RICERCA ITALIANA     

Similar FIRB:

• 1 - Protein misfolding and human pathologies: study of the pathologic conversion of globular proteins into fibrillar aggregates and development of drugs to inhibit misfolding and aggregation processes
• 2 - PROTEASES IN NORMAL AND PATHOLOGICAL CELL RESPONSES. IDENTIFICATION OF ENDOGENOUS SUBSTRATES AND INDUCED MOLECULAR MECHANISMS.
• 3 - GENE EXPRESSION AND ACCUMULATION OF AGRICULTURALLY IMPORTANT PROTEINS IN THE PLANT CELL:TRANSCRIPTIONAL AND POST-TRANSCRIPTIONAL MECHANISMS
• 4 - Signalling Proteomics (Signalomics): differential studies by novel strategies and technologies
• 5 - Development of innovative molecules for the treatment of neurodegenerative and neuroinflammatory disease
• 6 - PROTEIN FOLDING AND AGGREGATION: METALS AND BIOMOLECULES IN PROTEIN CONFORMATIONAL DISEASES
• 7 - Studies on interactions protein-copper, protein-protein, protein-nucleic acids and protein-lipids within membrane microdomains. Relevance for "membrane microdomains pathologies" comprehension, such as Prion diseases, Alzheimer disease and lipid-metabolism alterations.
• 8 - Molecular recognition and cell function
• 9 - Mechanisms of signal transduction and synaptic function: Development of molecular, cellular, and animal models.
• 10 - NEURODEGENERATIVE DISEASES AS A RESULT OF AN ALTERED PROCESSING OF NEURONAL PROTEINS. ANIMAL AND IN VITRO CULTURED MODELS.

Scientific and education field classification

• Field: Scienze chimiche
  • CHIMICA GENERALE E INORGANICA
• Field: Scienze biologiche
  • BIOCHIMICA

International Patent Classification

• 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)

