008). Structure and dynamics of a partially folded protein are decoupled from its mechanism of aggregation.J. Am. Chem. Soc. 130, 13040-13050.
Monsellier E., Ramazzotti M., Taddei N., Chiti F. (2008). PLoS Comput. Biol. 4, e1000199.
Bemporad F, Vannocci T, Varela L, Azuaga AI, Chiti F (2008). A model for the aggregation of the acylphosphatase from Sulfolobus solfataricus in its native-like state. Biochim. Biophys. Acta 1784, 1986-1996.
Sicorello A, Torrassa S, Soldi G, Gianni S, Travaglini-Allocatelli C, Taddei N, Relini A, Chiti F. (2009). Agitation and high ionic strength induce amyloidogenesis of a folded PDZ domain in native conditions.Biophys J. 96, 2289-2298.
Calamai M, Tartaglia GG, Vendruscolo M, Chiti F, Dobson CM. (2009). Mutational Analysis of the Aggregation-Prone and Disaggregation-Prone Regions of Acylphosphatase.J. Mol. Biol. 387, 965-974.
Motamedi-Shad N, Monsellier E, Chiti F (2009). Amyloid Formation by the Model Protein Muscle Acylphosphatase is Accelerated by Heparin and Heparan Sulfate Through a Scaffolding-Based Mechanism.J. Biochem. 146, 805-814.
Motamedi-Shad N, Monsellier E, Torrassa S, Relini A, Chiti F. (2009). Kinetic analysis of amyloid formation in the presence of heparan sulfate. Faster unfolding and change of pathway.J. Biol. Chem. 284, 29921-29934.
Ahmad B, Winkelmann J, Tiribilli B, Chiti F (2009). Searching for conditions to form stable protein oligomers with amyloid-like characteristics: the unexplored basic pH. Biochim. Biophys. Acta 1804, 223-234.
Campioni S, Mannini B, ZampagniM, Pensalfini A, ParriniC, EvangelistiE, ReliniA, StefaniM, DobsonCM, CecchiC, ChitiF. (2010). A causative link between the structure of aberrant protein oligomers and their toxicity. Nature Chem. Biol. 6, 140-147.
Relini A, Torrassa S, Ferrando R, Rolandi R, Campioni S, Chiti F, Gliozzi A. (2010). Detection of populations of amyloid-like protofibrils with different physical properties. Biophys. J. 98, 1277-1284.
Brorsson AC, Bolognesi B, Tartaglia GG, Shammas SL, Favrin G, Watson I, Lomas DA, Chiti F, Vendruscolo M, Dobson CM, Crowther DC, Luheshi LM. (2010). Intrinsic determinants of neurotoxic aggregate formation by the amyloid beta peptide. Biophys. J. 98, 1677-1684.
Pagano K, Bemporad F, Fogolari F, Esposito G, Viglino P, Chiti F, Corazza A. (2010). Structural and dynamics characteristics of Acylphosphatase from Sulfolobus solfataricus in the monomeric state and in the initial native-like aggregates.J. Biol. Chem. 285, 14689-14700.
Winkelmann J, Calloni G, Campioni S, Mannini B, Taddei N, Chiti F. (2010). Low-Level Expression of a Folding-Incompetent Protein in Escherichia coli: Search for the Molecular Determinants of Protein Aggregation In Vivo. J. Mol. Biol. 398, 600-613.
Monsellier E, Ramazzotti M, Taddei N, Chiti F. (2010). A computational approach for identifying the chemical factors involved in the glycosaminoglycans-mediated acceleration of amyloid fibril formation.PLoS One 5, e11363.
Ramshini H, Parrini C, Relini A, Zampagni M, Mannini B, Pesce A, Saboury AA, Nemat-Gorgani M, Chiti F. (2011). Large proteins have a great tendency to aggregate but a low propensity to form amyloid fibrils.PLoS One 6, e16075.
Zampagni M, Cascella R, Casamenti F, Grossi C, Evangelisti E, Wright D, Becatti M, Liguri G, Mannini B, Campioni S, Chiti F, Cecchi C. (2011). A comparison of the biochemical modifications caused by toxic and nontoxic protein oligomers in cells.J Cell Mol Med. 15, 2106-2116.
Ahmad B, Vigliotta I, Tatini F, Campioni S, Mannini B, Winkelmann J, Tiribilli B, Chiti F. (2011). The induction of α-helical structure in partially unfolded HypF-N does not affect its aggregation propensity. Protein Eng Des Sel. 24, 553-563.
De Simone A, Dhulesia A, Soldi G, Vendruscolo M, Hsu STD, Chiti F, Dobson CM (2011). Experimental Energy Surfaces Reveal theMechanisms of Maintenance of Protein Solubility. Proc. Natl. Acad. Sci. USA, 108, 21057-21062.
Fusco G, De Simone A, Hsu ST, Bemporad F, Vendruscolo M, Chiti F, Dobson CM (2012). ¹H, ¹³C and ¹⁵N resonance assignments of human muscle acylphosphatase. Biomol NMR Assign. 6, 27-29.
Saridaki T, Zampagni M, Mannini B, Evangelisti E, Taddei N, Cecchi C, Chiti F (2012). Glycosaminoglycans (GAGs) Suppress the Toxicity of HypF-N Prefibrillar Aggregates.J. Mol. Biol. 421, 616-630.
Evangelisti E, Cecchi C, Cascella R, Sgromo C, Becatti M, Dobson CM, Chiti F, Stefani M (2012). Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomers. J. Cell. Sci. 125, 2416-2427.
Motamedi-Shad N, Garfagnini T, Penco A, Relini A, Fogolari F, Corazza A, Esposito G, Bemporad F, Chiti F (2012) Rapid oligomer formation of human muscle acylphosphatase induced by heparan sulfate. Nature Struct. Mol. Biol. 19, 547-554.
Bemporad F, De Simone A, Chiti F, Dobson CM. (2012). Characterizing intermolecular interactions that initiate native-like protein aggregation.Biophys. J. 102, 2595-2604.
Mannini B, Cascella R, ZampagniR, van Waarde-VerhagenMAWH, MeehanS, RoodveldtC, CampioniS, BoninsegnaM, PencoA, ReliniA, Kampinga HH, Dobson CM, WilsonMR, CecchiC, Chiti F (2012). Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers. Proc. Natl. Acad. Sci. USA 109, 12479-12484.
Campioni S, Mannini B, López-Alonso JP, Shalova IN, Penco A, Mulvihill E, Laurents DV, Relini A, Chiti F (2012). Salt Anions Promote the Conversion of HypF-N into Amyloid-Like Oligomers and Modulate the Structure of the Oligomers and the Monomeric Precursor State. J. Mol. Biol. 424, 132-149.
Castillo V, Chiti F, Ventura S (2013). The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain.PLoS One 8, e58297.
Tatini F, Pugliese AM, Traini C, Niccoli S, Maraula G, Ed Dami T, Mannini B, Scartabelli T, Pedata F, Casamenti F, Chiti F (2013). Amyloid-β oligomer synaptotoxicity is mimicked by oligomers of the model protein HypF-N.Neurobiol Aging 34, 2100-2109.
Cascella R, Conti S, Tatini F, Evangelisti E, Scartabelli T, Casamenti F, Wilson MR, Chiti F, Cecchi C. (2013). Extracellular chaperones prevent Aβ42-induced toxicity in rat brains.Biochim Biophys Acta 1832, 1217-1226.
Mangione PP, Esposito G, Relini A, Raimondi S, Porcari R, Giorgetti S, Corazza A, Fogolari F, Penco A, Goto Y, Lee YH, Yagi H, Cecconi C, Naqvi MM, Gillmore JD, Hawkins PN, Chiti F, Rolandi R, Taylor GW, Pepys MB, Stoppini M, Bellotti V (2013). structure, folding dynamics, and amyloidogenesis of D76N β2-microglobulin: roles of shear flow, hydrophobic surfaces, and α-crystallin.J. Biol. Chem. 288, 30917-30930.
Monsef Shokri M, Ahmadian S, Bemporad F, Khajeh K, Chiti F (2013). Amyloid fibril formation by a normally folded protein in the absence of denaturants and agitation.Amyloid 20, 226-232.
Cascella R, Conti S, Mannini B, Li X, Buxbaum JN, Tiribilli B, Chiti F, Cecchi C (2013) Transthyretin suppresses the toxicity of oligomers formed by misfolded proteins in vitro.Biochim Biophys Acta 1832, 2302-2314.
Capitini C, Conti S, Perni M, Guidi F, Cascella R, De Poli A, Penco A, Relini A, Cecchi C, Chiti F (2014). TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells.PLoS One. 9, e86720.

Fabrizio CHITI

Interessi

Proteins have a generic tendency to convert from their soluble states into insoluble highly structured aggregates known as amyloid fibrils. Since these aggregates are toxic to the cells, especially in the form of early forming oligomers, the cellular machinery has evolved, among other requirements, to inhibit uncontrolled protein aggregation. Failure to inhibit protein aggregation often results in pathology. To date, a large number of very diverse human diseases, including Alzheimer's, Parkinson's disease and type II diabetes, have been recognised to be associated with the formation of amyloid fibrils or protein inclusions with amyloid-like properties. Amyloid fibril formation is also exploited by living organisms for the formation of fibrillar structures with specific biological functions, provided that this occurs under controlled conditions. Finally, the recent findings that the inclusion bodies formed after overexpression of heterologous proteins in bacteria are amyloid-like in structure and the increasing awareness that an enormous number of novel materials based on the amyloid motif can be constructed has expanded the interest of amyloid formation to biotechnology.

The research of this lab uses a multi angle approach to investigate the mechanisms by which soluble proteins assemble into ordered aggregates and by which the resulting aggregates cause cell dysfunction.  Here is a list of past and ongoing projects:

Study, at a molecular level, of the process by which native proteins convert into partially folded states necessary to initiate aggregation
Study, in molecular depth, of the conversion of partially folded states of proteins into amyloid fibrils and their precursor oligomers
Study of the relationship between structure and toxicity of protein oligomers
Investigation of molecular chaperones as inhibitors of the toxicity of protein oligomers
Investigation of small molecules as inhibitors on the formation and toxicity of protein oligomers
Study, at a molecular level, of the process of native-like aggregation, involving directly the folded state of a protein
Study of the effect of agents of the extracellular matrix, such as glycosamynoglycans, on the formation of amyloid fibrils, precursor oligomers and their toxicity
Editing of mathematical algorithms able to predict fundamental aspects of protein aggregation in vitro and in vivo
Elucidation of protein oligomers on neuronal function of primary neurons and rat brains

In addition to classical molecular biology and biochemical techniques for manipulation/mutation of genes and purification of their resulting proteins, the experimental work involves the utilisation of biophysical techniques for the characterisation of the folding and aggregation processes. These include turbidometry, fluorescence, circular dichroism and Fourier-transform infra-red spectroscopies, static and dynamic light scattering, stopped-flow devices. Studies of the interaction of protein aggregates with cells are based on the utilisation of cell cultures and specific protocols to assess their viability, oxidative stress and calcium homeostasis. Confocal microscopy and FACS are widely used. Projects involving nuclear magnetic resonance (NMR), atomic force microscopy (AFM), transmission electron microscopy (TEM), mass spectrometry (MS) and limited proteolysis are feasible through established collaborations.

Fabrizio CHITI

Pubblicazioni

Legenda

Contributo su rivista |

Articolo su libro |

Libro |

Contributo in atti di convegno (proceeding) |

Brevetto |

Curatela | Altro

Altro |

Tesi di Dottorato

Rinauro, Dillon J; Chiti, Fabrizio; Vendruscolo, Michele; Limbocker, Ryan (2024). Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases. MOLECULAR NEURODEGENERATION, vol. 19, pp. 0-0, ISSN:1750-1326 DOI

Muscat, Stefano; Errico, Silvia; Danani, Andrea; Chiti, Fabrizio; Grasso, Gianvito (2024). Leveraging Machine Learning-Guided Molecular Simulations Coupled with Experimental Data to Decipher Membrane Binding Mechanisms of Aminosterols. JOURNAL OF CHEMICAL THEORY AND COMPUTATION, vol. 20, pp. 8279-8289, ISSN:1549-9626 DOI

Serene W. Chen, Joseph D. Barritt, Roberta Cascella, Alessandra Bigi, Cristina Cecchi, Martina Banchelli, Angelo Gallo, James A. Jarvis, Fabrizio Chiti, Christopher M. Dobson, Giuliana Fusco, and Alfonso De Simone (2024). Structure-toxicity relationship in intermediate fibrils from lα-Synuclein condensates. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, vol. 146, pp. 10537-10549, ISSN:0002-7863 DOI

Bigi, Alessandra; Fani, Giulia; Bessi, Valentina; Napolitano, Liliana; Bagnoli, Silvia; Ingannato, Assunta; Neri, Lorenzo; Cascella, Roberta; Matteini, Paolo; Sorbi, Sandro; Nacmias, Benedetta; Cecchi, Cristina; Chiti, Fabrizio (2024). Putative novel CSF biomarkers of Alzheimer’s disease based on the novel concept of generic protein misfolding and proteotoxicity: the PRAMA cohort. TRANSLATIONAL NEURODEGENERATION, vol. 13, pp. 0-0, ISSN:2047-9158 DOI

Alessandra Bigi, Liliana Napolitano, Devkee M. Vadukul, Fabrizio Chiti, Cristina Cecchi, Francesco A. Aprile, Roberta Cascella (2024). A single-domain antibody detects and neutralises toxic Aβ42 oligomers in the Alzheimer's disease CSF. ALZHEIMER'S RESEARCH & THERAPY, vol. 16, pp. 0-0, ISSN:1758-9193 DOI Accesso ONLINE all'editore

Staderini, Tommaso; Bigi, Alessandra; Lagrève, Clément; Marzi, Isabella; Bemporad, Francesco; Chiti, Fabrizio (2024). Biophysical characterization of the phase separation of TDP-43 devoid of the C-terminal domain. CELLULAR AND MOLECULAR BIOLOGY LETTERS, vol. 29, pp. 0-0, ISSN:1689-1392 DOI

