{"id":43,"date":"2019-11-13T09:11:03","date_gmt":"2019-11-13T08:11:03","guid":{"rendered":"http:\/\/nmr-2019.laboratory.uniroma2.it\/?page_id=43"},"modified":"2019-11-13T10:10:54","modified_gmt":"2019-11-13T09:10:54","slug":"risultati-recenti","status":"publish","type":"page","link":"https:\/\/nmr-2019.laboratory.uniroma2.it\/?page_id=43","title":{"rendered":"Risultati Recenti"},"content":{"rendered":"

Pubblicazioni (ultimi cinque anni)
\nBiomolecole
\nLigand binding promiscuity of human liver fatty acid binding protein: structural and dynamic insights from an interaction study with glycocholate and oleate. F. Favretto, M. Assfalg, M. Gallo, D.O. Cicero, M. D\u2019Onofrio, H. Molinari. ChemBioChem, 14, 1807-1819 (2013).
\nExtracellular hydrolytic enzyme production by proteolytic bacteria from the Antarctic. M. Tropeano, S. V\u00e1zquez, S. Coria, A. Turjanski, D.O. Cicero, A. Bercovich, W. Mac Cormack. Polish Polar Res., 34, 253-267 (2013).
\n1H, 15N and 13C chemical shift assignments of the C-Ala domain of the alanyl-tRNA synthetase of the psychrophilic bacterium Bizionia argentinensis sp. nov. C. Smal, S. Zanzoni, M. D\u00b4Onofrio, H. Molinari, D. O. Cicero, M. Assfalg. Biomol. NMR Assign., 8, 415-418 (2014).
\nSolution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain. M. Aran, C. Smal, L. Pellizza, M. Gallo, L.H. Otero, S. Klinke, F.A. Goldbaum, E.R. Ithurralde, A. Bercovich, W.P. Mac Cormack, A.G. Turjanski, D.O. Cicero. Proteins, 82, 3062-3078 (2014).
\nStructural and functional characterization of a cold adapted stand-alone TPM domain reveals a relationship between dynamics and phosphatase activity. L. Pellizza, C. Smal, R.E. Ithurralde, A.G. Turjanski, D.O. Cicero, M. Aran. FEBS J., 283, 4370-4385 (2016).
\nNuclear factor (erythorid-derived 2)-like 2 (NRF2) drug discovery: Biochemical toolbox to develop NRF2 activators by reversible binding of Kelch-like ECH-associated protein 1 (KEAP1). A. Bresciani, A. Missineo, M. Gallo, M. Cerretani, P. Fezzardi, L. Tomei, D.O. Cicero, S. Altamura, A. Santoprete, R. Ingenito, E. Bianchi, R. Pacifici, C. Dominguez, I. Munoz-Sanjuan, S. Harper, L. Toledo-Sherman, L.C. Park, Arch. Biochem. Biophys., 631, 31-41 (2017).
\nMolecole organiche
\nSynthesis and characterization of functionalized meso-triaryl-tetrabenzocorroles. G. Pomarico, S. Nardis, M. Stefanelli, D.O. Cicero, M. Gra\u00e7a H. Vicente, Y. Fang, P. Chen, K.M. Kadish, R. Paolesse. Inorg. Chem., 52, 8834-8844 (2013).
