RICERCA ITALIANA     

Programmi di ricerca simili:

• 1 - RUOLO DELLE INTERAZIONI MOLECOLARI NELL'ACQUISIZIONE DELLA STRUTTURA FUNZIONALE DI PROTEINE MODELLO
• 2 - Proprieta’ strutturali e attivita’ funzionale di un complesso proteico modificante la cromatina nell’uomo
• 3 - Genomica strutturale di metalloproteine e delle loro interazioni funzionali
• 4 - APPROCCIO TEORICO-SPERIMENTALE AGLI STATI NON-NATIVI DELLE PROTEINE: FORMAZIONE DI FIBRILLE AMILOIDI, PROTEINE DISORDINATE E DENATURATE
• 5 - Struttura e funzioni nella patogenesi di proteine non catalitiche prodotte da Funghi e Oomiceti fitopatogeni.
• 6 - Proteine di regolazione nelle piante: analisi biomolecolare dell'interazione di proteine 14-3-3 e calmodulina con proteine bersaglio.
• 7 - STRUTTURA, RUOLO FUNZIONALE E PROPRIETA' ANTIMICROBICHE DELLE CIANOVIRINE EUCARIOTICHE
• 8 - 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.
• 9 - Cerato-platanina: Struttura e relazioni strutturali con altre proteine fungine correlate, variazioni nell'espressione genica indotte in platano e potenzialità nell'indurre resistenza per il controllo del cancro colorato.
• 10 - Fisiologia e patologia dell'assemblaggio, del traffico e del "signaling" di proteine nel reticolo endoplasmico

Classificazione scientifico-disciplinare

• Area scientifico disciplinare: Scienze chimiche
  • CHIMICA GENERALE E INORGANICA
  • CHIMICA ORGANICA
• Area scientifico disciplinare: Scienze biologiche
  • BIOCHIMICA
  • BIOLOGIA MOLECOLARE
  • BIOCHIMICA CLINICA E BIOLOGIA MOLECOLARE CLINICA
• Area scientifico disciplinare: Scienze mediche