Limbocker, Ryan; Cremades, Nunilo; Cascella, Roberta; Tessier, Peter M; Vendruscolo, Michele; Chiti, Fabrizio (2023). Characterization of Pairs of Toxic and Nontoxic Misfolded Protein Oligomers Elucidates the Structural Determinants of Oligomer Toxicity in Protein Misfolding Diseases. ACCOUNTS OF CHEMICAL RESEARCH, vol. 56, pp. 1395-1405, ISSN:1520-4898 DOI

Garfagnini, Tommaso; Bemporad, Francesco; Harries, Daniel; Chiti, Fabrizio; Friedler, Assaf (2023). Amyloid Aggregation Is Potently Slowed Down by Osmolytes Due to Compaction of Partially Folded State. JOURNAL OF MOLECULAR BIOLOGY, vol. 435, pp. 168281-168281, ISSN:1089-8638 DOI

Bigi A, Cascella R, Fani G, Bernacchioni C, Cencetti F, Bruni P, Chiti F, Donati C, Cecchi C. (2023). Sphingosine 1-phosphate attenuates neuronal dysfunction induced by amyloid-β oligomers through endocytic internalization of NMDA receptors. THE FEBS JOURNAL, vol. 290, pp. 112-133, ISSN:1742-4658 DOI

Silvia Errico, Giacomo Lucchesi, Davide Odino, Enass Youssef Osman, Roberta Cascella, Lorenzo Neri, Claudia Capitini, Martino Calamai, Francesco Bemporad, Cristina Cecchi, William A. Kinney, Denise Barbut, Annalisa Relini, Claudio Canale, Gabriella Caminati, Ryan Limbocker, Michele Vendruscolo, Michael Zasloff, Fabrizio Chiti* (2023). Quantitative Attribution of the Protective Effects of Aminosterols against Protein Aggregates to Their Chemical Structures and Ability to Modulate Biological Membranes. OPEN JOURNAL OF MEDICINAL CHEMISTRY, vol. 66, pp. 9519-9536, ISSN:2164-3121 DOI

Francesco Conti, Martina Banchelli, Valentina Bessi, Cristina Cecchi, Fabrizio Chiti, Sara Colantonio, Cristiano D’Andrea, Marella de Angelis, Davide Moroni, Benedetta Nacmias, Maria Antonietta Pascali, Sandro Sorbi, Paolo Matteini (2023). Alzheimer Disease detection from Raman spectroscopy of the cerebrospinal fluid via topological machine learning. ENGINEERING PROCEEDINGS, vol. 51, pp. 1-5, ISSN:2673-4591 DOI

Roberta Cascella, Martina Banchelli, Seyyed Abolghasem Ghadami, Diletta Ami, Maria Cristina Gagliani, Alessandra Bigi, Tommaso Staderini, Davide Tampellini, Katia Cortese, Cristina Cecchi, Antonino Natalello, Hadi Adibi, Paolo Matteini, Fabrizio Chiti (2023). An in situ and in vitro investigation of cytoplasmic TDP-43 inclusions reveals the absence of a clear amyloid signature. ANNALS OF MEDICINE, vol. 55, pp. 72-88, ISSN:1365-2060 DOI

Justus M Gabriel, Thomas Tan, Dillon J Rinauro, Claire M Hsu, Caleb J Buettner, Marshall Gilmer, Amrita Kaur, Tristan L McKenzie, Martin Park, Sophie Cohen, Silvia Errico, Aidan K Wright, Fabrizio Chiti, Michele Vendruscolo, Ryan Limbocker (2023). EGCG inactivates a pore-forming toxin by promoting its oligomerization and decreasing its solvent-exposed hydrophobicity. CHEMICO-BIOLOGICAL INTERACTIONS, vol. 371, pp. 110307-110307, ISSN:0009-2797 DOI

Barletti, Beatrice; Lucchesi, Giacomo; Muscat, Stefano; Errico, Silvia; Barbut, Denise; Danani, Andrea; Zasloff, Michael; Grasso, Gianvito; Chiti, Fabrizio; Caminati, Gabriella (2023). Reorganization of the outer layer of a model of the plasma membrane induced by a neuroprotective aminosterol. COLLOIDS AND SURFACES. B, BIOINTERFACES, vol. 222, pp. 1-12, ISSN:1873-4367 DOI Accesso ONLINE all'editore

Cascella R, Banchelli M, Abolghasem Ghadami S, Ami D, Gagliani MC, Bigi A, Staderini T, Tampellini D, Cortese K, Cecchi C, Natalello A, Adibi H, Matteini P, Chiti F. (2023). An in situ and in vitro investigation of cytoplasmic TDP-43 inclusions reveals the absence of a clear amyloid signature. ANNALS OF MEDICINE, vol. 55, pp. 72-88, ISSN:1365-2060 DOI

Giulia Fani, Chiara Ester La Torre, Roberta Cascella, Cristina Cecchi, Michele Vendruscolo, Fabrizio Chiti (2022). Misfolded protein oligomers induce an increase of intracellular Ca2+ causing an escalation of reactive oxidative species. CELLULAR AND MOLECULAR LIFE SCIENCES, vol. 79, pp. 500-500, ISSN:1420-9071 DOI

Roberta Cascella, Alessandra Bigi, Dylan Giorgino Riffert, Maria Cristina Gagliani, Emilio Ermini, Matteo Moretti, Katia Cortese, Cristina Cecchi, Fabrizio Chiti (2022). A quantitative biology approach correlates neuronal toxicity with the largest inclusions of TDP-43. SCIENCE ADVANCES, vol. eabm6376, pp. 1-13, ISSN:2375-2548 DOI

Alessandra Bigi, Roberta Cascella, Fabrizio Chiti, Cristina Cecchi (2022). Amyloid fibrils act as a reservoir of soluble oligomers, the main culprits in protein deposition diseases. BIOESSAYS, vol. Volume 44, pp. 1-11, ISSN:1521-1878 DOI

Claudia Capitini, Luca Pesce, Giulia Fani, Giacomo Mazzamuto, Massimo Genovese, Alessandra Franceschini, Paolo Paoli, Giuseppe Pieraccini, Michael Zasloff, Fabrizio Chiti, Francesco S Pavone, Martino Calamai (2022). Studying the trafficking of labeled trodusquemine and its application as nerve marker for light-sheet and expansion microscopy. THE FASEB JOURNAL, vol. 38, pp. e22655-e22655, ISSN:0892-6638 DOI

Tommaso Staderini, Alessandra Bigi, Daniele Mongiello, Cristina Cecchi, Fabrizio Chiti (2022). Biophysical characterization of full-length TAR DNA-binding protein (TDP-43) phase separation.. PROTEIN SCIENCE, vol. 31, pp. e4509-e4509, ISSN:0961-8368 DOI

Limbocker, Ryan; Errico, Silvia; Barbut, Denise; Knowles, Tuomas P. J.; Vendruscolo, Michele; Chiti, Fabrizio; Zasloff, Michael (2022). Squalamine and trodusquemine: two natural products for neurodegenerative diseases, from physical chemistry to the clinic. NATURAL PRODUCT REPORTS, vol. 39, pp. 742-753, ISSN:0265-0568 DOI

Kreiser, Ryan P; Wright, Aidan K; Sasser, Liam R; Rinauro, Dillon J; Gabriel, Justus M; Hsu, Claire M; Hurtado, Jorge A; McKenzie, Tristan L; Errico, Silvia; Albright, J Alex; Richardson, Lance; Jaffett, Victor A; Riegner, Dawn E; Nguyen, Lam T; LeForte, Kathleen; Zasloff, Michael; Hollows, Jared E; Chiti, Fabrizio; Vendruscolo, Michele; Limbocker, Ryan (2022). A Brain-Permeable Aminosterol Regulates Cell Membranes to Mitigate the Toxicity of Diverse Pore-Forming Agents. ACS CHEMICAL NEUROSCIENCE, vol. 13, pp. 1219-1231, ISSN:1948-7193 DOI

Chiti, Fabrizio; Kelly, Jeffery W (2022). Small molecule protein binding to correct cellular folding or stabilize the native state against misfolding and aggregation. CURRENT OPINION IN STRUCTURAL BIOLOGY, vol. 72, pp. 267-278, ISSN:0959-440X DOI

Fani, Giulia; Chiti, Fabrizio (2022). Mechanosensitivity of N-methyl-D-aspartate receptors (NMDAR) is the key through which amyloid beta oligomers activate them. NEURAL REGENERATION RESEARCH, vol. 17, pp. 1263-1264, ISSN:1673-5374 DOI

Chiti, Fabrizio; Sablina, Anna (2022). Editorial overview: Folding and binding. CURRENT OPINION IN STRUCTURAL BIOLOGY, vol. 74, pp. 102359-102359, ISSN:0959-440X DOI

Moretti, Matteo; Marzi, Isabella; Cantarutti, Cristina; Vivoli Vega, Mirella; Mandaliti, Walter; Mimmi, Maria Chiara; Bemporad, Francesco; Corazza, Alessandra; Chiti, Fabrizio (2022). Conversion of the Native N-Terminal Domain of TDP-43 into a Monomeric Alternative Fold with Lower Aggregation Propensity. MOLECULES, vol. 27, pp. 0-0, ISSN:1420-3049 DOI

Fusco, Giuliana; Bemporad, Francesco; Chiti, Fabrizio; Dobson, Christopher M; De Simone, Alfonso (2022). The role of structural dynamics in the thermal adaptation of hyperthermophilic enzymes. FRONTIERS IN MOLECULAR BIOSCIENCES, vol. 9, pp. 981312-981312, ISSN:2296-889X DOI

Ryan Limbocker, Roxine Staats, Sean Chia, Francesco S Ruggeri, Benedetta Mannini, Catherine K Xu, Michele Perni, Roberta Cascella, Alessandra Bigi, Liam R Sasser, Natalie R Block, Aidan K Wright, Ryan P Kreiser, Edward T Custy, Georg Meisl, Silvia Errico, Johnny Habchi, Patrick Flagmeier, Tadas Kartanas, Jared E Hollows, Lam T Nguyen, Kathleen LeForte, Denise Barbut, Janet R Kumita, Cristina Cecchi, Michael Zasloff, Tuomas P J Knowles, Christopher M Dobson, Fabrizio Chiti, Michele Vendruscolo (2021). Squalamine and its derivatives modulate the aggregation of amyloid-β and α-synuclein and suppress the toxicity of their oligomers. FRONTIERS IN NEUROSCIENCE, vol. 15, pp. 1-17, ISSN:1662-453X DOI

Roberta Cascella, Serene W Chen , Alessandra Bigi, José D Camino, Catherine K Xu, Christopher M Dobson, Fabrizio Chiti, Nunilo Cremades, Cristina Cecchi (2021). The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells. NATURE COMMUNICATIONS, vol. 12, pp. 1-16, ISSN:2041-1723 DOI

Giulia Fani, Benedetta Mannini, Giulia Vecchi, Roberta Cascella, Cristina Cecchi, Christopher M. Dobson, Michele Vendruscolo, Fabrizio Chiti (2021). Aβ oligomers dysregulate calcium homeostasis by mechanosensitive activation of AMPA and NMDA receptors.. ACS CHEMICAL NEUROSCIENCE, vol. 12, pp. 766-781, ISSN:1948-7193 DOI

Perni, Michele; Mannini, Benedetta; Xu, Catherine K; Kumita, Janet R; Dobson, Christopher M; Chiti, Fabrizio; Vendruscolo, Michele (2021). Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegans. SCIENTIFIC REPORTS, vol. 11, pp. 0-0, ISSN:2045-2322 DOI

Qafary, Minoo; Khajeh, Khosro; Ramazzotti, Matteo; Moosavi-Movahedi, Ali Akbar; Chiti, Fabrizio (2021). Urea titration of a lipase from Pseudomonas sp. reveals four different conformational states, with a stable partially folded state explaining its high aggregation propensity. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, vol. 174, pp. 32-41, ISSN:0141-8130 DOI

Errico, Silvia; Ramshini, Hassan; Capitini, Claudia; Canale, Claudio; Spaziano, Martina; Barbut, Denise; Calamai, Martino; Zasloff, Michael; Oropesa-Nuñez, Reinier; Vendruscolo, Michele; Chiti, Fabrizio (2021). Quantitative Measurement of the Affinity of Toxic and Nontoxic Misfolded Protein Oligomers for Lipid Bilayers and of its Modulation by Lipid Composition and Trodusquemine. ACS CHEMICAL NEUROSCIENCE, vol. 12, pp. 3189-3202, ISSN:1948-7193 DOI

Capitini, Claudia; Fani, Giulia; Vivoli Vega, Mirella; Penco, Amanda; Canale, Claudio; Cabrita, Lisa D; Calamai, Martino; Christodoulou, John; Relini, Annalisa; Chiti, Fabrizio (2021). Full-length TDP-43 and its C-terminal domain form filaments in vitro having non-amyloid properties. AMYLOID, vol. 28, pp. 56-65, ISSN:1744-2818 DOI

Leal-Lasarte, Magdalena; Mannini, Benedetta; Chiti, Fabrizio; Vendruscolo, Michele; Dobson, Christopher M; Roodveldt, Cintia; Pozo, David (2021). Distinct responses of human peripheral blood cells to different misfolded protein oligomers. IMMUNOLOGY, vol. 164, pp. 358-371, ISSN:1365-2567 DOI

Farrugia, Maria Ylenia; Caruana, Mario; Ghio, Stephanie; Camilleri, Angelique; Farrugia, Claude; Cauchi, Ruben J; Cappelli, Sara; Chiti, Fabrizio; Vassallo, Neville (2020). Toxic oligomers of the amyloidogenic HypF-N protein form pores in mitochondrial membranes. SCIENTIFIC REPORTS, vol. 10, pp. 17733-17733, ISSN:2045-2322 DOI