\nThe corrole and ferrocene marriage: 5,10,15-triferrocenylcorrolato Cu. G. Pomarico, A. Vecchi, F. Mandoj, O. Bortolini, D. O. Cicero, P. Galloni, R. Paolesse. Chem.Commun., 50, 4076-4078 (2014).
\nPhenyl Derivative of Iron 5,10,15-Tritolylcorrole. S. Nardis, D. O. Cicero, S. Licoccia, G. Pomarico, B. Berionni Berna, M. Sette, G. Ricciardi, A. Rosa, F. R. Fronczek, K. M. Smith, R. Paolesse, Inorg. Chem., 53, 4215-4227 (2014).
\nNew example of hemiporphycene formation from the corrole ring expansion. Y. Fang, F. Mandoj, S. Nardis, G. Pomarico, M. Stefanelli, D.O. Cicero, S. Lentini, A. Vecchi, Y. Cui, L. Zeng, K. Kadish, R. Paolesse, Inorg. Chem.,53, 7404-7415 (2014).
\nChemical characterization and surface properties of a new bioemulsifier produced by Pedobacter sp.strain MCC-Z. T. Beltrani, S. Chiavarini, D.O. Cicero, M. Grimaldi, C. Ruggeri, E. Tamburini, C. Cremisini. Int. J. Biol. Macromol.,72, 1090-1096 (2014).
\nWidening the scope of the corrole sulfonation. M.L. Naitana, S. Nardis, S. Lentini, D.O. Cicero, R. Paolesse. JPP, 19, 1-10 (2015).
\nSynthesis and frunctionalization of \uf062 alky-meso-triarylcorroles. G. Pomarico, M. Stefanelli, S. Nardis, S. Lentini, D.O. Cicero, G.T. McCandless, K.M. Smith, R. Paolesse. JPP, 19, 1-9 (2015).
\n5,10,15-Triferrocenylcorrole Complexes. G. Pomarico, P. Galloni, F. Mandoj, S. Nardis, M. Stefanelli, A. Vecchi, S. Lentini, D.O. Cicero, Y. Cui, L. Zeng, K.M. Kadish, R. Paolesse. Inorg. Chem., 54, 10256-10268 (2015).
\n\uf062-substituted ferrocenyl porphyrins: The role of the spacer and of the number of substituents on their structural and spectroscopic characteristics. C. Mazzuca, B. Di Napoli, S. Lentini, D.O. Cicero, E. Gatto, P. Tagliatesta, A. Palleschi. JPP, 20, 234-244 (2016).
\nThe scope of the \uf062-halogenation of triarylcorroles. S. Nardis, G. Pomarico, M. Stefanelli, S. Lentini, D.O. Cicero, F.R. Fronczek, K.M. Smith, R. Paolesse. JPP, 20, 1-10 (2016).
\nNMR spectroscopy of the phenyl derivative of germanium(IV) 5,10,15-tritolylcorrole. G. Ricciardi, D.O. Cicero, S. Lentini, S. Nardis, R. Paolesse, A. Rosa. JPP, 20, 525-533 (2016).
\nHighly emissive water soluble phosphorus corrole. M.L. Naitana, S. Nardis, G. Pomarico, M. Raggio, F. Caroleo, D.O. Cicero, S. Lentini, L. Prodi, D. Genovese, S. Mitta, A. Sgarlata, M. Fanfoni, L. Persichetti, R. Paolesse. Chem. Eur. J., 23, 905-916 (2017).
\nMetabolomica
\nA small sided game session affects salivary metabolite levels in young soccer players. D.O. Cicero, S. Di Marino, V. Dinallo, M. Pieri, V. Summa, A. Desideri, A. Bernardini, F. Perondi, S. D\u2019Ottavio. BSI, 5, 55-70 (2016).<\/p>\n

