Insight into conformational modification of alpha-synuclein in the presence of neuronal whole cells and of their isolated membranes (435 views)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468), 2015 Feb 18; 589(7): 798-804.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.519, 5-year impact factor: 3.478
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84923326923&partnerID=40&md5=97d917d32b1f9a1e05c753ca7a4a4817
Keywords: Alpha Synuclein, Cd Analyses, Nmr Spectroscopy, Protein?embranes Interaction, Protein-Membranes Interaction, Protein? Embranes Interaction, Protein–membranes Interaction, Di(n Succinimidyl)glutarate, Lysine, Unclassified Drug, Protein Binding, Snca Protein, Human, Article, Cell Membrane, Circular Dichroism, Confocal Microscopy, Conformational Transition, Controlled Study, Heteronuclear Single Quantum Coherence, Human Cell, Lipid Bilayer, Nuclear Magnetic Resonance Spectroscopy, Priority Journal, Protein Interaction, Whole Cell, Chemical Structure, Chemistry, Metabolism, Nuclear Magnetic Resonance Imaging, Protein Secondary Structure, Tumor Cell Line, Alpha-Synuclein, Models, Molecular, Protein Structure,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, C.N.R. via Mezzocannone, 16, 80134 Napoli, Italy.
DBSV - Dept. of Biotechnology and Life Sciences - Universita degli Studi dell'Insubria, via J.H. Dunant 3, 21100 Varese, Italy
The Protein Factory, Centro Interuniversitario di Biotecnologie Proteiche, Politecnico di Milano, ICRM CNR Milano, Universita degli studi dell'Insubria, Milano, Italy.
Dipartimento di Scienze e Tecnologie Ambientali, Biologiche e Farmaceutiche, Seconda Universita di Napoli via Vivaldi, 43, 81100 Caserta, Italy.
DBSV, Dept. of Biotechnology and Life Sciences, Università degli Studi dell'Insubria, via J.H. Dunant 3, Varese, Italy
References:
Fauvet, B., Mbefo, M.K., Fares, M.B., Desobry, C., Michael, S., Ardah, M.T., Tsika, E., Lion, N., alpha-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer (2012) J. Biol. Chem., 287, pp. 15345-1536
Bussell, R., Eliezer, D., A structural and functional role for 11-mer repeats in alpha-synuclein and other exchangeable lipid binding proteins (2003) J. Mol. Biol., 329, pp. 763-778
Giasson, B.I., Murray, I.V., Trojanowski, J.Q., Lee, V.M., A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly (2001) J. Biol. Chem., 276, pp. 2380-2386
Binolfi, A., Theillet, F.X., Selenko, P., Bacterial in-cell NMR of human alpha-synuclein: a disordered monomer by nature? (2012) Biochem. Soc. Trans., 40, pp. 950-954
Zarbiv, Y., Simhi-Haham, D., Israeli, E., Elhadi, S.A., Grigoletto, J., Sharon, R., Lysine residues at the first and second KTKEGV repeats mediate alpha-synuclein binding to membrane phospholipids (2014) Neurobiol. Dis., 70, pp. 90-98
Lokappa, S.B., Suk, J.E., Balasubramanian, A., Samanta, S., Situ, A.J., Ulmer, T.S., Sequence and membrane determinants of the random coil-helix transition of alpha-synuclein (2014) J. Mol. Biol., 426, pp. 2130-2144
Chong, S.S., Taneva, S.G., Lee, J.M., Cornell, R.B., The curvature sensitivity of a membrane-binding amphipathic helix can be modulated by the charge on a flanking region (2014) Biochemistry, 53, pp. 450-461
Moriarty, G.M., Janowska, M.K., Kang, L., Baum, J., Exploring the accessible conformations of N-terminal acetylated alpha-synuclein (2013) FEBS Lett., 587, pp. 1128-1138
Fusco, G., De Simone, A., Gopinath, T., Vostrikov, V., Vendruscolo, M., Dobson, C.M., Veglia, G., Direct observation of the three regions in alpha-synuclein that determine its membrane-bound behaviour (2014) Nat. Commun., 5, p. 3827
Vermaas, J.V., Tajkhorshid, E., Conformational heterogeneity of alpha-synuclein in membrane (2014) Biochim. Biophys. Acta
Deleersnijder, A., Gerard, M., Debyser, Z., Baekelandt, V., The remarkable conformational plasticity of alpha-synuclein: blessing or curse? (2013) Trends Mol. Med., 19, pp. 368-377
Habchi, J., Tompa, P., Longhi, S., Uversky, V.N., Introducing protein intrinsic disorder (2014) Chem. Rev., 114, pp. 6561-6588
Bartels, T., Choi, J.G., Selkoe, D.J., alpha-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation (2011) Nature, 477, pp. 107-110