Limbocker R.; Mannini B.; Cataldi R.; Chhangur S.; Wright A.K.; Kreiser R.P.; Albright J.A.; Chia S.; Habchi J.; Sormanni P.; Kumita J.R.; Ruggeri F.S.; Dobson C.M.; Chiti F.; Aprile F.A.; Vendruscolo M. (2020). Rationally designed antibodies as research tools to study the structure–toxicity relationship of amyloid-β oligomers. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, vol. 21, pp. 1-18, ISSN:1661-6596 DOI

Vivoli-Vega M.; Guri P.; Chiti F.; Bemporad F. (2020). Insight into the Folding and Dimerization Mechanisms of the N-Terminal Domain from Human TDP-43. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, vol. 21, pp. 6259-6259, ISSN:1422-0067 DOI

Errico, Silvia; Lucchesi, Giacomo; Odino, Davide; Muscat, Stefano; Capitini, Claudia; Bugelli, Chiara; Canale, Claudio; Ferrando, Riccardo; Grasso, Gianvito; Barbut, Denise; Calamai, Martino; Danani, Andrea; Zasloff, Michael; Relini, Annalisa; Caminati, Gabriella; Vendruscolo, Michele; Chiti, Fabrizio (2020). Making biological membrane resistant to the toxicity of misfolded protein oligomers: a lesson from trodusquemine. NANOSCALE, vol. 12, pp. 22596-22614, ISSN:2040-3372 DOI

Ghadami S.A.; Chia S.; Ruggeri F.S.; Meisl G.; Bemporad F.; Habchi J.; Cascella R.; Dobson C.M.; Vendruscolo M.; Knowles T.P.J.; Chiti F. (2020). Transthyretin Inhibits Primary and Secondary Nucleations of Amyloid-β Peptide Aggregation and Reduces the Toxicity of Its Oligomers. BIOMACROMOLECULES, vol. 21, pp. 1112-1125, ISSN:1525-7797 DOI

Martina Banchelli, Roberta Cascella, Cristiano D'Andrea, Leszek Cabaj, Iacopo Osticioli, Daniele Ciofini, Mai Suan Li, de Krzysztof Skupie´n, Marella de Angelis, Salvatore Siano, Cristina Cecchi, Roberto Pini, Giovanni La Penna, Fabrizio Chiti, Paolo Matteini (2020). Nanoscopic insights into the surface conformation of neurotoxic amyloid b oligomers. RSC ADVANCES, vol. 10, pp. 21907-21913, ISSN:2046-2069 DOI

Elham Rezvani Boroujeni, Seyed Masoud Hosseini, Giulia Fani, Cristina Cecchi, Fabrizio Chiti (2020). Soluble Prion peptide 107–120 protects neuroblastoma SH-SY5Y cells against oligomers associated with Alzheimer’s disease. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, vol. 21, pp. 7273-7294, ISSN:1422-0067 DOI

Ryan Limbocker, Benedetta Mannini, Francesco S. Ruggeri, Roberta Cascella, Catherine K. Xu, Michele Perni, Sean Chia, Serene W. Chen, Johnny Habchi, Alessandra Bigi, Ryan P. Kreiser, Aidan K. Wright, J. Alex Albright, Tadas Kartanas, Janet R. Kumita, Nunilo Cremades, Michael Zasloff, Cristina Cecchi, Tuomas P. J. Knowles, Fabrizio Chiti, Michele Vendruscolo, Christopher M. Dobson (2020). Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism. COMMUNICATIONS BIOLOGY, vol. 3, pp. 0-0, ISSN:2399-3642 DOI Accesso ONLINE all'editore

Jazaj D.; Ghadami S.A.; Bemporad F.; Chiti F. (2019). Probing conformational changes of monomeric transthyretin with second derivative fluorescence. SCIENTIFIC REPORTS, vol. 9, pp. 10988-10988, ISSN:2045-2322 DOI Accesso ONLINE all'editore

Hassan Ramshini , Reza Tayebee, Alessandra Bigi, Francesco Bemporad, Cristina Cecchi, Fabrizio Chiti (2019). Identification of Novel 1,3,5-Triphenylbenzene Derivative Compounds as Inhibitors of Hen Lysozyme Amyloid Fibril Formation. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, vol. 20, pp. 1-18, ISSN:1661-6596 DOI Accesso ONLINE all'editore

Baum J.; Chiti F.; De Simone A.; Knowles T.P.J.; Kumita J.R.; Radford S.E.; Robinson C.V.; Salvatella X.; Valelli K.; Vendruscolo M.; Pastore A.; Tartaglia G.G. (2019). Homage to Chris Dobson. FRONTIERS IN MOLECULAR BIOSCIENCES, vol. 6, pp. 137-137, ISSN:2296-889X DOI

Ryan Limbocker, Sean Chia, Francesco S. Ruggeri, Michele Perni, Roberta Cascella, Gabriella T. Heller, Georg Meisl, Benedetta Mannini, Johnny Habchi, Thomas C.T. Michaels, Pavan K. Challa, Minkoo Ahn, Samuel T. Casford, Nilumi Fernando, Catherine K. Xu, Nina D. Kloss, Samuel I.A. Cohen, Janet R. Kumita, Cristina Cecchi, Michael Zasloff, Sara Linse , Tuomas P.J. Knowles, Fabrizio Chiti, Michele Vendruscolo, Christopher M. Dobson (2019). Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes. NATURE COMMUNICATIONS, vol. 10, pp. 1-13, ISSN:2041-1723 DOI Accesso ONLINE all'editore

Cascella R, Perni M, Chen SW, Fusco G, Cecchi C, Vendruscolo M, Chiti F, Dobson CM, De Simone A. (2019). Probing the origin of the toxicity of oligomeric aggregates of α-synuclein with antibodies. ACS CHEMICAL BIOLOGY, vol. 14, pp. 1352-1362, ISSN:1554-8937 DOI

Francesco Bemporad, Cristina Cecchi, Fabrizio Chiti (2019). Capturing Aβ42 aggregation in the cell. JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 294, pp. 1488-1489, ISSN:1083-351X DOI Accesso ONLINE all'editore

Mannini, Benedetta; Vecchi, Giulia; Labrador-Garrido, Adahir; Fabre, Bertrand; Fani, Giulia; Munoz Franco, Jaime; Lilley, Kathryn S; Pozo, David; Vendruscolo, Michele; Chiti, Fabrizio; Dobson, Christopher M; Roodveldt, Cintia (2019). Differential interactome and innate immune response activation of two structurally distinct misfolded protein oligomers. ACS CHEMICAL NEUROSCIENCE, pp. 0-0, ISSN:1948-7193 DOI

Cascella R, Fani G, Bigi A, Chiti F, Cecchi C. (2019). Partial Failure of Proteostasis Systems Counteracting TDP-43 Aggregates in Neurodegenerative Diseases. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, vol. 20, pp. 0-0, ISSN:1661-6596 DOI

Vivoli Vega M, Cascella R, Chen SW, Fusco G, De Simone A, Dobson CM, Cecchi C, Chiti F. (2019). The toxicity of misfolded protein oligomers is independent of their secondary structure. ACS CHEMICAL BIOLOGY, vol. 14, pp. 1593-1600, ISSN:1554-8937 DOI

Vivoli Vega, Mirella; Nigro, Alessia; Luti, Simone; Capitini, Claudia; Fani, Giulia; Gonnelli, Leonardo; Boscaro, Francesca; Chiti, Fabrizio (2019). Isolation and characterization of soluble human full-length TDP-43 associated with neurodegeneration. FASEB JOURNAL, pp. fj201900474R-fj201900474R, ISSN:1530-6860 DOI

Del Poggetto, Edoardo; Toto, Angelo; Aloise, Chiara; Di Piro, Francesco; Gori, Ludovica; Malatesta, Francesco; Gianni, Stefano; Chiti, Fabrizio; Bemporad, Francesco* (2018). Stability of an aggregation-prone partially folded state of human profilin-1 correlates with aggregation propensity. THE JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 293, pp. 10303-10313, ISSN:0021-9258 DOI Accesso ONLINE all'editore

Rashno F.; Khajeh K.; Dabirmanesh B.; Sajedi R.H.; Chiti F. (2018). Insight into the aggregation of lipase from Pseudomonas sp. using mutagenesis: protection of aggregation prone region by adoption of α-helix structure. PROTEIN ENGINEERING, DESIGN & SELECTION, vol. 31, pp. 419-426, ISSN:1741-0134 DOI

D'Andrea, Cristiano; Foti, Antonino; Cottat, Maximilien; Banchelli, Martina; Capitini, Claudia; Barreca, Francesco; Canale, Claudio; de Angelis, Marella; Relini, Annalisa; Maragò, Onofrio M.; Pini, Roberto; Chiti, Fabrizio*; Gucciardi, Pietro G.; Matteini, Paolo (2018). Nanoscale Discrimination between Toxic and Nontoxic Protein Misfolded Oligomers with Tip-Enhanced Raman Spectroscopy. SMALL, vol. 14, pp. e1800890-e1800890, ISSN:1613-6810 DOI Accesso ONLINE all'editore

Perni M, Flagmeier P, Limbocker R, Cascella R, Aprile FA, Galvagnion C, Heller GT, Meisl G, Chen SW, Kumita JR, Challa PK, Kirkegaard JB, Cohen SIA, Mannini B, Barbut D, Nollen EAA, Cecchi C, Cremades N, Knowles TPJ, Chiti F, Zasloff M, Vendruscolo M, Dobson CM (2018). Multistep Inhibition of α‑Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine. ACS CHEMICAL BIOLOGY, vol. 13, pp. 2308-2319, ISSN:1554-8929 DOI

Capitini, Claudia; Patel, Jayneil R.; Natalello, Antonino; D'Andrea, Cristiano; Relini, Annalisa; Jarvis, James A.; Birolo, Leila; Peduzzo, Alessia; Vendruscolo, Michele; Matteini, Paolo; Dobson, Christopher M.; De Simone, Alfonso; Chiti, Fabrizio* (2018). Structural differences between toxic and nontoxic HypF-N oligomers. CHEMICAL COMMUNICATIONS, vol. 54, pp. 8637-8640, ISSN:1359-7345 DOI Accesso ONLINE all'editore

Reinier Oropesa-Nunez, Sandeep Keshavan, Silvia Dante, Alberto Diaspro, Benedetta Mannini, Claudia Capitini, Cristina Cecchi, Massimo Stefani, Fabrizio Chiti, Claudio Canale (2018). Toxic HypF-N oligomers selectively bind the plasma membrane to impair cell adhesion capability. BIOPHYSICAL JOURNAL, vol. 114, pp. 1357-1367, ISSN:0006-3495 DOI

Patel, Jayneil R.; Xu, Yingqi; Capitini, Claudia; Chiti, Fabrizio; De Simone, Alfonso* (2018). Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers. BIOMOLECULAR NMR ASSIGNMENTS, vol. 12, pp. 273-277, ISSN:1874-2718 DOI Accesso ONLINE all'editore

Elia, Francesco; Cantini, Francesca; Chiti, Fabrizio; Dobson, Christopher Martin; Bemporad, Francesco (2017). Direct Conversion of an Enzyme from Native-like to Amyloid-like Aggregates within Inclusion Bodies. BIOPHYSICAL JOURNAL, vol. 112, pp. 2540-2551, ISSN:0006-3495 DOI Accesso ONLINE all'editore

Cascella, Roberta; Evangelisti, Elisa; Bigi, Alessandra; Becatti, Matteo; Fiorillo, Claudia; Stefani, Massimo; Chiti, Fabrizio; Cecchi, Cristina (2017). Soluble Oligomers Require a Ganglioside to Trigger Neuronal Calcium Overload. JOURNAL OF ALZHEIMER'S DISEASE, vol. 60, pp. 923-938, ISSN:1387-2877 DOI

Giuliana, Fusco; Chen, Serene W.; Williamson, Philip T. F.; Roberta, Cascella; Michele, Perni; Jarvis, James A.; Cristina, Cecchi; Michele, Vendruscolo; Fabrizio, Chiti; Nunilo, Cremades; Liming, Ying; Dobson, Christopher M.; Alfonso De Simone, (2017). Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers. SCIENCE, vol. 358, pp. 1440-1443, ISSN:0036-8075 DOI Accesso ONLINE all'editore

Perni, Michele; Galvagnion, Céline; Maltsev, Alexander; Meisl, Georg; Müller, Martin B. D.; Challa, Pavan K.; Kirkegaard, Julius B.; Flagmeier, Patrick; Cohen, Samuel I. A.; Cascella, Roberta; Chen, Serene W.; Limboker, Ryan; Sormanni, Pietro; Heller, Gabriella T.; Aprile, Francesco A.; Cremades, Nunilo; Cecchi, Cristina; Chiti, Fabrizio; Nollen, Ellen A. A.; Knowles, Tuomas P. J.; Vendruscolo, Michele; Bax, Adriaan; Zasloff, Michael; M. Dobson, Christopher (2017). A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, vol. 114, pp. 1009-1017, ISSN:0027-8424 DOI Accesso ONLINE all'editore

Rashno, Fatemeh; Khajeh, Khosro*; Capitini, Claudia; Sajedi, Reza H.; Shokri, Maryam Monsef; Chiti, Fabrizio (2017). Very rapid amyloid fibril formation by a bacterial lipase in the absence of a detectable lag phase. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, vol. 1865, pp. 652-663, ISSN:1570-9639 DOI Accesso ONLINE all'editore

Ghadami, Seyyed Abolghasem; Bemporad, Francesco; Sala, Benedetta Maria; Tiana, Guido; Ricagno, Stefano; Chiti, Fabrizio (2017). FRET studies of various conformational states adopted by transthyretin. CELLULAR AND MOLECULAR LIFE SCIENCES, pp. 1-22, ISSN:1420-682X DOI Accesso ONLINE all'editore

Mannini, Benedetta; Chiti, Fabrizio (2017). Chaperones as Suppressors of Protein Misfolded Oligomer Toxicity. FRONTIERS IN MOLECULAR NEUROSCIENCE, vol. 10, pp. 98-98, ISSN:1662-5099 DOI

