RICERCA ITALIANA     

Programmi di ricerca simili:

• 1 - Aspetti molecolari di patologie conformazionali proteiche. Ruolo dei fattori ambientali sulle variazioni strutturali di proteine per la progettazione e la sintesi di agenti ad attività antiaggregante, antiossidante, antiglicante e chelante nonchè per applicazioni in diagnostica.
• 2 - PARTNERS DI INTERAZIONE DI PROTEINE AMILOIDOGENICHE PER LO STUDIO DEI PROCESSI DI MISFOLDING ED AGGREGAZIONE; POSSIBILI APPLICAZIONI
• 3 - APPROCCIO TEORICO-SPERIMENTALE AGLI STATI NON-NATIVI DELLE PROTEINE: FORMAZIONE DI FIBRILLE AMILOIDI, PROTEINE DISORDINATE E DENATURATE
• 4 - Ruolo dell'interazione dei metalli con il sistema Ubiquitina/Proteasoma nella patogenesi delle malattie conformazionali
• 5 - Individuazione di determinanti di folding e misfolding mediante mutagenesi sistematica
• 6 - Amiloidi e ripiegamento di proteine: un approccio teorico-sperimentale
• 7 - Processi chimici e modificazioni strutturali nella neurodegenerazione
• 8 - Misfolding di proteine e formazione di amiloide: studi sulle basi molecolari della comparsa e aggregazione di conformeri tossici e sulla interazione di questi con superfici sintetiche e con bersagli cellulari e tessutali
• 9 - Interattomi proteici: identificazione e caratterizzazione di network cellulari in differenti condizioni fisiopatologiche
• 10 - Un approccio multidisciplinare allo studio dell'aggregazione in vivo e in vitro di proteine contenenti tratti di poliglutammina. Ruolo dei fattori molecolari ed ambientali.

Classificazione scientifico-disciplinare

• Area scientifico disciplinare: Scienze biologiche
  • BIOCHIMICA

Classificazione brevettuale

• CHEMISTRY; METALLURGY
  • ORGANIC CHEMISTRY (such compounds as the oxides, sulfides, or oxysulfides of carbon, cyanogen, phosgene, hydrocyanic acid or salts thereof C01; products obtained from layered base-exchange silicates by ion-exchange with organic compounds such as ammonium, phosphonium or sulfonium compounds or by intercalation of organic compounds C01B33/44; macromolecular compounds C08; dyes C09; fermentation products C12; fermentation or enzyme-using processes to synthesise a desired chemical compound or composition or to separate optical isomers from a racemic mixture C12P; production of organic compounds by electrolysis or electrophoresis C25B3/00, C25B7/00)
    • PEPTIDES (peptides in foodstuffs A23; obtaining protein compositions for foodstuffs, working-up proteins for foodstuffs A23J; preparations for medicinal purposes A61K; peptides containing beta-lactam rings C07D; cyclic dipeptides not having in their molecule any other peptide link than those which form their ring, e.g. piperazine-2,5-diones, C07D; ergot alkaloids of the cyclic peptide type C07D519/02; macromolecular compounds having statistically distributed amino acid units in their molecules, i.e. when the preparation does not provide for a specific; but for a random sequence of the amino acid units, homopolyamides and block copolyamides derived from amino acids C08G69/00; macromolecular products derived from proteins C08H1/00; preparation of glue or gelatine C09H; single cell proteins, enzymes C12N; genetic engineering processes for obtaining peptides C12N15/00; compositions for measuring or testing processes involving enzymes C12Q; investigation or analysis of biological material G01N33/00)

Classificazione geografica

• Regione: Veneto

Bibliografia

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5. Sacchettini, J.C., and Kelly, J.W. (2002) Therapeutic strategies for human amyloid diseases. Nature Rev. Drug Discov. 4, 267–275.

6. Dobson, C. M. (2005). Structural biology: Prying into prions. Nature 435, 747-749.

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10. Making, O.S., and Serpell, L.C. (2005) Structures for amyloid fibrils. FEBS J. 272, 5950-5961.

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22. Fandrich, M., Forge, V., Buder, K., Kitter, M., Dobson, C.M., and Dieckmann, S. (2003) Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments. Proc. Natl. Acad. Sci. USA 100, 15463–15468.

23. Sirangelo, I., Malmo, C., Casillo, M., Mezzogiorno, A., Papa, M., and Irace, G. (2002). Tryptophanyl substitutions in apomyoglobin determine protein aggregation and amyloid-like fibril formation at physiological pH. J. Biol. Chem. 277, 45887–45891.

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34. Kheterpal, I., Williams, A., Murphy, C., Bledsoe, B., and Wetzel, R. (2001). Structural features of the Abeta amyloid fibril elucidated by limited proteolysis. Biochemistry, 2, 11757-11767.

35. Bousset, L., Redeker, V., Decottignies, P., Dubois, S., Le Marechal, P., and Melki, R. (2004) Structural characterization of the fibrillar form of the yeast Saccharonyces cerevisae prion Ure2p. Biochemistry 43, 5052–5032.

36. Miake, H., Mizusawa, H., Iwatsubo, T., and Hasegawa, M. (2002). Biochemical characterization of the core structure of alpha-synuclein filaments. J. Biol. Chem. 277, 19213-19219.

37. Polverino de Laureto, P., Taddei, N., Frare, E., Capanni, C., Costantini, S., Zurdo, J., Chiti, F., Dobson, C.M., and Fontana, A. (2003) Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis. J. Mol. Biol. 334, 129–141.

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42. Bomhoff, G., Sloan, K., McLain, C., Gogol, E.P., and Fisher, M.T. (2006) The effects of flavonoid baicalein and osmolytes on the Mg (2+) accelerated aggregation/fibrillation of carboxymethylated bovine 1SS-alpha-lactalbumin. Arch. Biochem. Biophys. (February 2006).

Parole Chiave

FOLDING DI PROTEINE, AGGREGAZIONE PROTEICA, APOMIOGLOBINA, BIOSPETTROSCOPIA, PROTEOLISI LIMITATA, AMILOIDOSI E MALATTIE PRIONICHE