Wang, W., Perovic, I., Chittuluru, J., Kaganovich, A., Nguyen, L.T., Liao, J., Auclair, J.R., Simorellis, A.K., A soluble alpha-synuclein construct forms a dynamic tetramer (2011) Proc. Natl. Acad. Sci. U.S.A., 108, pp. 17797-17802
Waudby, C.A., Camilloni, C., Fitzpatrick, A.W., Cabrita, L.D., Dobson, C.M., Vendruscolo, M., Christodoulou, J., In-cell NMR characterization of the secondary structure populations of a disordered conformation of alpha-synuclein within E. coli cells (2013) PLoS ONE, 8
Jang, A., Lee, H.J., Suk, J.E., Jung, J.W., Kim, K.P., Lee, S.J., Non-classical exocytosis of alpha-synuclein is sensitive to folding states and promoted under stress conditions (2010) J. Neurochem., 113, pp. 1263-1274
Bellani, S., Mescola, A., Ronzitti, G., Tsushima, H., Tilve, S., Canale, C., Valtorta, F., Chieregatti, E., GRP78 clustering at the cell surface of neurons transduces the action of exogenous alpha-synuclein (2014) Cell Death Differ.
Constantinescu, R., Constantinescu, A.T., Reichmann, H., Janetzky, B., Neuronal differentiation and long-term culture of the human neuroblastoma line SH-SY5Y (2007) J. Neural Transm. Suppl., pp. 17-28
Caldinelli, L., Albani, D., Pollegioni, L., One single method to produce native and Tat-fused recombinant human alpha-synuclein in Escherichia coli (2013) BMC Biotechnol., 13, p. 32
Bartels, T., Kim, N.C., Luth, E.S., Selkoe, D.J., N-alpha-acetylation of alpha-synuclein increases its helical folding propensity, GM1 binding specificity and resistance to aggregation (2014) PLoS One, 9
Mercurio, F.A., Marasco, D., Pirone, L., Scognamiglio, P.L., Pedone, E.M., Pellecchia, M., Leone, M., Heterotypic Sam-Sam association between Odin-Sam1 and Arap3-Sam: binding affinity and structural insights (2013) ChemBioChem, 14, pp. 100-106
Diana, D., Smaldone, G., De Antonellis, P., Pirone, L., Carotenuto, M., Alonzi, A., Di Gaetano, S., Fattorusso, R., Mapping functional interaction sites of human prune C-terminal domain by NMR spectroscopy in human cell lysates (2013) Chemistry
Smaldone, G., Falanga, A., Capasso, D., Guarnieri, D., Correale, S., Galdiero, M., Netti, P.A., Di Gaetano, S., GH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins (2013) Int. J. Nanomed., 8, pp. 2555-2565
Dettmer, U., Newman, A.J., Luth, E.S., Bartels, T., Selkoe, D., In vivo cross-linking reveals principally oligomeric forms of alpha-synuclein and beta-synuclein in neurons and non-neural cells (2013) J. Biol. Chem., 288, pp. 6371-6385
Scholtz, J.M., Qian, H., York, E.J., Stewart, J.M., Baldwin, R.L., Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water (1991) Biopolymers, 31, pp. 1463-1470
Masse, J.E., Keller, R., AutoLink: automated sequential resonance assignment of biopolymers from NMR data by relative-hypothesis-prioritization-based simulated logic (2005) J. Magn. Reson., 174, pp. 133-151
Farrow, N.A., Muhandiram, R., Singer, A.U., Pascal, S.M., Kay, C.M., Gish, G., Shoelson, S.E., Kay, L.E., Backbone dynamics of a free and a phosphopeptide-complexed src homology-2 domain studied by N-15 Nmr relaxation (1994) Biochemistry, 33, pp. 5984-6003
Uversky, V.N., Eliezer, D., Biophysics of Parkinson's Disease: structure and aggregation of alpha-synuclein (2009) Curr. Protein Pept. Sci., 10, pp. 483-499
Stefanovic, A.N., Stockl, M.T., Claessens, M.M., Subramaniam, V., alpha-Synuclein oligomers distinctively permeabilize complex model membranes (2014) FEBS J., 281, pp. 2838-2850
Lee, S.J., Origins and effects of extracellular alpha-synuclein: implications in Parkinson's disease (2008) J. Mol. Neurosci., 34, pp. 17-22
Eliezer, D., Kutluay, E., Bussell, R., Browne, G., Conformational properties of alpha-synuclein in its free and lipid-associated states (2001) J. Mol. Biol., 307, pp. 1061-1073
Bodner, C.R., Dobson, C.M., Bax, A., Multiple tight phospholipid-binding modes of alpha-synuclein revealed by solution NMR spectroscopy (2009) J. Mol. Biol., 390, pp. 775-790
Tompa, P., Fuxreiter, M., Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions (2008) Trends Biochem. Sci., 33, pp. 2-8
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468), 2015 Feb 18; 589(7): 798-804.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.519, 5-year impact factor: 3.478