Cascella, Roberta; Fani, Giulia; Capitini, Claudia; Rusmini, Paola; Poletti, Angelo; Cecchi, Cristina; Chiti, Fabrizio* (2017). Quantitative assessment of the degradation of aggregated TDP-43 mediated by the ubiquitin proteasome system and macroautophagy. THE FASEB JOURNAL, vol. 31, pp. 5609-5624, ISSN:0892-6638 DOI Accesso ONLINE all'editore

Chiti, Fabrizio*; Dobson, Christopher M. (2017). Protein misfolding, amyloid formation, and human disease: A summary of progress over the last decade. ANNUAL REVIEW OF BIOCHEMISTRY, vol. 86, pp. 27-68, ISSN:0066-4154 DOI Accesso ONLINE all'editore

Evangelisti, Elisa; Cascella, Roberta; Becatti, Matteo; Marrazza, Giovanna; Dobson, Christopher M.; Chiti, Fabrizio; Stefani, Massimo; Cecchi, Cristina (2016). Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases. SCIENTIFIC REPORTS, vol. 6, pp. 1-14, ISSN:2045-2322 DOI Accesso ONLINE all'editore

Pasqualina Liana Scognamiglio; Concetta Di Natale; Marilisa Leone; Roberta Cascella; Cristina Cecchi; Lisa Lirussi; Giulia Antoniali; Domenico Riccardi; Giancarlo Morelli; Gianluca Tell; Fabrizio Chiti; Daniela Marasco (2016). Destabilisation, aggregation, toxicity and cytosolic mislocalisation of nucleophosmin regions associated with acute myeloid leukemia. ONCOTARGET, vol. 7, pp. 59129-59143, ISSN:1949-2553 DOI Accesso ONLINE all'editore

Cascella, Roberta; Capitini, Claudia; Fani, Giulia; Dobson, Christopher M.; Cecchi, Cristina; Chiti, Fabrizio (2016). Quantification of the Relative Contributions of Loss-of function and Gain-of-function Mechanisms in TAR DNA-binding Protein 43 (TDP-43) Proteinopathies. JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 291, pp. 19437-19448, ISSN:1083-351X DOI Accesso ONLINE all'editore

Del Poggetto, Edoardo; Gori, Ludovica; Chiti, Fabrizio* (2016). Biophysical analysis of three novel profilin-1 variants associated with amyotrophic lateral sclerosis indicates a correlation between their aggregation propensity and the structural features of their globular state. BIOLOGICAL CHEMISTRY, vol. 397, pp. 927-937, ISSN:1431-6730 DOI Accesso ONLINE all'editore

Oropesa-Nuñez, R; Seghezza, S; Dante, S; Diaspro, A; Cascella, R; Cecchi, C; Stefani, M; Chiti, F; Canale, C (2016). Interaction of toxic and non-toxic HypF-N oligomers with lipid bilayers investigated at high resolution with atomic force microscopy. ONCOTARGET, vol. 7, pp. 44991-45004, ISSN:1949-2553

Cappelli, S; Penco, A; Mannini, Benedetta; Cascella, Roberta; Wilson, M; Ecroyd, H; Li, X; Buxbaum, J; Dobson, Cm; Cecchi, Cristina; Relini, A; Chiti, Fabrizio (2016). Effect of molecular chaperones on aberrant protein oligomers in vitro: super- versus sub-stoichiometric chaperone concentrations. BIOLOGICAL CHEMISTRY, pp. 0-0, ISSN:1431-6730 DOI

Ramshini, Hassan; Mannini, Benedetta; Khodayari, Kaveh; Ebrahim-Habibi, Azadeh; Moghaddasi, Azam Sadat; Tayebee, Reza; Chiti, Fabrizio* (2016). Bis(indolyl)phenylmethane derivatives are effective small molecules for inhibition of amyloid fibril formation by hen lysozyme. EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY, vol. 124, pp. 361-371, ISSN:0223-5234 DOI Accesso ONLINE all'editore

M. Leri; D. Nosi; A. Natalello; R. Porcari; M. Ramazzotti; F. Chiti; V. Bellotti; S.M. Doglia; M. Stefani; M. Bucciantini (2016). The polyphenol Oleuropein aglycone hinders the growth of toxic transthyretin amyloid assemblies. JOURNAL OF NUTRITIONAL BIOCHEMISTRY, vol. 30, pp. 153-166, ISSN:0955-2863 DOI Accesso ONLINE all'editore

Guerrini, Luca; Arenal, Raul; Mannini, Benedetta; Chiti, Fabrizio; Pini, Roberto; Matteini, Paolo; Alvarez-Puebla, Ramon A (2015). SERS Detection of Amyloid Oligomers on Metallorganic-Decorated Plasmonic Beads. ACS APPLIED MATERIALS & INTERFACES, vol. 7, pp. 9420-9428, ISSN:1944-8252 DOI

Conti, Simona; Li, Xinyi; Gianni, Stefano; Ghadami, Seyyed Abolghasem; Buxbaum, Joel; Cecchi, Cristina; Chiti, Fabrizio; Bemporad, Francesco (2015). Investigating partially unfolded conformations populated by monomeric human transthyretin. In: 40th FEBS Congress: The Biochemical basis of life, WILEY-BLACKWELL, vol. 282 Supplement 1, pp. 325-325.

Cascella, Roberta; Evangelisti, Elisa; Becatti, Matteo; Dobson, C. M.; Chiti, Fabrizio; Stefani, Massimo; Cecchi, Cristina (2015). Molecular links between aberrant protein oligomers and neurodegeneration in Alzheimer’s disease. In: 40TH FEBS CONGRESS The Biochemical Basis of Life, Berlin, July 4–9, 2015, FEBS Press, vol. 282, pp. 172-173.

Lindberg, Iris; Shorter, James; Wiseman, R Luke; Chiti, Fabrizio; Dickey, Chad A; Mclean, Pamela J (2015). Chaperones in Neurodegeneration. THE JOURNAL OF NEUROSCIENCE, vol. 35, pp. 13853-13859, ISSN:1529-2401 DOI

Del Poggetto, Edoardo; Chiti, Fabrizio; Bemporad, Francesco (2015). The Folding process of Human Profilin-1, a novel protein associated with familial amyotrophic lateral sclerosis. SCIENTIFIC REPORTS, vol. 5, pp. 1-12, ISSN:2045-2322 DOI Accesso ONLINE all'editore

Del Poggetto, E; Bemporad, F; Tatini, F; Chiti, F. (2015). Mutations of Profilin-1 Associated with Amyotrophic Lateral Sclerosis Promote Aggregation Due to Structural Changes of Its Native State. ACS CHEMICAL BIOLOGY, vol. 10, pp. 2553-2563, ISSN:1554-8937 DOI

Di Natale, Concetta; Scognamiglio, Pasqualina Liana; Cascella, Roberta; Cecchi, Cristina; Russo, Anna; Leone, Marilisa; Penco, Amanda; Relini, Annalisa; Federici, Luca; Di Matteo, Adele; Chiti, Fabrizio; Vitagliano, Luigi; Marasco, Daniela (2015). Nucleophosmin contains amyloidogenic regions that are able to form toxic aggregates under physiological conditions. THE FASEB JOURNAL, vol. 29, pp. 3689-3701, ISSN:0892-6638 DOI Accesso ONLINE all'editore

Evangelisti, Elisa; Cascella, Roberta; Calamai, Martino; Chiti, Fabrizio; Cecchi, Cristina; Stefani, Massimo (2014). Single particle tracking to study the binding of protein misfolded oligomer to membrane ganglioside GM1. In: FEBS EMBO 2014 Conference, Paris, August 30- 4 September 2014, FEBS Press, vol. 281, pp. 208-208.

Conti S; Li X; Gianni S; Ghadami SA; Buxbaum JN; Cecchi C; Chiti F; and Bemporad F. (2014). A Complex Equilibrium among Partially Unfolded Conformations in Monomeric Transthyretin. BIOCHEMISTRY, vol. 53, pp. 4381-4392, ISSN:0006-2960 DOI

Capitini, Claudia; Conti, Simona; Perni, Michele; Guidi, Francesca; Cascella, Roberta; Poli, Angela De; Penco, Amanda; Relini, Annalisa; Cecchi, Cristina; Chiti, Fabrizio (2014). TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells. In: FEBS EMBO 2014 Conference, Paris, August 30- 4 September 2014, FEBS Press, vol. 281, pp. 642-642.

Mannini B; Mulvihill E; Sgromo C; Cascella R; Khodarahmi R; Ramazzotti M; Dobson CM; Cecchi C; and Chiti F (2014). Toxicity of Protein Oligomers Is Rationalized by a Function Combining Size and Surface Hydrophobicity. ACS CHEMICAL BIOLOGY, vol. 9, pp. 2309-2317, ISSN:1554-8929 DOI

de Rosa M;Bemporad F;Pellegrino S;Chiti F;Bolognesi M;Ricagno S (2014). Edge strand engineering prevents native-like aggregation in Sulfolobus solfataricus acylphosphatase.. THE FEBS JOURNAL, vol. 281, pp. 4072-4084, ISSN:1742-464X DOI

Claudia Capitini; Simona Conti; Michele Perni; Francesca Guidi; Roberta Cascella; Angela De Poli; Amanda Penco; Annalisa Relini; Cristina Cecchi; Fabrizio Chiti (2014). TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells. PLOS ONE, vol. 9, pp. e86720-e86720, ISSN:1932-6203 DOI

Monsef Shokri M;Ahmadian S;Bemporad F;Khajeh K;Chiti F (2013). Amyloid fibril formation by a normally folded protein in the absence of denaturants and agitation.. AMYLOID, vol. in press, pp. in press-in press, ISSN:1350-6129 DOI

Castillo V;Chiti F;Ventura S (2013). The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain.. PLOS ONE, vol. 8, pp. e58297-e58297, ISSN:1932-6203 DOI

Mangione PP;Esposito G;Relini A;Raimondi S;Porcari R;Giorgetti S;Corazza A;Fogolari F;Penco A;Goto Y;Lee YH;Yagi H;Cecconi C;Naqvi MM;Gillmore JD;Hawkins PN;Chiti F;Rolandi R;Taylor GW;Pepys MB;Stoppini M;Bellotti V (2013). Structure, folding dynamics and amyloidogenesis of Asp76Asn β2-microglobulin: roles of shear flow, hydrophobic surfaces and α crystallin.. THE JOURNAL OF BIOLOGICAL CHEMISTRY, vol. in press, pp. in press-in press, ISSN:0021-9258 DOI

Francesca Tatini; Anna Maria Pugliese; Chiara Traini; Sandra Niccoli; Giovanna Maraula; Teresa Ed Dami; Benedetta Mannini; Tania Scartabelli; Felicita Pedata; Fiorella Casamenti; Fabrizio Chiti (2013). Amyloid-β oligomer synaptotoxicity is mimicked by oligomers of the model protein HypF-N. NEUROBIOLOGY OF AGING, vol. 34, pp. 2100-2109, ISSN:0197-4580 DOI

Clauda, Capitini; Simona, Conti; Michele, Perni; Francesca, Guidi; Roberta, Cascella; Amanda, Penco; Annalisa, Relini; Cristina, Cecchi; Fabrizio, Chiti (2013). TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells. In: 38th FEBS Congress, Saint Petersburg, Russia, July 6–11, 2013, FEBS Press, vol. 280, pp. 415-415.

Roberta Cascella; Simona Conti; Benedetta Mannini; Xinyi Li; Joel N. Buxbaum; Bruno Tiribilli; Fabrizio Chiti; Cristina Cecchi (2013). Transthyretin suppresses the toxicity of oligomers formed by misfolded proteins in vitro. BIOCHIMICA ET BIOPHYSICA ACTA. MOLECULAR BASIS OF DISEASE, vol. 1832, pp. 2302-2314, ISSN:0925-4439 DOI

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B.Ahmad; I.Vigliotta; F.Tatini; S.Campioni; B.Mannini; J.Winkelmann; B.Tiribilli; F.Chiti (2011). The induction of α-helical structure in partially unfolded HypF-N does not affect its aggregation propensity. PROTEIN ENGINEERING, DESIGN & SELECTION, vol. 24, pp. 553-563, ISSN:1741-0126 DOI

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K.F. DUBAY; A.P. PAWAR; F. CHITI ; J. ZURDO; C.M. DOBSON; M. VENDRUSCOLO (2004). Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains.. JOURNAL OF MOLECULAR BIOLOGY, vol. 341, pp. 1317-1326, ISSN:0022-2836 DOI

D. DEGL'INNOCENTI; N. TADDEI; M. RAMAZZOTTI; M. STEFANI; F. CHITI; G. RAMPONI (2004). Selection of antibody fragments specific for analpha-helix region of acylphosphatase. JOURNAL OF MOLECULAR RECOGNITION, vol. 17, pp. 62-66, ISSN:0952-3499 DOI Accesso ONLINE all'editore

C. CAPANNI; N. TADDEI; S. GABRIELLI; L. MESSORI; P. ORIOLI; F. CHITI; M. STEFANI; G. RAMPONI (2004). Investigation of the effects of copper ions on protein aggregation using a model system.. CELLULAR AND MOLECULAR LIFE SCIENCES, vol. 61, pp. 982-991, ISSN:1420-682X

G. PLAKOUTSI; N. TADDEI; M. STEFANI; F. CHITI (2004). Aggregation of the acylphosphatase from S. solfataricus. The folded and partially unfolded states can be both precursors for amyloid formation.. THE JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 279, pp. 14111-14119, ISSN:0021-9258 DOI

A. RELINI; S. TORRASSA; R. ROLANDI; A. GLIOZZI; C. ROSANO; C. CANALE; M. BOLOGNESI; G. PLAKOUTSI; M. BUCCIANTINI; F. CHITI; M. STEFANI (2004). Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils.. JOURNAL OF MOLECULAR BIOLOGY, vol. 338, pp. 943-957, ISSN:0022-2836 DOI

F. BEMPORAD; C. CAPANNI; M. CALAMAI; M.L. TUTINO; M. STEFANI; F. CHITI (2004). Studying the folding process of the acylphosphatase from Sulfolobus solfataricus. A comparative analysis with other proteins from the same superfamily. BIOCHEMISTRY, vol. 43, pp. 9116-9126, ISSN:0006-2960 DOI