Biostructural, Biochemistry \u00a0and NMR spectroscopy laboratory<\/b><\/p>\n

RECENT RESULTS<\/b><\/p>\n

\u00a0Solution structure \u00a0of \u00a0Syringomycin in micelles<\/b><\/p>\n

\u00a0 \u00a0 \u00a0 \u00a0\u00a0\"syrE_noesy_SDS\"<\/a>\"12.jpg\"<\/p>\n

NOESY\u00a0 spectrum of\u00a0 Syringomycin in perdeuterated SDS micelles and three dimensional structure\u00a0 of\u00a0 Syringomycin in SDS micelles after MD simulation\u00a0 in octane water system.<\/b><\/p>\n

Anselmi M, Eliseo T, Zanetti-Polzi L, Fullone MR, Fogliano V, Di Nola A, Paci M, Grgurina I. Structure of the lipodepsipeptide syringomycin E in phospholipids and sodium dodecylsulphate micelle studied by circular dichroism, NMR spectroscopy and molecular dynamics. Biochim Biophys Acta. 2011 Sep;1808(9):2102-10.<\/em><\/p>\n

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Solution structure of\u00a0 the protein E2 of HPV , Papilloma virus\u00a0 and complex with its DNA consensus sequence .<\/b><\/p>\n

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NMR \u00a0HSQC of the \u00a0E2 protein\u00a0 from Papilloma Virus-HPV 16.<\/b><\/p>\n

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Solution structure of the E2 protein fron Papilloma Virus HPV \u2013 16\u00a0 by NMR<\/b><\/p>\n

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\u00a0Complex of\u00a0 E2 protein of human papilloma Virus HPV 16 with its\u00a0 DNA consensus sequence.<\/b><\/p>\n

Eliseo T, S\u00e1nchez IE, Nadra AD, Dellarole M, Paci M, de Prat Gay G, Cicero DO., Indirect DNA readout on the protein side: coupling between histidine protonation,global structural cooperativity, dynamics, and DNA binding of the human papillomavirus type 16 E2C domain. J Mol Biol. 2009 May 1;388(2):327-44<\/em><\/p>\n

Cicero DO, Nadra AD, Eliseo T, Dellarole M, Paci M, de Prat-Gay G. Structuraland thermodynamic basis for the enhanced transcriptional control by the human papillomavirus strain-16 E2 protein. Biochemistry. 2006 May 30;45(21):6551-60.<\/em><\/p>\n

Structural study of the \u201c calmodulin-like\u201d\u00a0 protein Mcl1p<\/b><\/p>\n

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Three dimensional representation of the solution structure of the protein Mcl1p , the calmodulin like protein\u00a0 determined by NMR and molecular dynamics simulation .<\/p>\n

Amata I, Gallo M, Pennestri M, Paci M, Ragnini-Wilson A, Cicero DO.N-lobe dynamics of myosin light chain dictates its mode of interaction with myosin V IQ1. Biochemistry. 2008 Nov 25;47(47):12332-45.<\/em><\/p>\n

Pennestri M, Melino S, Contessa GM, Casavola EC, Paci M, Ragnini-Wilson A,Cicero DO. Structural basis for the interaction of the myosin light chain Mlc1p with the myosin V Myo2p IQ motifs. J Biol Chem. 2007 Jan 5;282(1):667-79.<\/em><\/p>\n

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The structure of\u00a0 the NS3 viral proteases<\/b><\/p>\n

NS3 of Dengue virus<\/b><\/p>\n

\"Immagine6\"<\/a><\/p>\n

Three dimensional structure of the \u00a0NS3 protease of Dengue virus from NMR data, MD simulations and biochemical studies.<\/p>\n

Melino S, Paci M. Progress for dengue virus diseases. Towards the NS2B-NS3pro inhibition for a therapeutic-based approach. FEBS J. 2007 Jun;274(12):2986-3002.<\/em><\/p>\n

Melino S, Fucito S, Campagna A, Wrubl F, Gamarnik A, Cicero DO, Paci M. The active essential CFNS3d protein complex. FEBS J. 2006 Aug;273(16):3650-62.<\/em><\/p>\n

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Structure.function relationship in the enzyme Azotobacter Vinelandii Rhodanese. \u00a0MD and functional studies. The NMR assignment of the Azotobacter Vinelandii Rhodanese.<\/b><\/p>\n

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The chemical shift mapping of AV Rhodanese .<\/p>\n

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Red\u00a0 resonances \u00a0changing from E to ES (and to ESe)<\/p>\n

Green residues behave\u00a0 differently \u00a0\u00a0loading\u00a0 S and Se .<\/p>\n

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Melino S, Cicero DO, Orsale M, Forlani F, Pagani S, Paci M. Azotobacter vinelandii rhodanese: selenium loading and ion interaction studies. Eur J Biochem. 2003 Oct;270(20):4208-15.<\/em><\/p>\n

Melino S, Cicero DO, Orsale M, Forlani F, Pagani S, Paci M. Azotobacter<\/em><\/p>\n

vinelandii rhodanese: selenium loading and ion interaction studies. Eur JBiochem. 2003 Oct;270(20):4208-15.<\/em><\/p>\n

Fasano M, Orsale M, Melino S, Nicolai E, Forlani F, Rosato N, Cicero D,<\/em><\/p>\n