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84923326923&partnerID=40&md5=97d917d32b1f9a1e05c753ca7a4a4817
Keywords: Alpha Synuclein, Cd Analyses, Nmr Spectroscopy, Protein?embranes Interaction, Protein-Membranes Interaction, Protein? Embranes Interaction, Protein–membranes Interaction, Di(n Succinimidyl)glutarate, Lysine, Unclassified Drug, Protein Binding, Snca Protein, Human, Article, Cell Membrane, Circular Dichroism, Confocal Microscopy, Conformational Transition, Controlled Study, Heteronuclear Single Quantum Coherence, Human Cell, Lipid Bilayer, Nuclear Magnetic Resonance Spectroscopy, Priority Journal, Protein Interaction, Whole Cell, Chemical Structure, Chemistry, Metabolism, Nuclear Magnetic Resonance Imaging, Protein Secondary Structure, Tumor Cell Line, Alpha-Synuclein, Models, Molecular, Protein Structure,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, C.N.R. via Mezzocannone, 16, 80134 Napoli, Italy.
DBSV - Dept. of Biotechnology and Life Sciences - Universita degli Studi dell'Insubria, via J.H. Dunant 3, 21100 Varese, Italy
The Protein Factory, Centro Interuniversitario di Biotecnologie Proteiche, Politecnico di Milano, ICRM CNR Milano, Universita degli studi dell'Insubria, Milano, Italy.
Dipartimento di Scienze e Tecnologie Ambientali, Biologiche e Farmaceutiche, Seconda Universita di Napoli via Vivaldi, 43, 81100 Caserta, Italy.
DBSV, Dept. of Biotechnology and Life Sciences, Università degli Studi dell'Insubria, via J.H. Dunant 3, Varese, Italy
References:
Fauvet, B., Mbefo, M.K., Fares, M.B., Desobry, C., Michael, S., Ardah, M.T., Tsika, E., Lion, N., alpha-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer (2012) J. Biol. Chem., 287, pp. 15345-1536
Bussell, R., Eliezer, D., A structural and functional role for 11-mer repeats in alpha-synuclein and other exchangeable lipid binding proteins (2003) J. Mol. Biol., 329, pp. 763-778
Giasson, B.I., Murray, I.V., Trojanowski, J.Q., Lee, V.M., A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly (2001) J. Biol. Chem., 276, pp. 2380-2386
Binolfi, A., Theillet, F.X., Selenko, P., Bacterial in-cell NMR of human alpha-synuclein: a disordered monomer by nature? (2012) Biochem. Soc. Trans., 40, pp. 950-954
Zarbiv, Y., Simhi-Haham, D., Israeli, E., Elhadi, S.A., Grigoletto, J., Sharon, R., Lysine residues at the first and second KTKEGV repeats mediate alpha-synuclein binding to membrane phospholipids (2014) Neurobiol. Dis., 70, pp. 90-98
Lokappa, S.B., Suk, J.E., Balasubramanian, A., Samanta, S., Situ, A.J., Ulmer, T.S., Sequence and membrane determinants of the random coil-helix transition of alpha-synuclein (2014) J. Mol. Biol., 426, pp. 2130-2144
Chong, S.S., Taneva, S.G., Lee, J.M., Cornell, R.B., The curvature sensitivity of a membrane-binding amphipathic helix can be modulated by the charge on a flanking region (2014) Biochemistry, 53, pp. 450-461
Moriarty, G.M., Janowska, M.K., Kang, L., Baum, J., Exploring the accessible conformations of N-terminal acetylated alpha-synuclein (2013) FEBS Lett., 587, pp. 1128-1138
Fusco, G., De Simone, A., Gopinath, T., Vostrikov, V., Vendruscolo, M., Dobson, C.M., Veglia, G., Direct observation of the three regions in alpha-synuclein that determine its membrane-bound behaviour (2014) Nat. Commun., 5, p. 3827
Vermaas, J.V., Tajkhorshid, E., Conformational heterogeneity of alpha-synuclein in membrane (2014) Biochim. Biophys. Acta
Deleersnijder, A., Gerard, M., Debyser, Z., Baekelandt, V., The remarkable conformational plasticity of alpha-synuclein: blessing or curse? (2013) Trends Mol. Med., 19, pp. 368-377
Habchi, J., Tompa, P., Longhi, S., Uversky, V.N., Introducing protein intrinsic disorder (2014) Chem. Rev., 114, pp. 6561-6588
Bartels, T., Choi, J.G., Selkoe, D.J., alpha-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation (2011) Nature, 477, pp. 107-110
Wang, W., Perovic, I., Chittuluru, J., Kaganovich, A., Nguyen, L.T., Liao, J., Auclair, J.R., Simorellis, A.K., A soluble alpha-synuclein construct forms a dynamic tetramer (2011) Proc. Natl. Acad. Sci. U.S.A., 108, pp. 17797-17802