M. MONTI; B.L. GAROLLA DI BARD; G. CALLONI; F. CHITI; A. AMOREASANO; G. RAMPONI; P. PUCCI (2004). The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process.. JOURNAL OF MOLECULAR BIOLOGY, vol. 336, pp. 253-262, ISSN:0022-2836 DOI

P. POLVERINO DE LAURETO; N. TADDEI; E. FRARE; C. CAPANNI; S. COSTANTINI; J. ZURDO; F. CHITI ; C.M. DOBSON; A. FONTANA (2003). Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis. JOURNAL OF MOLECULAR BIOLOGY, vol. 334, pp. 129-141, ISSN:0022-2836

G. ESPOSITO; J. GARCIA; P. MANGIONE; S. GIORGETTI; A. CORAZZA; P. VIGLINO; F. CHITI ; A. ANDREOLA; P. DUMY; D. BOOTH; P. HAWKINS; V. BELLOTTI (2003). STRUCTURAL AND FOLDING DYNAMICS PROPERTIES OF T70N VARIANT OF HUMAN LYSOZYME. THE JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 278, pp. 25910-25918, ISSN:0021-9258

G. CALLONI; N. TADDEI; K.W. PLAXCO; G. RAMPONI; M. STEFANI; F. CHITI (2003). Comparison of the folding processes of distantly related proteins. Importance of hydrophobic content in folding.. JOURNAL OF MOLECULAR BIOLOGY, vol. 330, pp. 577-591, ISSN:0022-2836

M. CALAMAI; N. TADDEI; M. STEFANI; G. RAMPONI; F. CHITI (2003). Relative influence of hydrophobicity and net charge in the aggregation of two homologous proteins.. BIOCHEMISTRY, vol. 42, pp. 15078-15083, ISSN:0006-2960

Donatella Degl’Innocenti;Matteo Ramazzotti;Riccardo Marzocchini;Fabrizio Chiti;Giovanni Raugei;Giampietro Ramponi (2003). Characterization of a novel Drosophila melanogaster acylphosphatase. FEBS LETTERS, vol. 535, pp. 171-174, ISSN:0014-5793 DOI

F.CHITI; M.STEFANI; N.TADDEI; G. RAMPONI; CM.DOBSON (2003). Rationalization of the effects of mutations on peptide and protein aggregation rates. NATURE, vol. 424, pp. 805-808, ISSN:0028-0836

F. CHITI ; N. TADDEI; F. BARONI; C. CAPANNI; M. STEFANI; G. RAMPONI; C.M. DOBSON (2002). Kinetic partitioning of protein folding and aggregation. NATURE STRUCTURAL BIOLOGY, vol. 9, pp. 137-143, ISSN:1072-8368

I. MILLET; L.E. TOWNSLEY; F. CHITI ; S. DONIACH; K. PLAXCO (2002). EQUILIBRIUM COLLAPSE AND THE KINETIC 'FOLDABILITY' OF PROTEINS.. BIOCHEMISTRY, vol. 41, pp. 321-325, ISSN:0006-2960

F. CHITI ; M. CALAMAI; N. TADDEI; M. STEFANI; G. RAMPONI; CM. DOBSON (2002). Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, vol. 99, pp. 16419-16426, ISSN:0027-8424

M. BUCCIANTINI; E. GIANNONI; F. CHITI; F. BARONI; L. FORMIGLI; J. ZURDO; N. TADDEI; G. RAMPONI; C. DOBSON; M. STEFANI (2002). Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. NATURE, vol. 416(6880), pp. 507-511, ISSN:0028-0836, Nature America Incorporated:345 Park Avenue South, 6th Floor:New York, NY 10010:(888)331-6288, EMAIL: institutions@natureny.com, INTERNET: http://www.nature.com, Fax: (212)689-9108: DOI

E. DE LORENZI; S. GROSSI; G. MASSOLINI; S. GIORGETTI; P. MANGIONE; A. ANDREOLA; F. CHITI ; V. BELLOTTI; G. CACCIALANZA (2002). CAPILLARY ELECTROPHORESIS INVESTIGATION OF A PARTIALLY UNFOLDED CONFORMATION OF ?2-MICROGLOBULIN.. ELECTROPHORESIS, vol. 23, pp. 918-925, ISSN:0173-0835

F. CHITI ; M. BUCCIANTINI; C. CAPANNI; N. TADDEI; C.M. DOBSON; M. STEFANI (2001). Solution conditions can promote formation of either amyloid protofilament or mature fibrils from the HypF N-terminal domain. PROTEIN SCIENCE, vol. 10, pp. 2541-2547, ISSN:0961-8368

F. CHITI; E. DE LORENZI; S. GROSSI; P. MANGIONE; S. GIORGETTI; G. CACCIALANZA; C.M.DOBSON; G. MERLINI; G. RAMPONI; V. BELLOTTI (2001). A partially structured species of beta 2-microglobulin is significantly populated under physiological conditions and involved in fibrillogenesis.. THE JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 276, pp. 46714-46721, ISSN:0021-9258

N. TADDEI; F. CHITI ; M. STEFANI; C. DOBSON; G. RAMPONI (2001). Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation.. PROTEIN SCIENCE, vol. 10(4), pp. 879-886, ISSN:0961-8368 DOI

F. CHITI ; P. MANGIONE; A. ANDREOLA; S. GIORGETTI; M. STEFANI; C.M. DOBSON; V. BELLOTTI; N. TADDEI (2001). Detection of two partially structured species in the folding process of the amyloidogenic protein beta 2-microglobulin.. JOURNAL OF MOLECULAR BIOLOGY, vol. 307, pp. 379-391, ISSN:0022-2836 DOI

N. TADDEI; C.CAPANNI; F.CHITI; M.STEFANI; CM.DOBSON; G.RAMPONI (2001). Folding and aggregation are selectively influenced by the conformational preferences of the alpha-helices of muscle acylphosphatase. THE JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 276, pp. 37149-37154, ISSN:0021-9258

B. Verzola; F. Chiti; G. Manao; ; P. Righetti (2000). Monitoring equilibria and kinetics of proteins folding/unfolding reactions by capillary zone electrophoresis. ANALYTICAL BIOCHEMISTRY, vol. 282, pp. 239-244, ISSN:0003-2697 DOI Accesso ONLINE all'editore

D. HAMADA, F. CHITI, J.I. GUIJARRO, M. KATAOKA, N. TADDEI; C.M. DOBSON (2000). Evidence concerning rate-limiting steps in protein folding from the effects of trifluoroethanol. NATURE STRUCTURAL BIOLOGY, vol. 7, pp. 58-61, ISSN:1072-8368 DOI

F. CHITI; N. TADDEI, M. BUCCIANTINI, P. WHITE, G. RAMPONI, C.M. DOBSON (2000). Mutational analysis of the propensity for amyloid formation by a globular protein.. EMBO JOURNAL, vol. 19, pp. 1441-1449, ISSN:0261-4189

N.TADDEI; F.CHITI; T.FIASCHI; M.BUCCIANTINI; C.CAPANNI; M. STEFANI; L.SERRANO; CM.DOBSON; G.RAMPONI G. (2000). Stabilisation of alpha-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatase folding. JOURNAL OF MOLECULAR BIOLOGY, vol. 300, pp. 633-647, ISSN:0022-2836

T. PERTINHEZ; D. HAMADA; L. J. SMITH; F. CHITI ; N. TADDEI; M. STEFANI; C.M. DOBSON; (2000). Initial denaturing conditions influence the slow folding phase of acylphosphatase associated with proline isomerisation. PROTEIN SCIENCE, vol. 9, pp. 1466-1473, ISSN:0961-8368

F. CHITI ; N. TADDEI; P.W. WHITE; M. BUCCIANTINI; F. MAGHERINI; M. STEFANI; C.M. DOBSON (1999). Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. NATURE STRUCTURAL BIOLOGY, vol. 6, pp. 1005-1009, ISSN:1072-8368

N.TADDEI; F.CHITI; P.PAOLI; T.FIASCHI; M.BUCCIANTINI; M. STEFANI; G.RAMPONI; CM.DOBSON (1999). Thermodynamics and kinetics of folding of common type acylphosphatase. BIOCHEMISTRY, vol. 38, pp. 2135-2142, ISSN:0006-2960, American Chemical Society:1155 Sixteenth Street Northwest:Washington, DC 20036:(800)227-5558, EMAIL: service@acs.org, INTERNET: http://www.pubs.acs.org, Fax: (614)447-3671:

F. CHITI ; P. WEBSTER; N. TADDEI; A. CLARK; M. STEFANI; G. RAMPONI; C. DOBSON (1999). Designing conditions for in vitro formation of amyloid fibrils.. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, vol. 96, pp. 3590-3594, ISSN:0027-8424

P. Paoli; N. Taddei; T. Fiaschi; D. Veggi; G. Camici; G. Manao; G. Raugei; F. Chiti; G. Ramponi (1999). The contribution of acidic residues to the conformational stability of common-type acylphosphatase. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, vol. 363, pp. 349-355, ISSN:0003-9861 DOI Accesso ONLINE all'editore

F. CHITI; N. TADDEI; E. GIANNONI; N. VAN NULAND; G. RAMPONI; C. DOBSON (1999). Development of enzymatic activity during protein folding. Detection of a spectroscopically silent native-like intermediate of muscle acylphosphatase.. THE JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 274(29), pp. 20151-20158, ISSN:0021-9258, American Society for Biochemistry and Molecular Biology:9650 Rockville Pike:Bethesda, MD 20814:(301)530-7145, EMAIL: asbmb@asbmb.faseb.org, INTERNET: http://www.faseb.org/asbmb, Fax: (301)571-1824:

F. CHITI ; N. TADDEI; P. WEBSTER; D. HAMADA; T. FIASCHI; G. RAMPONI; C. DOBSON (1999). Acceleration of the folding of acylphosphatase by stabilization of local secondary structure.. NATURE STRUCTURAL BIOLOGY, vol. 6, pp. 380-387, ISSN:1072-8368 DOI

M.Bucciantini; M.Stefani; N.Taddei; F.Chiti; S.Rigacci; G.Ramponi (1998). Sequence-specific recognition of peptide substrates by the low Mr phosphotyrosine protein phosphatase isoforms. FEBS LETTERS, vol. 422, pp. 213-217, ISSN:0014-5793

N.A.J van Nuland; F. Chiti; N. Taddei; G. Raugei; G. Ramponi; C.M. Dobson (1998). Slow folding of muscle acilfosfatase in the absence of intermediates. JOURNAL OF MOLECULAR BIOLOGY, vol. 283, pp. 883-891, ISSN:0022-2836

F. Chiti; F. Magherini; N. Taddei; C. Ilardi; M. Stefani; M. Bucciantini; C.M. Dobson; G. Ramponi (1998). Studies on enzymatic activity and conformational stability of muscle acylphosphatase mutated at conserved lysine residues. PROTEIN ENGINEERING, vol. 11, pp. 557-561, ISSN:0269-2139

F. Chiti; N.A.J. van Nuland; N. Taddei; F. Magherini; M. Stefani; G. Ramponi; C.M. Dobson (1998). Conformational stability of muscle acylphosphatase: the role of temperature, denaturant concentration and pH. BIOCHEMISTRY, vol. 37, pp. 1447-1455, ISSN:0006-2960

A. MODESTI; R. MARZOCCHINI; G. RAUGEI; F. CHITI; A. SERENI; F. MAGHERINI; G. RAMPONI (1998). Cloning, expression and characterization of a new human LMW-PTP isoform originating by alternative splicing. FEBS LETTERS, vol. 431, pp. 111-115, ISSN:0014-5793

F. Chiti; N. Taddei; N.A.J. van Nuland; F. Magherini; M. Stefani; G. Ramponi; C.M. Dobson (1998). Structural characterization of the transition state for folding of muscle acylphosphatase. JOURNAL OF MOLECULAR BIOLOGY, vol. 283, pp. 893-903, ISSN:0022-2836

N. Taddei; F. Chiti; F. Magherini; M. Stefani; M.M.G.M. Thunnissen; P. Nordlund; G. Ramponi (1997). Structural and kinetic investigations on the 15-21 and 42-45 loops of muscle acylphosphatase: evidence for their involvement in enzyme catalysis and conformational stabilization. BIOCHEMISTRY, vol. 36, pp. 7217-7224, ISSN:0006-2960

N. Taddei; F. Magherini; F. Chiti; M. Bucciantini; G. Raugei; M. Stefani; G. Ramponi (1996). C-terminal region contributes to muscle acylphosphatase three-dimensional structure stabilisation. FEBS LETTERS, vol. 384, pp. 172-176, ISSN:0014-5793

N. Taddei; M. Stefani; F. Magherini; F. Chiti; A. Modesti; G. Raugei; G. Ramponi (1996). Looking for residues involved in the muscle acylphosphatase catalytic mechanism and structural stabilization: role of Asn41, Ther42 and Thr46. BIOCHEMISTRY, vol. 22, pp. 7077-7083, ISSN:0006-2960

A. Modesti; N. Taddei; F. Chiti; M. Bucciantini; F. Magherini; S. Rigacci; M. Stefani; G. Raugei; G. Ramponi (1996). Properties of cys21-mutated muscle acylphosphatase. JOURNAL OF PROTEIN CHEMISTRY, vol. 15, pp. 27-34, ISSN:0277-8033

Fabrizio CHITI

Curriculum

Personalia

Work address: Dipartimento di Scienze Biomediche Sperimentali e Cliniche, Sezione di Scienze Biohchimiche, Università di Firenze, Viale Morgagni 50, I-50134 Firenze
Phone (lab) +39-055-2751220
e-mail fabrizio.chiti/at/unifi.it
web page http://www.fabriziochiti.it
Place and Date of birth: Florence (Italy) on 7^th July 1971
Sex: Male
Nationality: Italian
Marital Status: Married to Giada Socci since 1999, two children.