Pagani S, Paci M. Surface changes and role of buried water molecules during thsulfane sulfur transfer in rhodanese from Azotobacter vinelandii: a fluorescence<\/em><\/p>\n

quenching and nuclear magnetic relaxation dispersion spectroscopic study.<\/em><\/p>\n

Biochemistry. 2003 Jul 22;42(28):8550-7.<\/em><\/p>\n

Gallo M, Melino S, Melis R, Paci M, Cicero DO. Backbone NMR assignment of the 29.6 kDa rhodanese protein from Azotobacter vinelandii. J Biomol NMR. 2006;36 Suppl 1:73.<\/em><\/p>\n

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Applications of NMR spectroscopy to Food science .<\/b><\/p>\n

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Pizzoferrato L. , M. Paci\u00a0 and G. Rotilio, Structural modification and bioavailabillity of starch componentes upon the extent of Maillard reaction: and enzymatic degradation and solid state C-13 CP MAS NMR study,( 1998)\u00a0 J. Agric. Food Chem.46, 438-441.<\/em><\/p>\n

Laura Pizzoferrato,\u00a0 Giuseppe Rotilio and Maurizio Paci, Modification of structure and\u00a0 digestibility of starch components of the chestnut\u00a0 upon cooking:\u00a0 an enzymatic degradation and a solid state\u00a0 13C CP MAS NMR study.( 1999) J. Agric. Food Chem., 47, 4060-4063<\/em><\/p>\n

Laura Pizzoferrato, Pamela Manzi,\u00a0 Fabio Bertocchi , G.\u00a0\u00a0 Fanelli,\u00a0 Giuseppe Rotilio\u00a0 and Maurizio Paci , Solid state\u00a0 13C CP MAS NMR spectroscopy of\u00a0\u00a0\u00a0 mushrooms gives\u00a0 directly the\u00a0 ratio between polysaccharides and proteins\u00a0 depending on the species and clones. (2000)\u00a0 J. Agric. Food Chem., 48, 5484-5488.<\/em><\/p>\n

Bertocchi F, Paci M. (2008). Applications of high-resolution solid-state NMR spectroscopy in food science. Journal of Agricultural And Food Chemistry, 56, 9317-9327<\/em><\/p>\n

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Application of Diffusion NMR spectroscopy ( DOSY) to chemical , biological and pharmaceutical studies.<\/b><\/p>\n

Molecular weight selection by diffusion NMR spectra of different MW Poly ethilene oxide\u00a0( PEO). The calibration curve.<\/p>\n

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\"Diapositiva10\"<\/a><\/p>\n","protected":false},"excerpt":{"rendered":"

Pubblicazioni (ultimi cinque anni) Biomolecole Ligand binding promiscuity of human liver fatty acid binding protein: structural and dynamic insights from an interaction study with glycocholate and oleate. F. Favretto, M. Assfalg, M. Gallo, D.O. Cicero, M. D\u2019Onofrio, H. Molinari. ChemBioChem,<\/p>\n","protected":false},"author":2,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":[],"_links":{"self":[{"href":"https:\/\/nmr-2019.laboratory.uniroma2.it\/index.php?rest_route=\/wp\/v2\/pages\/43"}],"collection":[{"href":"https:\/\/nmr-2019.laboratory.uniroma2.it\/index.php?rest_route=\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/nmr-2019.laboratory.uniroma2.it\/index.php?rest_route=\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/nmr-2019.laboratory.uniroma2.it\/index.php?rest_route=\/wp\/v2\/users\/2"}],"replies":[{"embeddable":true,"href":"https:\/\/nmr-2019.laboratory.uniroma2.it\/index.php?rest_route=%2Fwp%2Fv2%2Fcomments&post=43"}],"version-history":[{"count":3,"href":"https:\/\/nmr-2019.laboratory.uniroma2.it\/index.php?rest_route=\/wp\/v2\/pages\/43\/revisions"}],"predecessor-version":[{"id":62,"href":"https:\/\/nmr-2019.laboratory.uniroma2.it\/index.php?rest_route=\/wp\/v2\/pages\/43\/revisions\/62"}],"wp:attachment":[{"href":"https:\/\/nmr-2019.laboratory.uniroma2.it\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=43"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}