Waudby, C.A., Camilloni, C., Fitzpatrick, A.W., Cabrita, L.D., Dobson, C.M., Vendruscolo, M., Christodoulou, J., In-cell NMR characterization of the secondary structure populations of a disordered conformation of alpha-synuclein within E. coli cells (2013) PLoS ONE, 8
Jang, A., Lee, H.J., Suk, J.E., Jung, J.W., Kim, K.P., Lee, S.J., Non-classical exocytosis of alpha-synuclein is sensitive to folding states and promoted under stress conditions (2010) J. Neurochem., 113, pp. 1263-1274
Bellani, S., Mescola, A., Ronzitti, G., Tsushima, H., Tilve, S., Canale, C., Valtorta, F., Chieregatti, E., GRP78 clustering at the cell surface of neurons transduces the action of exogenous alpha-synuclein (2014) Cell Death Differ.
Constantinescu, R., Constantinescu, A.T., Reichmann, H., Janetzky, B., Neuronal differentiation and long-term culture of the human neuroblastoma line SH-SY5Y (2007) J. Neural Transm. Suppl., pp. 17-28
Caldinelli, L., Albani, D., Pollegioni, L., One single method to produce native and Tat-fused recombinant human alpha-synuclein in Escherichia coli (2013) BMC Biotechnol., 13, p. 32
Bartels, T., Kim, N.C., Luth, E.S., Selkoe, D.J., N-alpha-acetylation of alpha-synuclein increases its helical folding propensity, GM1 binding specificity and resistance to aggregation (2014) PLoS One, 9
Mercurio, F.A., Marasco, D., Pirone, L., Scognamiglio, P.L., Pedone, E.M., Pellecchia, M., Leone, M., Heterotypic Sam-Sam association between Odin-Sam1 and Arap3-Sam: binding affinity and structural insights (2013) ChemBioChem, 14, pp. 100-106
Diana, D., Smaldone, G., De Antonellis, P., Pirone, L., Carotenuto, M., Alonzi, A., Di Gaetano, S., Fattorusso, R., Mapping functional interaction sites of human prune C-terminal domain by NMR spectroscopy in human cell lysates (2013) Chemistry
Smaldone, G., Falanga, A., Capasso, D., Guarnieri, D., Correale, S., Galdiero, M., Netti, P.A., Di Gaetano, S., GH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins (2013) Int. J. Nanomed., 8, pp. 2555-2565
Dettmer, U., Newman, A.J., Luth, E.S., Bartels, T., Selkoe, D., In vivo cross-linking reveals principally oligomeric forms of alpha-synuclein and beta-synuclein in neurons and non-neural cells (2013) J. Biol. Chem., 288, pp. 6371-6385
Scholtz, J.M., Qian, H., York, E.J., Stewart, J.M., Baldwin, R.L., Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water (1991) Biopolymers, 31, pp. 1463-1470
Masse, J.E., Keller, R., AutoLink: automated sequential resonance assignment of biopolymers from NMR data by relative-hypothesis-prioritization-based simulated logic (2005) J. Magn. Reson., 174, pp. 133-151
Farrow, N.A., Muhandiram, R., Singer, A.U., Pascal, S.M., Kay, C.M., Gish, G., Shoelson, S.E., Kay, L.E., Backbone dynamics of a free and a phosphopeptide-complexed src homology-2 domain studied by N-15 Nmr relaxation (1994) Biochemistry, 33, pp. 5984-6003
Uversky, V.N., Eliezer, D., Biophysics of Parkinson's Disease: structure and aggregation of alpha-synuclein (2009) Curr. Protein Pept. Sci., 10, pp. 483-499
Stefanovic, A.N., Stockl, M.T., Claessens, M.M., Subramaniam, V., alpha-Synuclein oligomers distinctively permeabilize complex model membranes (2014) FEBS J., 281, pp. 2838-2850
Lee, S.J., Origins and effects of extracellular alpha-synuclein: implications in Parkinson's disease (2008) J. Mol. Neurosci., 34, pp. 17-22
Eliezer, D., Kutluay, E., Bussell, R., Browne, G., Conformational properties of alpha-synuclein in its free and lipid-associated states (2001) J. Mol. Biol., 307, pp. 1061-1073
Bodner, C.R., Dobson, C.M., Bax, A., Multiple tight phospholipid-binding modes of alpha-synuclein revealed by solution NMR spectroscopy (2009) J. Mol. Biol., 390, pp. 775-790
Tompa, P., Fuxreiter, M., Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions (2008) Trends Biochem. Sci., 33, pp. 2-8
Insight into conformational modification of alpha-synuclein in the presence of neuronal whole cells and of their isolated membranes