Education

20/12/1995M.Sc. Degree (Laurea vecchio ordinamento) in Biological Sciences at the University of Florence (Italy). Final marks were 110/110 cum laude et encomium.
20/05/2000PhD degree (D.Phil) in Chemistry at the University of Oxford (United Kingdom) with a thesis titled “Folding Studies of Acylphosphatase”. Supervisor was Prof. Christopher M. Dobson. Examiners were Martin Karplus and Alan Fersht.

Research Experience

01/10/1996 - 31/01/2000Ph.D. student in the laboratory of the Prof. C. M. Dobson, Department of Chemistry, University of Oxford (United Kingdom)
01/02/2000 - 31/01/2002Post-doc in the laboratory of Prof. G. Ramponi, Department of Biochemistry, University of Florence (Italy)
01/02/2002 - 31/10/2002Post-doc in the laboratory of Prof. C. M. Dobson, Department of Chemistry, University of Cambridge (UK)
01/11/2002 – 30/12/2010Associate Professor of Biochemistry, affiliated to the Department of Biochemistry for research and to the Faculty of Medicine for teaching, University of Florence (Italy)
30/12/2010 - presentFull Professor of Biochemistry, affiliated to the Department of Biochemistry for research and to the Faculty of Medicine for teaching, University of Florence (Italy)

Academic Honours

7/10/1996 - 8/10/1998“Marie Curie” Fellowship from the European Commission (no. BI04CT965113)
9/10/1998 – 8/01/1999Research Prize (Premio di Ricerca) from the Italian Society of Biochemistry
01/02/1999 – 31/01/2000“Giuseppe Guelfi” Training Fellowship (Borsa di Perfezionamento) from the Accademia Nazionale dei Lincei (no. 33/cc)
01/05/1999 – 31/08/1999Training fellowship (Contributo per Attività di Formazione) from the Consorzio Interuniversitario Biotecnologie (no. 681/u/MM/cp/98)
01/02/2000 – 31/01/2002Research Fellowship from the Italian Telethon Foundation (no. 453.bi)
13/09/1999Prize from the publishing company McGraw-Hill at the 44^th Congress of the Italian Society of Biochemistry as “author of a significant paper published from 1998 to 1999”
23/09/2000Gold Medal from the Italian Society of Biochemistry as author of the most significant poster presented at the 45^th Congress of the Italian Society of Biochemistry
27/10/2003"Jean-Francois LeFèvre Lecture" at the Ecole Supérieure de Biotechnologie de Strasbourg (ESBS)
12/10/2005Membership to the EMBO Young Investigator Programme for years 2006-2008.
Year 2005Elected Member of the Editorial Board of Protein Engineering Design and Selection
Year 2005Elected Member of the Editorial Board of Amyloid
Year 2006ElectedMember of the Centre of Excellence DENOTHE (Faculty of Medicine, University of Florence, Italy)
25-28/03/2006Elected Main organiser of the “EMBO-FEBS workshop on amyloid formation” (Florence, Italy, 25-28 March 2006)
21-25/07/2007Elected as one of the two Meeting Chairs of the 21^st Annual Symposium of the Protein Society (Boston, Massachusetts, July 21-25, 2007)
Year 2006Elected member of the Editorial Board of The Open Structural Biology Journal
23-26/09/2008Elected a one of the four main organisers of the 53th Congress of the Italian Society of Biochemistry (Riccione, Italy, 23-26 September 2008)
Year 2008Elected member of the Italian Scholarship Advisory Committee of the Giovanni Armenise-Harvard Foundation for years 2008-2010
24/06/2010 “Roncaglia-Mari” Award for the year 2010 as a main contributor in Science (the Award was presented by the Accademia Nazionale dei Lincei in the presence of the President of the Italian Republic Giorgio Napolitano)

Recent Lectures at International Meetings (years 2002-2013)

15-20 June 2002, Snowmass, Colorado. Amyloids & other abnormal protein folding processes. Invited Lecture
3-5 October 2002, Verona, Italy. Horizon Symposium on "Protein Folding and Disease" organised by the Nature Publishing Group and Aventis. Invited Lecture.
27-29 November 2002, Saitama, Japan. First international workshop "Frontiers in Molecular Neuropathology", Invited Lecture.
29 march - 2 April 2003, Firenze, Italy. Fifth European Symposium of the Protein Society. Invited Lecture.
3-5 April 2003. Roma, Italy. International congress on Protein Folding and Misfolding. Invited Lecture.
5-16 May 2003. Trieste, Italy. International Workshop on Proteomics: Protein Structure, Function and Interactions. Invited Lecture.
9-12 September 2003. Lyon, France. CECAM workshop on Protein Folding: bringing theory and experiment closer together. InvitedLecture.
17-22 October 2003. Fondation des Treilles, France. Conference on "Disorders of Protein Folding". Invited Lecture.
27 October 2003. Strasbourg, France. Jean-Francois LeFèvre Lecture at the Ecole Supérieure de Biotechnologie de Strasbourg (ESBS). Invited Lecture.
9-11 February 2004. Boston, USA. Second ICAM workshop on physical principles of amyloid diseases. Invited Lecture.
18-22 April 2004. Tours, France. Xth International Symposium on Amyloid and Amyloidosis. Invited Lecture.
13-15 May 2004. Bedlewo, Poland. Workshop on Structure and Function of Biomolecules. Invited Lecture.
4-8 July 2004. Urbino, Italy. European School of Medicinal Chemistry. Invited Lecture.
14-16 October 2004. Berlin, Germany. Formation and Stability of b-sheets. Invited Lecture.
9-13 December 2004. Pavia, Italy. International Workshop on Dialysis related amyloidosis: from molecular mechanisms to therapies. Invited Lecture.
17-20 May 2005. Aalborg, Denmark. PhD course on protein aggregation and fibrillation. Invited Lecture.
28 May - 2 June 2005. Zakopane, Italy. EMBO–FEBS Workshop on Biology of Molecular Chaperones. Invited Lecture
18-23 June 2005. San Diego, California. 19^th American peptide Symposium. Invited Lecture.
16-20 July 2005.Lausanne, Switzerland. The First International ICAM Workshop on Protein Aggregation and Amyloid Formation in Systemic and Neurodegenerative Diseases. Invited Lecture.
23-30 August 2005. Firenze, Italy. XX Congress of the International Union of Crystallography. Invited Lecture.
4-8 October 2005.Rimini, Italy. First European Conference on Chemistry for Life Sciences. Invited Lecture.
2006. Henry Stewart Talks Series, Protein Folding, Aggregation and Design. Invited Audio-visual presentation.
25-28 March 2006. Firenze, Italy. EMBO-FEBS Workshop on Amyloid Formation. Invited Lecture and Main Organiser
3-6 May 2006. Vienna, Austria. EMBO YIP Meeting. Standard Short Presentation.
22-25 May 2006. Lyon, France. CECAM Workshop on Protein Aggregation. Invited Lecture.
10-15 June 2006. Snowmass Village, Colorado. FASEB Summer Research Conference: Amyloid fibril formation, protein misfolding & Disease. Chemistry, Physiology and disease. Invited Lecture.
19-22 September 2006. Lyon, France. CECAM Workshop on Protein Folding and misfolding: bringing theory to experiment and viceversa. Invited Lecture.
17-24 September 2006. Heidelberg, Germany. EMBO YIP PhD COURSE. Invited Lecture.
12-15 April 2007. Roscoff, France. Jaques-Monod Conference. Invited Lecture.
19-21 May 2007. Milan, Italy. 3^rd meeting on the Molecular mechanisms of neurodegeneration. Invited Lecture.
9-14 June 2007. Tomar, Portugal. EMBO-FEBS Workshop on Chaperones in Normal and Aberrant Protein Folding, Aging and Cancer. Invited Lecture.
7-12 July 2007. Vienna, Austria. 32^nd Annual FEBS Congress, Molecular Machines. Invited Lecture.
26-29 September 2007. Riva del Garda, Italy. 9^th Annual Congress of the FISV. Invited Lecture.
10 December 2007. Zurich, Switzerland. Encounter on protein aggregation at ETH. Invited Lecture
18-20 June 2008. Heidelberg, Germany. EMBO YIP Meeting. Standard Short Presentation.
14-15 September 2008. Cologne, Germany. Klenk Symposium on Protein misfolding and disease. Invited Lecture.
8-11 February 2009. Halle, Germany. Structure of amyloid fibrils and mechanisms of amyloid formation. Invited Lecture
23-28 May 2009. Dubrovnik, Croatia. The biology of molecular chaperones. Invited Lecture.
28 June-28 July 2009. Snowmass Village, Colorado, USA. FASEB SRC Amyloid Fibril Formation and Protein Misfolding: Molecular Mechanisms and Cellular Effects. Invited Lecture.
8-9 April 2010. Cambridge, UK. From Neuroscience to Nanoscience. Invited Lecture
18-21 April 2010. Rome, Italy. The XII International Symposium on Amyloidosis. Invited Lecture.
4-8 May 2010. Cold Spring Harbor Laboratory. New York. Molecular Chaperones and Stress Responses. Selected Abstract.
27-30 August 2010. Warsaw, Poland. Proteins: structures, folding and interactions. Invited Lecture.
3 September 2010. Liège, Belgium. Protein folding and stability. Invited Lecture.
15-17 November 2010. Julich, Germany. Expanding the frontiers of biomolecular sciences. Invited Lecture.
24-28 January 2011. Venice, Italy. Protein Stability and pathways of self-assembly. Invited Lecture.
19-24 May 2011. Grundlsee, Austria. The biology of molecular chaperones. Invited Lecture.
23-25 June 2011. Parma, Italy. 6th CLU workshop. Selected abstract.
16-21 July 2011. Paris, France. Alzheimer’s Association International Conference. Selected abstract.
11-16 September 2011, Lecce, Italy. XXIV Congresso Nazionale della Società Italiana di Chimica. Invited Lecture.
22 September 2011, Milan, Italy, 2nd CONVEGNO NAZIONALE ARiSLA, Invited Lecture.
16-18 February 2012 Bressanone, Italy, Physics Of Protein Folding And Aggregation. Invited Lecture.
10-14 June 2012, Monte Verità, Switzerland, International Conference on Molecular Crowding 2012. Invited Lecture
16-20 July 2012, Dresden, Germany, The Emerging Dynamic View of proteins: proteins plasticity in Allostery, Evolution, and Self-Assembly, Invited Lecture
24 October 2012, Milan, Italy. 3° Convegno Nazionale ARiSLA. Invited Lecture
28-30 November 2012, Wollongong, Australia, Proteostasis and Disease Symposium. Invited Lecture
18-20 September 2013, Ferrara, Italy. 57th meeting of the Italian Society of Biochemistry and Molecular Biology. Invited Lecture
4-5 November 2013, Cambridge, UK, 1st Annual meeting of the Centre for Misfolding Diseases. Invited Lecture

Teaching

Academic years from 2002-2003 to 2007-2008. Ca. 80 hours of teaching per year (10 CFU/year), Course of Biochemistry, Faculty of Medicine, Univ. di Firenze. Ca. 340 hours of exams and tutorials.
Academic years 2008-2009 and 2009-2010. Ca. 16 hours of teaching per year (2 CFU/year), Course of Structure and function of proteins, Faculty of Medicine, Univ. di Firenze. Ca. 5 hours of exams.
Academic years 2008-2009 and 2009-2010. Ca. 20 hours of teaching per year (2 CFU/year), Course of Chemistry, Faculty of Medicine, Univ. di Firenze. Ca. 15 hours of exams.
Academic years 2009-2010 and 2010-2011. Ca. 16 hours of teaching per year (2 CFU/year), Course of Cellular Biochemistry, Faculty of Medicine, Univ. di Firenze. Ca. 20 hours of exams.
Year 2010-2011 and 2011-2012, Ca. 40 hours of teaching per year (4 CFU/year), Course of Chemistry, Faculty of Medicine, Univ. di Firenze. Ca. 200 hours of exams and tutorials per year.
Academic years 2011-2012. Ca. 24 hours of teaching per year (3 CFU/year), Course of protein homeostasis and associated diseases, Faculty of Medicine, Univ. di Firenze. Ca. 4 hours of exams.
Over 20 Invited seminars at Italian and Foreign Universities and Research Institutes.
Ca. 18 Invited Lectures at National Meetings

Invited Reviews and Book Chapters

Chiti F and Dobson CM (2006). Invited review titled “Protein misfolding, functional amyloid, and human disease”. Ann. Rev. Biochem. 75, 333-366.
Chiti F (2006). Chapter titled “The influence of hydrophobicity, secondary structure propensity and charge in protein aggregation” for the book Protein Misfolding, Aggregation, and Conformational Diseases. Vladimir N. Uversky and Anthony L. Fink Editors, Kluwer Academic / Plenum Publishers, pp. 43-59
Plakoutsi G, Marcon G and Chiti F (2006). Chapter titled “Investigation of amyloid formation by globular proteins under conditions in which they are in their native state”. In “Amyloid, Prions and other Protein Aggregates” Methods in Enzymology 413, 75-91.
Bemporad F, Calloni G, Campioni S, Plakoutsi G, Taddei N and Chiti F (2006). Invited review titled “Sequence and Structural Determinants of amyloid fibril formation” Accounts of Chemical Research 39, 620-627.
Monsellier E and Chiti F (2007). Invited review titled “Prevention of amyloid-like aggregation as a driving force of protein evolution”. EMBO Reports 8, 737-742.
Bellotti V and Chiti F (2008). Invited review titled “Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseases” Curr. Op. Struct. Biol. 18, 771-779.
Chiti F and Dobson CM (2009). Invited review titled “Amyloid formation by globular proteins under native conditions”. Nature Chem. Biol. 5, 15-22.
Bemporad F and Chiti F (2009). “Native-like aggregation” of the acylphosphatase from Sulfolobus solfataricus and its biological implications. FEBS Lett. 583, 2630-2638.
Campioni S, Monsellier E and Chiti F (2010). Chapter titled “Why proteins misfold?” for the book “Protein Misfolding Diseases: Current and Emerging Principles and Therapies” Marina Ramirez-Alvarado, Chris Dobson, Jeff Kelly editors, John Wiley and Sons, pp 3-20.
Belli M, Ramazzotti M, Chiti F. (2011). Prediction of amyloid aggregation in vivo. EMBO Rep. 12, 657-663.
Bemporad F, Chiti F (2012). Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships.Chem. Biol. 19, 315-327.
Bemporad F, Chiti F (2012). Chapter titled “Pathways of amyloid formation” for the book “Amyloid Fibrils and Prefibrillar Aggregates: Molecular and Biological Properties” Daniel Otzen editor, Wiley-VCH, pp. 151-166.