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

Lipocaline
1) Akerstrom, B., Flower, D.R. and Salier, J-P (2000). Lipocalins: unity in diversity. Biochim. Biophys. Acta 1482, 1-8.
a) Siero albumina
a1 - Peters, T. Jr. (1996) All about Albumin. Biochemistry, Genetics and Medical Applications. Acad. Press, San Diego.
a2 - Carter, D.C., He, X.M., Munson, S.H., Twigg, P.D., Gernert, K.M., Broom, M.B., Miller, T.Y. (1989). Three-dimensional structure of human serum albumin. Science 244, 1195-1198.
a3 - Carter, D.C., and Ho, J.X. (1994). Structure of serum albumin. Adv. Protein Chem. 45, 153-203.
a4 - Curry, S., Mandelkow, H., Brick, P., Franks, N.(1998). Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nat. Struct. Biol. 5, 827-835.
a5 - Petitpas I.I., Bhattacharya, A.A., Twine, S., East, M., and Curry, S. (2001).Crystal structure analysis of warfarin binding to human serum albumin: anatomy of drug site J.Biol.Chem., 22804-22809.
b) Beta Lattoglobulina
b1 - Sawyer, L. and Kontopidis, G. (2000). The core lipocalin, bovine beta lactoglobulin. Biochim. Biophys. Acta 1482, 136-148.
b2 - Brownlow, S., Morais Cabral, J.H., Cooper, R., Flower, D.R., Yewdall, S.J., Polikarpov, I., North, A.C.T. & Sawyer, L. (1997). Bovine beta-Lactoglobulin at 1.8 A resolution - still an enigmatic lipocalin. Structure 5, 481-495.
b3 - Qin, B.Y., Bewley, M.C., Creamer, L. K., Baker, M.H., Baker, N.E. & Jameson, G.B. (1998). Structural basis of the Tanford Transition of Bovine beta-Lactoglobulin. Biochemistry 37, 14014-14023.
b4 - Wu, S.Y., Perez, M.D., Puyol, P. and Sawyer, L. (1999) Beta-Lactoglobulin binds palmitate within its central cavity. J. Biol. Chem.,274, 170-174.
b5 - Ragona L., Fogolari F., Catalano M., Ugolini R., Zetta L. and Molinari H. (2003) EF loop conformational change triggers ligand binding in beta-lactoglobulins. J Biol Chem. 278, 38840-38846.
b6 - Ragona, L., Fogolari, F., Romagnoli, S., Zetta, L., Maubois, J.L. and Molinari, H. (1999) Unfolding and Refolding of bovine beta-Lactoglobulin Monitored by Hydrogen Exchange measurements. J. Mol. Biol., 293, 953-969.
c) Alfa 1 microglobulina
c1 - Akerstrom, B., Logddberg, L., Berggard, T., Osmark, P. and Lindqvist, A. (2000). Alpha1 microglobulin: a yellow-brown lipocalin. Biochim. Biophys. Acta 1482, 172-184.
c2 - Akerstrom, B. and Logddberg, L. (1990). An intriguing member of the lipocalin protein family: alpha 1-microglobulin. Trends in Biochem. Sci. 15, 240-243.
c3 - Berggard, T., Cohen, A., Persson, P., Lindqvist, A., Cedervall, T., Silow, M., Thogersen, I. B,, Jonsson, J. .A, Enghild, J.J., Akerstrom,B. (1999). Alpha1-microglobulin chromophores are located to three lysine residues semiburied in the lipocalin pocket and associated with a novel lipophilic compound. Protein Science 8, 2611-2620.
c4 - Amoresano A., Minchiotti L., Cosulich E. M., Campagnoli M., Pucci P., Andolfo A., Gianazza E. and Galliano M. (2000). Structural Characterization of the oligosaccharide chains of human alpha-1 microglobulin from urine and amniotic fluid. Eur. J. Biochem. 267, 1-9.
d) Apolipoprotein D
d1 - Weech P.K., Provost P., Tremblay N.M., Camato R.N., Milne R.W., Marcel Y.L..and Rassart E. (1991). Apolipoprotein D -- an atypical apolipoprotein. Prog. Lipid Res., 30, 259-266.
d2 - Rassart E., Bedirian A., Do Carmo S., Guinard O., Sirois J., Terrisse L. and Milne R. (2000). Apolipoprotein D. Biochim. Biophys. Acta, 1482, 185-198.
d3 - Goessling W.and Zucker S.D.(2000). Role of apolipoprotein D in the transport of bilirubin in plasma. Am. J. Physiol. Gastrointest. Liver Physiol., 279, G356-65.
d4 - Morais Cabral J.H., Atkins G.L., Sanchez L.M., Lopez-Boado Y.S., Lopez-Otin C. and Sawyer L. (1995). Arachidonic acid binds to apolipoprotein D: implications for the protein's function. FEBS Lett. 366, 53-56.
d5 - Zeng C., Spielman A.I., Vowels B.R., Leyden J.J., Biemann K.and Preti G. (1996). A human axillary odorant is carried by apolipoprotein D. Proc. Natl. Acad. Sci. U.S.A. 93, 6626-6630.