Abstract A change in the conformational plasticity of α-Synuclein (α-Syn) is hypothesised to be a key step in the pathogenic mechanism of Parkinson's disease (PD). Here, we report the study of extracellular α-Syn interaction with whole cells and membranes isolated from the neuronal SH-SY5Y cells, exploiting NMR and CD spectroscopies. In addition, the crosslinking agent DSG was used to freeze the conformational and oligomeric state of α-Syn in the presence of cells. These data, in a quasi-physiological environment, confirm the protein monomeric state with a propensity to adopt a transient alpha helical following interaction with biological membranes. © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Abstract A change in the conformational plasticity of α-Synuclein (α-Syn) is hypothesised to be a key step in the pathogenic mechanism of Parkinson's disease (PD). Here, we report the study of extracellular α-Syn interaction with whole cells and membranes isolated from the neuronal SH-SY5Y cells, exploiting NMR and CD spectroscopies. In addition, the crosslinking agent DSG was used to freeze the conformational and oligomeric state of α-Syn in the presence of cells. These data, in a quasi-physiological environment, confirm the protein monomeric state with a propensity to adopt a transient alpha helical following interaction with biological membranes. © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Insight into conformational modification of alpha-synuclein in the presence of neuronal whole cells and of their isolated membranes
Insight into conformational modification of alpha-synuclein in the presence of neuronal whole cells and of their isolated membranes
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Impact Factor: 5.696
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Farina B, Doti N, Pirone L, Malgieri G, Pedone E, Ruvo M, Fattorusso R
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McNeill A, Wu RM, Tzen KY, Aguiar PC, Arbelo JM, Barone P, Bhatia K, Barsottini O, Bonifati V, Bostantjopoulou S, Bressan R, Cossu G, Cortelli P, Felicio A, Ferraz HB, Herrera J, Houlden H, Hoexter M, Isla C, Lees A, Lorenzo-Betancor O, Mencacci NE, Pastor P, Pappata S, Pellecchia MT, Silveria-Moriyama L, Varrone A, Foltynie T, Schapira AH
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Mercurio FA, Marasco D, Pirone L, Scognamiglio PL, Pedone E, Pellecchia M, Leone M
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Malgieri G, Zaccaro L, Leone M, Bucci E, Esposito S, Baglivo I, Del Gatto A, Russo L, Scandurra R, Pedone PV, Fattorusso R, Isernia C
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Cucinotta V, Giuffrida A, Grasso G, MacCarrone G, Mazzaglia A, Messina M, Vecchio G
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Verardi R, Traaseth NJ, Shi L, Porcelli F, Monfregola L, De Luca S, Amodeo P, Veglia G, Scaloni A
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Farina B, Pirone L, Russo L, Viparelli F, Doti N, Pedone C, Pedone E, Fattorusso R
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Impact Factor: 3.129
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Diana D, Ziaco B, Scarabelli G, Pedone C, Colombo G, D'Andrea LD, Fattorusso R
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Impact Factor: 5.476
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Abbate M, Casella G, Fiore T, Grasso G, Pellerito C, Scopelliti M, Spinella A, Pellerito L
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Puglisi A, Rizzarelli E, Vecchio G, Iacovino R, Benedetti E, Pedone C, Saviano M
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Impact Factor: 2.605
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Kaczmarek K, Farina B, Zubrzak P, Jankowski S, Zimecki M, Suder P, Benedetti E, Fattorusso R, Saviano M, Zabrocki J
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Diana D, Ziaco B, Colombo G, Scarabelli G, Romanelli A, Fedone C, Fattorusso R, D'Andrea LD
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Impact Factor: 5.454
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Malgieri G, Russo L, Esposito S, Baglivo I, Zaccaro L, Pedone EM, Di Blasio B, Isernia C, Pedone PV, Fattorusso R
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Impact Factor: 9.598
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De Pinto V, Tomasello F, Messina A, Guarino F, Benz R, La Mendola D, Magrì A, Milardi D, Pappalardo G