Publications of original articles (excluding reviews)

Modesti A., Taddei N., Chiti F., Bucciantini M., Magherini F., Rigacci S., Stefani M., Raugei G. and Ramponi G. (1996). Properties of Cys21 mutated muscle acylphosphatases. J. Prot. Chem. 15, 27-34.
Taddei N., Magherini F., Chiti F., Bucciantini M., Raugei G., Stefani M. and Ramponi G. (1996). C-terminal region contributes to muscle acylphosphatase three-dimensional structure stabilization. FEBS Lett. 384, 172-176.
Taddei N., Stefani M., Magherini F., Chiti F., Modesti A., Raugei G. and Ramponi G. (1996). Looking for residues involved in muscle acylphosphatase catalytic mechanism and structural stabilization: the role of Asn41, Thr42 and Thr46. Biochemistry, 35, 7077-7083.
Taddei N., Chiti F., Magherini F., Stefani M., Thunnissen M.M.G.M., Nordlund P. and Ramponi G. (1997). Structural and kinetic investigations on the 15-21 and 42-45 loops of muscle acylphosphatase: evidence for their involvement in enzyme catalysis and conformational stabilisation. Biochemistry, 36, 7217-7224.
Chiti F., van Nuland N.A.J., Taddei N., Magherini F., Stefani M., Ramponi G. and Dobson C.M. (1998). Conformational stability of muscle acylphosphatase. The role of temperature, denaturant concentration and pH. Biochemistry, 37, 1447-1455.
Bucciantini M., Stefani M., Taddei N., Chiti F., Rigacci S. and Ramponi G. (1998). Sequence-specific recognition of peptide substrates by the low M-r phosphotyrosine protein phosphatase isoforms. FEBS Lett., 422, 213-217.
Modesti A., Marzocchini R., Raugei G., Chiti F., Sereni A., Magherini F. and Ramponi G. (1998). Cloning, expression and characterization of a new human LMW-PTP isoform originating by alternative splicing. FEBS Lett. 431, 111-115.
Chiti F., Magherini F., Taddei N., Ilardi C., Stefani M., Bucciantini M., Dobson C.M. and Ramponi G. (1998). Studies of enzymatic activity and conformational stability of muscle acylphosphatase mutated at conserved lysine residues. Protein Eng. 11, 557-561.
van Nuland N.A.J., Chiti F., Taddei N., Raugei G., Ramponi G. and Dobson C.M. (1998). Slow folding of muscle acylphosphatase in the absence of intermediates. J. Mol. Biol. 283, 883-891.
Chiti F., Taddei N., van Nuland N.A.J., Magherini F., StefaniM., RamponiG. and DobsonC.M.(1998). Structural characterisation of the transition state for folding of muscle acylphosphatase. J. Mol. Biol. 283, 893-903.
Taddei N., Chiti F., Paoli P. Fiaschi T., Bucciantini M., Stefani M., Dobson C.M. and Ramponi G. (1999). Thermodynamics and kinetics of folding of common-type acylphosphatase: comparison to the highly homologous muscle isoenzyme. Biochemistry 38, 2135-2142.
Paoli P., Taddei N., Fiaschi T., Veggi D., Camici G., Manao G., Raugei G., Chiti F. and Ramponi G. (1999). The contribution of acidic residues to the conformational stability of common-type acylphosphatase. Arch. Biochem. Biophys. 363, 349-355.
Chiti F., Webster M., Taddei N., Clark, A., Stefani M., Ramponi G. and Dobson C.M. (1999). Designing conditions for in vitro formation of amyloid fibrils. Proc. Natl. Acad. Sci. USA 96, 3590-3594.
Chiti F., Taddei N., Webster P., Hamada D., Fiaschi T., Ramponi G. and Dobson C.M. (1999). Acceleration of the folding of acylphosphatase by stabilisation of local secondary structure. Nature Struct. Biol. 6, 380-387.
Chiti F., Taddei N., Giannoni E., van Nuland N.A.J., Ramponi G. and Dobson C.M. (1999). Development of enzymatic activity during protein folding. J. Biol. Chem. 274, 20151-20158.
Chiti F., Taddei N., White P.M., Bucciantini M., Magherini F., Stefani M. and Dobson C.M. (1999). Mutational analysis of acylphosphatase reveals the importance of topology and contact order in protein folding.Nature Struct. Biol. 6, 1005-1009.
Hamada D., Chiti F., Guijarro J.I., Kataoka M., Taddei N. and Dobson C.M. (2000). Evidence concerning rate-limiting steps in protein folding from the effects of trifluoroethanol. Nature Struct. Biol. 7, 58-61.
Chiti F., Taddei N., Bucciantini M., White P., Ramponi G. and Dobson C.M. (2000). Mutational analysis of the propensity for amyloid formation by a globular protein. EMBO J. 19, 1441-1449.
Verzola B., Chiti F., Manao G. and Righetti P.G. (2000). Monitoring equilibria and kinetics of protein folding/unfolding reactions by capillary zone electrophoresis. Anal. Biochem. 282, 239-244.
Taddei N., Chiti F., Fiaschi T., Bucciantini M., Capanni C., Stefani M., Serrano L., Dobson C.M. and Ramponi G. (2000). Stabilisation of alpha-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatase folding. J. Mol. Biol. 300, 633-647.
Pertinhez T.A., Hamada D., Smith L.J., Chiti F., Taddei N., Stefani M. and Dobson C.M. (2000). Initial denaturing conditions influence the slow folding phase of acylphosphatase associated with proline isomerization. Protein Sci. 9, 1466-1473.
Chiti F., Mangione P., Andreola A., Giorgetti S., Stefani M., Dobson C.M., Bellotti V. and Taddei N. (2001). Detection of two partially structured species in the folding process of the amyloidogenic protein b2-microglobulin. J. Mol. Biol. 307, 379-391.
Chiti F., Taddei N., Stefani M., Dobson C.M. and Ramponi G. (2001). Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation. Protein Sci. 10, 879-886.
Taddei N., Capanni C., Chiti F., Stefani M., Dobson C.M. and Ramponi G. (2001). Folding and aggregation are selectively influenced by the conformational preferences of the a-helices of muscle acylphosphatase. J. Biol. Chem., 276, 37149-37154.
Chiti F., De Lorenzi E., Grossi S., Mangione P., Giorgetti S., Caccialanza G., Dobson C.M., Merlini G., Ramponi G. and Bellotti V. (2001). A partially structured species of b2-microglobulin is significantly populated under physiological conditions and involved in fibrillogenesis. J. Biol. Chem. 276, 46714-46721.
Chiti F., Bucciantini M., Capanni C., Taddei N., Dobson C.M. and Stefani M. (2001). Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain. Protein Sci. 10, 2541-2547.
Millet I.S., Townsley L.E., Chiti F., Doniach S. and Plaxco K.W. (2002). Equilibrium collapse and the kinetic 'foldability' of proteins. Biochemistry 41, 321-325.
Chiti F., Taddei N., Baroni F., Capanni C., Stefani M., Ramponi G. and Dobson C.M. (2002). Kinetic partitioning of protein folding and aggregation. Nature Struct. Biol. 9, 137-143.
De Lorenzi E., Grossi S., Massolini G., Giorgetti S., Mangione P., Andreola A., Chiti F., Bellotti V. and Caccialanza G. (2002). Capillary electrophoresis investigation of a partially unfolded conformation of b2-microglobulin. Electrophoresis 23, 918-925.
Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., Zurdo J., Taddei N., Ramponi G., Dobson C.M. and Stefani M. (2002). Inherent toxicity of aggregates implies a common origin for protein misfolding diseases. Nature 416, 507-511.*
Chiti F, Calamai M, Taddei N, Stefani M, Ramponi G, Dobson CM. (2002). Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases. Proc. Natl. Acad. Sci. USA 99, 16419-16426.
Degl'Innocenti D, Ramazzotti M, Marzocchini R, Chiti F, Raugei G, Ramponi G. (2003). Characterization of a novel Drosophila melanogaster acylphosphatase. FEBS Lett. 30, 171-174.
Esposito G, Garcia J, Mangione P, Giorgetti S, Corazza A, Viglino P, Chiti F, Andreola A, Dumy P, Booth D, Hawkins PN, Bellotti V. (2003). Structural and folding dynamics properties of T70N variant of human lysozyme. J. Biol. Chem. 278, 25910-25918
Calloni G, Taddei N, Plaxco KW, Ramponi G, Stefani M, Chiti F (2003). Comparison of the folding processes of distantly related proteins. Importance of hydrophobic content in folding. J. Mol. Biol. 330, 577-591.
Chiti F, Stefani M, Taddei N, Ramponi G, Dobson CM. (2003). Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424, 805-808.
Polverino de Laureto P, Taddei N, Frare E, Capanni C, Costantini S, Zurdo J, Chiti F, Dobson CM, Fontana A. (2003). Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis. J. Mol. Biol. 334, 129-141.
Calamai M, Taddei N, Stefani M, Ramponi G, Chiti F (2003). Relative Influence of Hydrophobicity and Net Charge in the Aggregation of two Homologous Proteins. Biochemistry 42, 15078-15083.
Degl’Innocenti D, Taddei N, Ramazzotti M, Stefani M, Chiti F and Ramponi G. Selection of antibody fragments specific for an a-helix region of acylphosphatase. (2004). J. Mol. Recognit. 17, 62-66.
Monti M., Lelj Garolla Di Bard B, Calloni G, Chiti F, Amoresano A, Ramponi G and Pucci P. (2004). The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process. J. Mol. Biol. 336, 253-262.
Plakoutsi G, Stefani M, Taddei N and Chiti F. (2004). Aggregation of the acylphosphatase from S. solfataricus. The folded and partially unfolded states can be both precursors for amyloid formation. J. Biol. Chem. 279, 14111-14119.
CapanniC, Taddei N, Gabrielli S, Messori L, OrioliP, ChitiF, Stefani M and Ramponi G (2004). Investigation of the effects of copper ions on protein aggregation using a model system. Cell. Mol. Life. Sci. 61, 982-991.
ReliniA, CanaleC, TorrassaS, RolandiR, Gliozzi A, Rosano C, Bolognesi M, Plakoutsi G, Bucciantini M, Chiti F and Stefani M. (2004). Monitoring the process of HypF-N fibrillization and liposome permeabilization by fibril precursors. J. Mol. Biol. 338, 943-957.
Ventura S, Zurdo J, Narayanan S, Parreño M. Mangues R, Reif B, Chiti F, Giannoni E, Dobson CM, Aviles FX. and Serrano L. (2004). Short amino acid stretches play an important role in protein amyloid formation. The SH3 case. Proc. Natl. Acad. Sci. USA, 101, 7258-63.
Bucciantini M, Calloni G, Chiti F, Formigli L, Nosi D, Dobson CM and Stefani M. (2004). Pre-fibrillar amyloid protein aggregates share common features of cytotoxicity. J. Biol. Chem. 279, 31374-31382.
Bemporad F, Capanni C, Calamai M, Tutino ML, Stefani M and Chiti F. (2004). Studying the folding process of the acylphosphatase from S. solfataricus. A comparative analysis with other proteins from the same superfamily. Biochemistry 43, 9116-9126.
DuBay KF, Pawar AP, Chiti F, Zurdo J, Dobson CM and Vendruscolo M. (2004). Predicting Absolute Aggregation Rates of amyloidogenic polypeptide chains. J. Mol. Biol. 341, 1317-1326.
Bucciantini M, Rigacci S, Berti A, Pieri L, Cecchi C, Nosi D, Formigli L, Chiti F and Stefani M (2005). Patterns of cell death triggered in two different cell lines by HypF-N pre-fibrillar aggregates. FASEB J. 19, 437-439
Calloni G, Zoffoli S, Stefani M, Dobson CM, Chiti F. (2005). Investigating the effects of mutations on protein aggregation in the cell. J. Biol. Chem. 280, 10607-10613.
Maxwell KL., Wildes D, Zarrine-Afsar A, de los Rios MA, Brown AG, Friel CT, Hedberg L, Horng J-C, Bona D, Miller EJ, Valle-Blisle A, Main ERG, Bemporad F, Qiu L, Teilum K, Vu N-D, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai Y, Hagen SJ, Serrano L, Oliveberg M, Raleigh DP, Wittung-Stafshede P, Radford SE, Jackson SE, Sosnick TR, Marqusee S, Davidson AR and Plaxco KW (2005). Protein folding: defining a standard set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602-616.
Calamai M, Canale C, Relini A, Stefani M, Chiti F and Dobson CM (2005). Reversal of Protein Aggregation Provides Evidence for Multiple Aggregated States. J. Mol. Biol. 346, 603-616.
Marcon G, Plakoutsi G, Canale C, Relini A., Taddei N., Dobson CM, Ramponi G and Chiti F (2005). Amyloid formation from HypF-N under conditions in which the protein is initially in its native state. J. Mol. Biol. 347, 323-35.
Pawar AP, DuBay KF, Zurdo J, Chiti F, Vendruscolo M and Dobson CM (2005). Prediction of “aggregation-prone” and “aggregation-susceptible” regions in proteins associated with neurodegenerative diseases. J. Mol. Biol. 350, 379-392.
Fowler SB, Poon S, Muff R, Chiti F, Dobson CM, Zurdo J. (2005). Rational design of aggregation-resistant bioactive peptides: reengineering human calcitonin. Proc. Natl. Acad. Sci. USA 102, 10105-10110.
Plakoutsi G, Bemporad F, Calamai M, Taddei N, Dobson CM, Chiti F. (2005). Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates. J. Mol. Biol. 351, 910-922.
