Pubblicazioni (ultimi cinque anni)
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’Onofrio, H. Molinari. ChemBioChem, 14, 1807-1819 (2013).
Extracellular hydrolytic enzyme production by proteolytic bacteria from the Antarctic. M. Tropeano, S. Vázquez, S. Coria, A. Turjanski, D.O. Cicero, A. Bercovich, W. Mac Cormack. Polish Polar Res., 34, 253-267 (2013).
1H, 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´Onofrio, H. Molinari, D. O. Cicero, M. Assfalg. Biomol. NMR Assign., 8, 415-418 (2014).
Solution 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).
Structural 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).
Nuclear 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).
Molecole organiche
Synthesis and characterization of functionalized meso-triaryl-tetrabenzocorroles. G. Pomarico, S. Nardis, M. Stefanelli, D.O. Cicero, M. Graça H. Vicente, Y. Fang, P. Chen, K.M. Kadish, R. Paolesse. Inorg. Chem., 52, 8834-8844 (2013).
The 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).
Phenyl 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).
New 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).
Chemical 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).
Widening the scope of the corrole sulfonation. M.L. Naitana, S. Nardis, S. Lentini, D.O. Cicero, R. Paolesse. JPP, 19, 1-10 (2015).
Synthesis and frunctionalization of  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).
5,10,15-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).
-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).
The scope of the -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).
NMR 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).
Highly 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).
A 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’Ottavio. BSI, 5, 55-70 (2016).

Biostructural, Biochemistry  and NMR spectroscopy laboratory


 Solution structure  of  Syringomycin in micelles


NOESY  spectrum of  Syringomycin in perdeuterated SDS micelles and three dimensional structure  of  Syringomycin in SDS micelles after MD simulation  in octane water system.

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.


Solution structure of  the protein E2 of HPV , Papilloma virus  and complex with its DNA consensus sequence .


NMR  HSQC of the  E2 protein  from Papilloma Virus-HPV 16.


Solution structure of the E2 protein fron Papilloma Virus HPV – 16  by NMR

fig 5new

 Complex of  E2 protein of human papilloma Virus HPV 16 with its  DNA consensus sequence.

Eliseo T, Sánchez 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

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.

Structural study of the “ calmodulin-like”  protein Mcl1p


Three dimensional representation of the solution structure of the protein Mcl1p , the calmodulin like protein  determined by NMR and molecular dynamics simulation .

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.

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.


The structure of  the NS3 viral proteases

NS3 of Dengue virus


Three dimensional structure of the  NS3 protease of Dengue virus from NMR data, MD simulations and biochemical studies.

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.

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.


Structure.function relationship in the enzyme Azotobacter Vinelandii Rhodanese.  MD and functional studies. The NMR assignment of the Azotobacter Vinelandii Rhodanese.





The chemical shift mapping of AV Rhodanese .





Red  resonances  changing from E to ES (and to ESe)

Green residues behave  differently   loading  S and Se .



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.

Melino S, Cicero DO, Orsale M, Forlani F, Pagani S, Paci M. Azotobacter

vinelandii rhodanese: selenium loading and ion interaction studies. Eur JBiochem. 2003 Oct;270(20):4208-15.

Fasano M, Orsale M, Melino S, Nicolai E, Forlani F, Rosato N, Cicero D,

Pagani S, Paci M. Surface changes and role of buried water molecules during thsulfane sulfur transfer in rhodanese from Azotobacter vinelandii: a fluorescence

quenching and nuclear magnetic relaxation dispersion spectroscopic study.

Biochemistry. 2003 Jul 22;42(28):8550-7.

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.


Applications of NMR spectroscopy to Food science .


Pizzoferrato L. , M. Paci  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)  J. Agric. Food Chem.46, 438-441.

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

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

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



Application of Diffusion NMR spectroscopy ( DOSY) to chemical , biological and pharmaceutical studies.

Molecular weight selection by diffusion NMR spectra of different MW Poly ethilene oxide ( PEO). The calibration curve.








Untitled-10 Untitled-11






Leave a comment

Leave a Reply

Your email address will not be published. Required fields are marked *

You may use these HTML tags and attributes: <a href="" title=""> <abbr title=""> <acronym title=""> <b> <blockquote cite=""> <cite> <code> <del datetime=""> <em> <i> <q cite=""> <strike> <strong>