* Determination of the conformation of the human VDAC1 N-terminal peptide, a protein moiety essential for the functional properties of the pore (470 views)
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Impact Factor: 3.446
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Milardi D, Arnesano F, Grasso G, Magrì A, Tabbì G, Scintilla S, Natile G, Rizzarelli E
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Impact Factor: 10.031
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De Capua A, Goodman M, Amino Y, Saviano M, Benedetti E
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Impact Factor: 4.1
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D'Andrea LD, Iaccarino G, Fattorusso R, Sorriento D, Carannante C, Capasso D, Trimarco B, Pedone C
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Falcigno L, Oliva R, D'Auria G, Maletta M, Dettin M, Pasquato A, Di Bello C, Paolillo L
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Lombardi A, Nastri F, Marasco D, Maglio O, De Sanctis G, Sinibaldi F, Santucci R, Coletta M, Pavone V
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Impact Factor: 4.353
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Oliva R, Falcigno L, D'Auria G, Dettin M, Scarinci C, Pasquato A, Di Bello C, Paolillo L
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Oliva R, Falcigno L, D'Auria G, Dettin M, Scarinci C, Pasquato A, Di Bello C, Paolillo L
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Isernia C, Bucci E, Leone M, Zaccaro L, Di Lello P, Digilio G, Esposito S, Saviano M, Di Blasio B, Pedone C, Pedone PV, Fattorusso R
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Saviano G, Rossi F, Benedetti E, Pedone C, Mierke DF, Maione A, Zanotti G, Tancredi T, Saviano M
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Zanotti G, Falcigno L, Saviano M, D'Auria G, Bruno BM, Campanile T, Paolillo L
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Impact Factor: 4.614
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Impellizzeri G, Pappalardo G, Purrello R, Rizzarelli E, Santoro AM
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Impact Factor: 5.153
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D'Auria G, Maglio O, Nastri F, Lombardi A, Mazzeo M, Morelli G, Paolillo L, Pedone C, Pavone V
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* NMR spectroscopy in the conformational analysis of peptides: an overview (91 views)
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Mercurio FA, Di Natale C, Pirone L, Vincenzi M, Marasco D, De Luca S, Pedone EM, Leone M
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Impact Factor: 5.476
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Calvanese L, Foca A, Sandomenico A, Foca G, Caporale A, Doti N, Iaccarino E, Leonardi A, D'Auria G, Ruvo M, Falcigno L
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Cavallari E, Carrera C, Aime S, Reineri F
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Celentano V, Diana D, Di Salvo C, De Rosa L, Romanelli A, Fattorusso R, D'Andrea LD
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Farina B, De Paola I, Russo L, Capasso D, Liguoro A, Gatto AD, Saviano M, Pedone PV, Di Gaetano S, Malgieri G, Zaccaro L, Fattorusso R
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Bottini A, Wu B, Barile E, De SK, Leone M, Pellecchia M
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Impact Factor: 5.696
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Farina B, Doti N, Pirone L, Malgieri G, Pedone E, Ruvo M, Fattorusso R
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Impact Factor: 3.191
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McNeill A, Wu RM, Tzen KY, Aguiar PC, Arbelo JM, Barone P, Bhatia K, Barsottini O, Bonifati V, Bostantjopoulou S, Bressan R, Cossu G, Cortelli P, Felicio A, Ferraz HB, Herrera J, Houlden H, Hoexter M, Isla C, Lees A, Lorenzo-Betancor O, Mencacci NE, Pastor P, Pappata S, Pellecchia MT, Silveria-Moriyama L, Varrone A, Foltynie T, Schapira AH
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Impact Factor: 3.534