Parrini C, Taddei N, Ramazzotti M, Degl'Innocenti D, Ramponi G, Dobson CM, Chiti F. (2005). Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregation. Structure 13, 1143-1151.
Calamai M, Chiti F, Dobson CM. (2005). Amyloid Fibril Formation can Proceed from Different Conformations of a Partially Unfolded Protein. Biophys. J. 89, 4201-4210
Soldi G, Bemporad F, Torrassa S, Relini A, Ramazzotti M, Taddei N, Chiti F (2005). Amyloid formation of a protein in the absence of unfolding and destabilisation of the native state. Biophys. J. 89, 4234-4244.
Corazza A, Rosano C, Pagano K, Alverdi V, Esposito G, Capanni C, Bemporad F, Plakoutsi G, Stefani M, Chiti F, Zuccotti S, Bolognesi M, Viglino P. (2006). Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus. Proteins 62, 64-79.
Bemporad F, Taddei N, Stefani M, Chiti F (2006). Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase. Protein Sci. 15, 862-870.
Plakoutsi G, Bemporad F, Monti M, Pagnozzi D, Pucci P, Chiti F. (2006). Exploring the mechanism of formation of native-like and precursor amyloid oligomers for the native acylphosphatase from Sulfolobus solfataricus. Structure 14, 993-1001.
Baglioni S, Casamenti F, Bucciantini M, Luheshi LM, Taddei N, Chiti F, Dobson CM, Stefani M. (2006). Prefibrillar amyloid aggregates could be generic toxins in higher organisms. J. Neurosci. 26, 8160-8167.
Soldi G, Plakoutsi G, Taddei N, Chiti F (2006). Stabilization of a native protein mediated by ligand binding inhibits amyloid formation independently of the aggregation pathway. J. Med. Chem. 49, 6057-6064.
Calamai M, Kumita JR, Mifsud J, Parrini C, Ramazzotti M, Ramponi G, Taddei N, Chiti F, Dobson CM. (2006). Nature and Significance of the Interactions between Amyloid Fibrils and Biological Polyelectrolytes. Biochemistry 45, 12806-12815.
Trovato A, Chiti F, Maritan A, Seno F. (2006). Insight into the Structure of Amyloid Fibrils from the Analysis of Globular Proteins. PLoS Comput. Biol. 2, e170.
Picotti P, De Franceschi G, Frare E, Spolaore B, Zambonin M, Chiti F, de Laureto PP, Fontana A. (2007). J. Mol. Biol. 367, 1237-45.
Monsellier E, Ramazzotti M, de Laureto PP, Tartaglia GG, Taddei N, Fontana A, Vendruscolo M, Chiti F. (2007). The distribution of residues in a polypeptide sequence is a determinant of aggregation optimized by evolution. Biophys J. 93, 4382-4891.
Luheshi LM, Tartaglia GG, Brorsson AC, Pawar AP, Watson IA, Vendruscolo M, Lomas DA, Dobson CM, Crowther DC (2007). Systematic in vivo Analysis of the Intrinsic Determinants of Amyloid b Pathogenicity. PloS Biol. 5, e290.
Soldi G, Bemporad F, Chiti F (2008). The Degree of Structural Protection at the Edge ‚-Strands Determines the Pathway of Amyloid Formation in Globular Proteins. J. Am. Chem. Soc. 130, 4295-302.
Bemporad F, Gsponer J, Hopeharuoho HI, Plakoutsi G, Stati G, Stefani M, Taddei N, Vendruscolo M, Chiti F (2008). Biological function in a non-native partially folded state of a protein. EMBO J. 27, 1525-1535.
Campioni S, Mossuto MF, Torrassa S, Calloni G, de Laureto PP, Relini A, Fontana A, Chiti F. (2008). Conformational properties of the aggregation precursor state of HypF-N. J. Mol. Biol. 379, 554-567.
Parrini C, Bemporad F, Baroncelli A, Gianni S, Travaglini-Allocatelli C, Kohn JE, Ramazzotti M, Chiti F, Taddei N. (2008). The folding process of acylphosphatase from Escherichia coli is remarkably accelerated by the presence of a disulfide bond. J. Mol. Biol. 379, 1107-1118.
Tartaglia GG, Pawar AP, Campioni S, Dobson CM, Chiti F, Vendruscolo M (2008). Prediction of Aggregation-Prone Regions in Structured Proteins. J. Mol. Biol. 380, 425-436.
Calloni G, Lendel C, Campioni S, Giannini S, Gliozzi A, Relini A, Vendruscolo M, Dobson CM, Salvatella X, Chiti F. (2008). Structure and dynamics of a partially folded protein are decoupled from its mechanism of aggregation.J. Am. Chem. Soc. 130, 13040-13050.
Monsellier E., Ramazzotti M., Taddei N., Chiti F. (2008). PLoS Comput. Biol. 4, e1000199.
Bemporad F, Vannocci T, Varela L, Azuaga AI, Chiti F (2008). A model for the aggregation of the acylphosphatase from Sulfolobus solfataricus in its native-like state. Biochim. Biophys. Acta 1784, 1986-1996.
Sicorello A, Torrassa S, Soldi G, Gianni S, Travaglini-Allocatelli C, Taddei N, Relini A, Chiti F. (2009). Agitation and high ionic strength induce amyloidogenesis of a folded PDZ domain in native conditions.Biophys J. 96, 2289-2298.
Calamai M, Tartaglia GG, Vendruscolo M, Chiti F, Dobson CM. (2009). Mutational Analysis of the Aggregation-Prone and Disaggregation-Prone Regions of Acylphosphatase.J. Mol. Biol. 387, 965-974.
Motamedi-Shad N, Monsellier E, Chiti F (2009). Amyloid Formation by the Model Protein Muscle Acylphosphatase is Accelerated by Heparin and Heparan Sulfate Through a Scaffolding-Based Mechanism.J. Biochem. 146, 805-814.
Motamedi-Shad N, Monsellier E, Torrassa S, Relini A, Chiti F. (2009). Kinetic analysis of amyloid formation in the presence of heparan sulfate. Faster unfolding and change of pathway.J. Biol. Chem. 284, 29921-29934.
Ahmad B, Winkelmann J, Tiribilli B, Chiti F (2009). Searching for conditions to form stable protein oligomers with amyloid-like characteristics: the unexplored basic pH. Biochim. Biophys. Acta 1804, 223-234.
Campioni S, Mannini B, ZampagniM, Pensalfini A, ParriniC, EvangelistiE, ReliniA, StefaniM, DobsonCM, CecchiC, ChitiF. (2010). A causative link between the structure of aberrant protein oligomers and their toxicity. Nature Chem. Biol. 6, 140-147.
Relini A, Torrassa S, Ferrando R, Rolandi R, Campioni S, Chiti F, Gliozzi A. (2010). Detection of populations of amyloid-like protofibrils with different physical properties. Biophys. J. 98, 1277-1284.
Brorsson AC, Bolognesi B, Tartaglia GG, Shammas SL, Favrin G, Watson I, Lomas DA, Chiti F, Vendruscolo M, Dobson CM, Crowther DC, Luheshi LM. (2010). Intrinsic determinants of neurotoxic aggregate formation by the amyloid beta peptide. Biophys. J. 98, 1677-1684.
Pagano K, Bemporad F, Fogolari F, Esposito G, Viglino P, Chiti F, Corazza A. (2010). Structural and dynamics characteristics of Acylphosphatase from Sulfolobus solfataricus in the monomeric state and in the initial native-like aggregates.J. Biol. Chem. 285, 14689-14700.
Winkelmann J, Calloni G, Campioni S, Mannini B, Taddei N, Chiti F. (2010). Low-Level Expression of a Folding-Incompetent Protein in Escherichia coli: Search for the Molecular Determinants of Protein Aggregation In Vivo. J. Mol. Biol. 398, 600-613.
Monsellier E, Ramazzotti M, Taddei N, Chiti F. (2010). A computational approach for identifying the chemical factors involved in the glycosaminoglycans-mediated acceleration of amyloid fibril formation.PLoS One 5, e11363.
Ramshini H, Parrini C, Relini A, Zampagni M, Mannini B, Pesce A, Saboury AA, Nemat-Gorgani M, Chiti F. (2011). Large proteins have a great tendency to aggregate but a low propensity to form amyloid fibrils.PLoS One 6, e16075.
Zampagni M, Cascella R, Casamenti F, Grossi C, Evangelisti E, Wright D, Becatti M, Liguri G, Mannini B, Campioni S, Chiti F, Cecchi C. (2011). A comparison of the biochemical modifications caused by toxic and nontoxic protein oligomers in cells.J Cell Mol Med. 15, 2106-2116.
Ahmad B, Vigliotta I, Tatini F, Campioni S, Mannini B, Winkelmann J, Tiribilli B, Chiti F. (2011). The induction of α-helical structure in partially unfolded HypF-N does not affect its aggregation propensity. Protein Eng Des Sel. 24, 553-563.
De Simone A, Dhulesia A, Soldi G, Vendruscolo M, Hsu STD, Chiti F, Dobson CM (2011). Experimental Energy Surfaces Reveal theMechanisms of Maintenance of Protein Solubility. Proc. Natl. Acad. Sci. USA, 108, 21057-21062.
Fusco G, De Simone A, Hsu ST, Bemporad F, Vendruscolo M, Chiti F, Dobson CM (2012). ¹H, ¹³C and ¹⁵N resonance assignments of human muscle acylphosphatase. Biomol NMR Assign. 6, 27-29.
Saridaki T, Zampagni M, Mannini B, Evangelisti E, Taddei N, Cecchi C, Chiti F (2012). Glycosaminoglycans (GAGs) Suppress the Toxicity of HypF-N Prefibrillar Aggregates.J. Mol. Biol. 421, 616-630.
Evangelisti E, Cecchi C, Cascella R, Sgromo C, Becatti M, Dobson CM, Chiti F, Stefani M (2012). Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomers. J. Cell. Sci. 125, 2416-2427.
Motamedi-Shad N, Garfagnini T, Penco A, Relini A, Fogolari F, Corazza A, Esposito G, Bemporad F, Chiti F (2012) Rapid oligomer formation of human muscle acylphosphatase induced by heparan sulfate. Nature Struct. Mol. Biol. 19, 547-554.
Bemporad F, De Simone A, Chiti F, Dobson CM. (2012). Characterizing intermolecular interactions that initiate native-like protein aggregation.Biophys. J. 102, 2595-2604.
Mannini B, Cascella R, ZampagniR, van Waarde-VerhagenMAWH, MeehanS, RoodveldtC, CampioniS, BoninsegnaM, PencoA, ReliniA, Kampinga HH, Dobson CM, WilsonMR, CecchiC, Chiti F (2012). Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers. Proc. Natl. Acad. Sci. USA 109, 12479-12484.
Campioni S, Mannini B, López-Alonso JP, Shalova IN, Penco A, Mulvihill E, Laurents DV, Relini A, Chiti F (2012). Salt Anions Promote the Conversion of HypF-N into Amyloid-Like Oligomers and Modulate the Structure of the Oligomers and the Monomeric Precursor State. J. Mol. Biol. 424, 132-149.
Castillo V, Chiti F, Ventura S (2013). The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain.PLoS One 8, e58297.
Tatini F, Pugliese AM, Traini C, Niccoli S, Maraula G, Ed Dami T, Mannini B, Scartabelli T, Pedata F, Casamenti F, Chiti F (2013). Amyloid-β oligomer synaptotoxicity is mimicked by oligomers of the model protein HypF-N.Neurobiol Aging 34, 2100-2109.
Cascella R, Conti S, Tatini F, Evangelisti E, Scartabelli T, Casamenti F, Wilson MR, Chiti F, Cecchi C. (2013). Extracellular chaperones prevent Aβ42-induced toxicity in rat brains.Biochim Biophys Acta 1832, 1217-1226.
Mangione PP, Esposito G, Relini A, Raimondi S, Porcari R, Giorgetti S, Corazza A, Fogolari F, Penco A, Goto Y, Lee YH, Yagi H, Cecconi C, Naqvi MM, Gillmore JD, Hawkins PN, Chiti F, Rolandi R, Taylor GW, Pepys MB, Stoppini M, Bellotti V (2013). structure, folding dynamics, and amyloidogenesis of D76N β2-microglobulin: roles of shear flow, hydrophobic surfaces, and α-crystallin.J. Biol. Chem. 288, 30917-30930.
Monsef Shokri M, Ahmadian S, Bemporad F, Khajeh K, Chiti F (2013). Amyloid fibril formation by a normally folded protein in the absence of denaturants and agitation.Amyloid 20, 226-232.
Cascella R, Conti S, Mannini B, Li X, Buxbaum JN, Tiribilli B, Chiti F, Cecchi C (2013) Transthyretin suppresses the toxicity of oligomers formed by misfolded proteins in vitro.Biochim Biophys Acta 1832, 2302-2314.
Capitini C, Conti S, Perni M, Guidi F, Cascella R, De Poli A, Penco A, Relini A, Cecchi C, Chiti F (2014). TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells.PLoS One. 9, e86720.

Fabrizio CHITI

Interest

Study, at a molecular level, of the process by which native proteins convert into partially folded states necessary to initiate aggregation
Study, in molecular depth, of the conversion of partially folded states of proteins into amyloid fibrils and their precursor oligomers
Study of the relationship between structure and toxicity of protein oligomers
Investigation of molecular chaperones as inhibitors of the toxicity of protein oligomers
Investigation of small molecules as inhibitors on the formation and toxicity of protein oligomers
Study, at a molecular level, of the process of native-like aggregation, involving directly the folded state of a protein
Study of the effect of agents of the extracellular matrix, such as glycosamynoglycans, on the formation of amyloid fibrils, precursor oligomers and their toxicity
Editing of mathematical algorithms able to predict fundamental aspects of protein aggregation in vitro and in vivo
Elucidation of protein oligomers on neuronal function of primary neurons and rat brains