Geographical classification

• Region: Veneto

Bibliografia

(1) Möller, C., Allen, M., Elings, V., Engel, A. and Müller, D.J. (1999) Tapping mode atomic force microscopy produces faithful high-resolution images of protein surfaces. Biophys. J. 77, 1050-1058
(2) Müller, D.J., Janovjak, H., Letho, T., Kuerschner, L. and Anderson, K. (2002) Observing structure, function and assembly of single proteins by AFM. Prog. Biophys. Mol. Biol. 79, 1-43.
(3) Carrion-Vasquez, M., Oberhauser, A. F., Fischer, T. E., Marszalek,P. E. Li, H. and Fernandez J. M. (2000) Mechanical design of proteins studied by single-molecule force spectroscopy and protein engineering. Prog. Biophys. Mol. Biol. 74, 63-91.
(4) Palmer, R. E., Pratontep, S. and Boyen, H.-G. (2003) Nanostructured surfaces from size-selected clusters. Nature Mat. 2, 443-448.New
(5) Dalvit, C., Ardini, E., Flocco, M., Fogliatto, G., Mongelli, N. and Veronesi, M. (2003). A general NMR method for rapid, efficient, and reliable biochemical screening. J. Am. Chem. Soc. 125, 14620-14625.
(6) Clote, P. and Backofen, R. (2002) Computational Molecular Biology: An Introduction. Wiley Series in Mathematical and Computational Biology. (John Wiley & Sons, New York).
(7) Friesner, R.A. (ed.) (2002) Computational Methods for Protein Folding, Advances in Chemical Physics, vol. 120 (John Wiley & Sons, New York).
(8) Abkevich, V. I., Gutin A. M. and Shaknovich, E. I. (1994) Free energy landscape for protein folding kinetics: Intermediates, traps, and multiple pathways in theory and lattice models simulations. J. Chem. Phys. 101, 6052-6062.
(9) Broglia , R. A. and Tiana, G. (2004) Lattice model of protein folding and of non-conventional drug design. J. Phys. Condens. Matter 16, R111-R144
(10) Betancourt, M.R. and Thirumalai, D. (1999) Pair potentials for protein folding: Choice of reference states and sensitivity of predicted native states to variations of interaction schemes. Protein Sci. 8, 361-369.
(11) Fogolari , F., Brigo, A. and Molinari, H. (2002) The Poisson-Boltzmann equation for biomolecular electrostatics: a tool for structural biology. J. Mol. Recognit. 15, 377-392.
(12) Akerstrom, B., Flower, D. and Salier , J.P., Lipocalins: Unity in diversity. Review. (2000) Biochim. Biophys. Acta 1482, 1-8.
(13) Urade, U. and Hayaishi, O. (2000). Prostaglandin D synthase: Structure and function. Vitam. Horm. 56, 89-120.
(14) Di Pietro, S.M., Córsico, B., Perduca, M., Monaco, H.L. and Santomè, J.A. (2003).Structural and biochemical characterization of toad liver fatty acid-binding protein. Biochemistry 42, 8192-8203.
(15) Peters, T. Jr. (1996) All about Albumin. Biochemistry, Genetics and Medical Applications. Acad. Press, San Diego.
(16) Sirtori, C.R., Calabresi, L. and Franceschini, G. (1999). Recombinant apolipoproteins for the treatment of vascular diseases. Atherosclerosis 142, 29-40.
(17) Borhani, D.W., Rogers, D.P., Engler, J.A. and Brouillette, C.G. (1997). Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation. Proc. Natl. Acad. Sci. USA 94, 12291-12296.
(18) Narayanaswami, V. and Ryan, R.O. (2000). Molecular basis of exchangeable apolipoprotein function. Biochim. Biophys. Acta 1483, 15-36.
(19) Yu, L-G, Fernig, D.G., Smith, J. A., Milton, J.D. and Rhodes, J. M. (1993). Reversible inhibition of proliferation of epithelial cell lines by Agaricus bisporus (edible mushroom) lectin. Cancer Res. 53, 4627-4632.
(20) Kilpatrick, D.C. (1999). Mechanisms and assessment of lectin-mediated mitogenesis. Mol. Biotechnol. 11, 55-65.
(21) Monzavi, R., and Cohen, P. (2002) IGFs and IGFBPs: Role in health and disease. Best Pract. Res. Clin. Endocrinol. Metab. 16, 433-47.
(22) Furstenberger, G. and Senn, H.J. (2002) Insulin-like growth factors and cancer. Lancet Oncol. 3, 298-302.
(23) D'Alessio, G., Di Donato, A., Mazzarella, L., and Piccoli, R. (1997). Seminal ribonuclease: The importance of diversity in ribonucleases: Structures and functions (D'Alessio, G. & Riordan, J. F., pp. 383-423, Academic Press, New York, N.Y.).
(24) De Lorenzo, C., Nigro, A., Piccoli, R. and D'Alessio, G. (2002) . A new RNase-based immunoconjugate selectively cytotoxic for ErbB2-overexpressing cells. FEBS Lett. 516, 208-12.
(25) Frillingos, S., Sahin-toth, M., Wu, J. and Kaback, H.R. (1998). Cys scanning mutagenesis: A novel approach to structure-function relationship in polytopic membrane proteins. FASEB J. 12, 1281-1299.
(26) Guastella, J., Nelson, N., Nelson, H., Czyzykk, L., Keynan, S., Miedel, M.C., Davidson, N., Lester, H.A. and Kanner, B.I. (1990). Cloning and espression of a rat brain GABA transporter. Science. 249, 1303-1306.
(27) Castagna, M., Shayakul, C., Trotti, D., Sacchi, V.F., Harvey, W.R. and Hediger, M.A. (1998). Cloning and characterization of a potassium-coupled amino acid transporter. Proc. Natl. Acc. Sci. USA. 95, 5395-5400.
(28) Amer, R.E. (2000) Inhibitors of mammalian central nervous system selective amino acid transporters, Curr.Med.Chem. 7, 199-209.
(29) Temussi, P. A., Masino, L. and Pastore, A (2003). From Alzheimer to Huntington: Why is a structural understanding so difficult? EMBO J. 22, 355-361.
(30) Hashimoto, M., Rockenstein, E., Crews, L. and Masliah, E. (2003) Role of protein aggregation in mitochondrial dysfunction and neurodegeneration in Alzheimer's and Parkinson's diseases, Neuromolecular Med. 4, 21-36.
(31) Crescenzi, O., Tomaselli, S., Guerrini, R., Salvadori, S., D'Ursi, A. M., Temussi, P. A. and Picone, D. (2002). Solution structure of the Alzheimer amyloid beta-peptide (1-42) in an apolar microenvironment: Similarity with a virus fusion domain. Eur. J. Biochem. 269, 5642-5648.
(32) Gulbins, E., Dreschers, S. and Bock, J. (2003) Role of mitochondria in apoptosis Exp. Physiol. 88, 85-90.
(33) Robert, J. and Jarry, C. (2003) Multidrugresistance reversal agents. J. Med. Chem., 46, 4805-4817.
(34) Belkin, M. and Schwartz, M. (1989) New biological phenomena associated with laser radiation. Health Phys. 56, 687-690.
(35) Bauer, S., Kemter, K., Bacher, A., Huber, R., Fischer, M. and Steinbacher, S. (2003) Crystal structure of S. pombe riboflavin kinase reveals a novel ATP and riboflavin-binding fold. J. Mol. Biol 326, 1463-1473.
(36) Gerdes ,S.Y., Scholle, M.D., D'Souza, M., Bernal, A. Baev, M.V., Farrell, M., Kurnasov, O.V., Daugherty, M.D., Mseeh, F., Polanuyer, B.M., Campbell, J.W., Anantha, S., Shatalin, K.Y., Chowdhury, S.A., Fonstein, M.Y. and Osterman A.L. (2002). From genetic footprinting to antimicrobial drug targets: examples in cofactor biosynthetic pathways. J. Bacteriol. 184, 4555-72.
(37) Decker, K. and Brandsch, R. (1991). Flavoproteins with a covalent histidyl(N3)-8 alpha-riboflavin linkage. Biofactors 3, 69-81.
(38) Mewies, M., McIntire, W.S. and Scrutton, N.S. (1998) Covalent attachment of flavin adenin dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: the current states of affairs. Prot. Sci. 7, 7-20.

Keywords

Atomic force microscopy (AFM); Protein crystallography; Biomolecular NMR; Molecular dynamics simulations; Biomolecular recognition; Protein structure-function relationships