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Mercurio FA, Marasco D, Pirone L, Scognamiglio PL, Pedone E, Pellecchia M, Leone M
* Heterotypic Sam-Sam Association Between Odin-Sam1 And Arap3-Sam: Binding Affinity And Structural Insights (372 views)
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Impact Factor: 2.92
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Malgieri G, Zaccaro L, Leone M, Bucci E, Esposito S, Baglivo I, Del Gatto A, Russo L, Scandurra R, Pedone PV, Fattorusso R, Isernia C
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Impact Factor: 2.87
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Cucinotta V, Giuffrida A, Grasso G, MacCarrone G, Mazzaglia A, Messina M, Vecchio G
* Diaminotrehalose-capped β-cyclodextrin, a new member of hemispherodextrins: Synthesis, thermodynamic and spectroscopic characterization and its exploitation in chiral electrokinetic chromatography (400 views)
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Impact Factor: 2.733
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Verardi R, Traaseth NJ, Shi L, Porcelli F, Monfregola L, De Luca S, Amodeo P, Veglia G, Scaloni A
* Probing membrane topology of the antimicrobial peptide distinctin by solid-state NMR spectroscopy in zwitterionic and charged lipid bilayers (486 views)
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Impact Factor: 3.99
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Farina B, Pirone L, Russo L, Viparelli F, Doti N, Pedone C, Pedone E, Fattorusso R
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Impact Factor: 3.129
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Diana D, Ziaco B, Scarabelli G, Pedone C, Colombo G, D'Andrea LD, Fattorusso R
* Structural analysis of a helical peptide unfolding pathway (461 views)
Chemistry (ISSN: 1521-3765, 0947-6539, 1521-3765electronic), 2010 May 10; 16(18): 5400-5407.
Impact Factor: 5.476
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Abbate M, Casella G, Fiore T, Grasso G, Pellerito C, Scopelliti M, Spinella A, Pellerito L
* Structural characterization of triorganotin(IV) complexes with sodium fusidate and DFT calculations (377 views)
J Organomet Chem (ISSN: 0022-328x), 2010 May 1; 695(9): 1405-1413.
Impact Factor: 2.205
View Export to BibTeX Export to EndNote
Puglisi A, Rizzarelli E, Vecchio G, Iacovino R, Benedetti E, Pedone C, Saviano M
* Crystal And Molecular Structure Of Beta-Cyclodextrins Functionalized With The Anti-Inflammatory Drug Etodolac (416 views)
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Impact Factor: 2.605
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Kaczmarek K, Farina B, Zubrzak P, Jankowski S, Zimecki M, Suder P, Benedetti E, Fattorusso R, Saviano M, Zabrocki J
* Synthesis, conformational analysis and immunological activity of β3Phe-substituted Cyclolinopeptide A analogues (460 views)
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Impact Factor: 1.807
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Diana D, Ziaco B, Colombo G, Scarabelli G, Romanelli A, Fedone C, Fattorusso R, D'Andrea LD
* Structural determinants of the unusual helix stability of a de novo engineered vascular endothelial growth factor (VEGF) mimicking peptide (470 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2008; 14(14): 4164-4166.
Impact Factor: 5.454
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Malgieri G, Russo L, Esposito S, Baglivo I, Zaccaro L, Pedone EM, Di Blasio B, Isernia C, Pedone PV, Fattorusso R
* The Prokaryotic Cys2his2 Zinc Finger Domain Adopts A Novel Fold As Revealed By The Solution Structure Of Agrobacterium Tumefaciens Ros Dna Binding Domain (462 views)
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Impact Factor: 9.598
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De Pinto V, Tomasello F, Messina A, Guarino F, Benz R, La Mendola D, Magrì A, Milardi D, Pappalardo G
* Determination of the conformation of the human VDAC1 N-terminal peptide, a protein moiety essential for the functional properties of the pore (470 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2007 May 7; 8(7): 744-756.