d6 - Mahadik S.P., Khan M.M., Evans D.R.and Parikh V.V. (2002). Elevated plasma level of apolipoprotein D in schizophrenia and its treatment and outcome. Schizophr. Res. 58, 55-62.
e) Prostaglandin D synthase (beta trace)
e1 - Peitsch, M.C. and Boguski, M.S. (1991). The first lipocalin with enzymatic activity. TIBS 16, 363.
e2- Urade, U.,and Hayaishi, O. (2000). Prostaglandin D synthase: structure and function. Vitamins and Hormones, 56, 89-120.
e3- Urade, Y. and Hayaishi, O (2000). Biochemical, structural, genetic, physiological and pathophysiological features of lipocalin-type prostaglandin D synthase. Biochim. Biophys. Acta 1482, 259-271.
e4 - Hoffmann, A., Conradt, H.S., Gross, G., Nimtz, M., Lottspeich, F. and Wurster, U. (1993). Purification and chemical characterization of beta-trace protein from human cerebrospinal fluid: its identification as prostaglandin D Synthase.
f) Fatty acid-binding protein (basica) da fegato di pollo
f1 - Banaszak, L., Winter, N., Xu, Z., Bernlohr, D. A., Cowan. S. and Jones, T. A. (1994). Lipid-binding proteins: a family of fatty acid and retinoid transport proteins. Advances in Protein Chemistry 45, 89-151.
f2 - Thompson, J., Reese Wagoner, A. and Banaszak, L. (1999) . Liver fatty acid binding protein: species variation and the accomodation of different ligands. Biochim. Biophys. Acta 1441, 117-130.
f3 - Scapin, G., Spadon, P., Pengo, L., Mammi, M., Zanotti, G. and Monaco, H. L. (1988). Chicken liver basic fatty acid-binding protein (pI=9.0). Purification, crystallization and preliminary X-ray data. Febs Lett. 240, 196-200.
f4 - Scapin, G., Spadon, P., Mammi. M., Zanotti, G. and Monaco, H. L. (1990). Crystal structure of chicken liver basic fatty acid-binding protein at2.7 A resolution. Mol. and Cell. Biochem. 98, 95-99.
f5 - Ceciliani, F., Monaco, H. L., Ronchi, S., Faotto, L. and Spadon, P. (1994). The primary structure of a basic (pI 9.0) fatty acid-binding protein from liver of Gallus domesticus. Comp. Biochem. Physiol. 109B, 261-271.
f6 - Lücke, C., Zhang, F., Hamilton, J.A., Sacchettini, J.C. and Rüterjans, H. (2000). Solution structure of ileal lipid binding protein in complex with glycocholate. Eur. J. Biochem. 267, 2929-2938.
f7 - Kurz, M., Brachvogel, V., Matter, H., Stengelin, S., Thuring, H. and Kramer, W. (2003). Insights into the bile acid transportation system: The human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins: Structure, Function, and Genetics. 50, 312-328.
g) Riboflavin-binding protein
g1 - White, H. B. III & Merrill A. H. Jr. (1988). Riboflavin-binding proteins. Ann. Rev. Nutr. 8: 279-299 (1988)
g2 - Monaco H.L (1997). Crystal Structure of chicken riboflavin-binding protein. The EMBO J. 18, 1475-1483.
g3 - Monaco H. L. (2002). Riboflavin-binding protein in Wiley Encyclopedia of Molecular Medicine, Thomas E. Creighton editor., 2807-10. John Wiley & Sons.
h) Intrinsic Factor
h1) Seetharam B.and Bose S., Li N. (1999). Cellular import of cobalamin (Vitamin B-12). J Nutr., 129, 1761-1764.
h2) Brada N., Gordon M.M., Wen J.and Alpers D.H. (2001). Transfer of cobalamin from intrinsic factor to transcobalamin II. J. Nutr. Biochem., 12, 200-206
h3) Fedosov S.N., Berglund L., Fedosova N.U., Nexo E. and Petersen T.E. (2002). Comparative analysis of cobalamin binding kinetics and ligand protection for intrinsic factor, transcobalamin, and haptocorrin. J. Biol. Chem. 277, 9989-9996.
h4) Lindblom A., Quadt N., Marsh T., Aeschlimann D., Morgelin M., Mann K., Maurer P.and Paulsson M. (1999). The intrinsic factor-vitamin B12 receptor, cubilin, is assembled into trimers via a coiled-coil alpha-helix. J. Biol. Chem., 274, 6374-6380.
i) Astaxanthin-binding protein
i1) Zagalsky P.F. and Herring P.J. (1997). Studies on the blue astaxanthin-proteins of Velella velella (Coelenterata: Chondrophora). Philos Trans R Soc Lond B Biol Sci.279, 289-326.

Parole Chiave

CRISTALLOGRAFIA; RISONANZA MAGNETICA NUCLEARE; ANALISI DI SEQUENZE; SPETTROMETRIA DI MASSA; MODELLISTICA MOLECOLARE; ELETTROFORESI NON CONVENZIONALE; PROTEINE DI TRASPORTO; MOLECOLE IDROFOBICHE; LIPOCALINE