Impact Factor: 3.446
View Export to BibTeX Export to EndNote
Milardi D, Arnesano F, Grasso G, Magrì A, Tabbì G, Scintilla S, Natile G, Rizzarelli E
* Ubiquitin stability and the Lys63-linked polyubiquitination site are compromised on copper binding (378 views)
Angew Chem Int Ed (ISSN: 1433-7851, 1521-3773electronic, 1433-7851linking), 2007; 46(42): 7993-7995.
Impact Factor: 10.031
View Export to BibTeX Export to EndNote
De Capua A, Goodman M, Amino Y, Saviano M, Benedetti E
* Conformation analysis of aspartame-based sweeteners by NMR spectroscopy, molecular dynamics simulations, and X-ray diffraction studies (614 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2006 Feb; 7(2): 377-387.
Impact Factor: 4.1
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D'Andrea LD, Iaccarino G, Fattorusso R, Sorriento D, Carannante C, Capasso D, Trimarco B, Pedone C
* Targeting angiogenesis: Structural characterization and biological properties of a de novo engineered VEGF mimicking peptide (653 views)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2005 Oct 4; 102(40): 14215-14220.
Impact Factor: 10.231
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Falcigno L, Oliva R, D'Auria G, Maletta M, Dettin M, Pasquato A, Di Bello C, Paolillo L
* Structural investigation of the HIV-1 envelope glycoprotein gp160 cleavage site 3: Role of site-specific mutations (419 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2004 Dec 3; 5(12): 1653-1661.
Impact Factor: 3.474
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Lombardi A, Nastri F, Marasco D, Maglio O, De Sanctis G, Sinibaldi F, Santucci R, Coletta M, Pavone V
* Design of a new mimochrome with unique topology (534 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2003 Nov 21; 9(22): 5643-5654.
Impact Factor: 4.353
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Oliva R, Falcigno L, D'Auria G, Dettin M, Scarinci C, Pasquato A, Di Bello C, Paolillo L
* Structural investigation of the HIV-1 envelope glycoprotein gp160 cleavage site (361 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2003 Sep 4; 4(8): 727-733.
Impact Factor: 3.992
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Oliva R, Falcigno L, D'Auria G, Dettin M, Scarinci C, Pasquato A, Di Bello C, Paolillo L
* Structural investigation of the HIV-1 envelope glycoprotein gp160 cleavage site, 2: relevance of an N-terminal helix (360 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2003 Aug 4; 4(8): 727-733.
Impact Factor: 2.92
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Isernia C, Bucci E, Leone M, Zaccaro L, Di Lello P, Digilio G, Esposito S, Saviano M, Di Blasio B, Pedone C, Pedone PV, Fattorusso R
* NMR structure of the single QALGGH zinc finger domain from the Arabidopsis thaliana SUPERMAN protein (429 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2003 Mar 3; 4(2-3): 171-180.
Impact Factor: 3.992
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Saviano G, Rossi F, Benedetti E, Pedone C, Mierke DF, Maione A, Zanotti G, Tancredi T, Saviano M
* Structural consequences of metal complexation of cyclo[Pro-Phe-Phe-Ala-Xaa]2 decapeptides (447 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2001 Mar 16; 7(6): 1176-1183.
Impact Factor: 4.614
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Zanotti G, Falcigno L, Saviano M, D'Auria G, Bruno BM, Campanile T, Paolillo L
* Solid state and solution conformation of [Ala7]-phalloidin: A synthetic phallotoxin analogue (463 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2001; 7(7): 1479-1485.
Impact Factor: 4.614
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Impellizzeri G, Pappalardo G, Purrello R, Rizzarelli E, Santoro AM
Synthesis, spectroscopic characterisation, and metal ion interaction of a new α-helical peptide (490 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 1998; 4(9): 1791-1798.
Impact Factor: 5.153
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D'Auria G, Maglio O, Nastri F, Lombardi A, Mazzeo M, Morelli G, Paolillo L, Pedone C, Pavone V
Hemoprotein models based on a covalent helix-heme-helix sandwich: 2. Structural characterization of Co(III) mimochrome I Δ and Λ isomers (486 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 1997; 3(3): 350-362.
Impact Factor: 4.828
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43 Records (42 excluding Abstracts).
Total impact factor: 184.68 (181.146 excluding Abstracts).
Total 5 year impact factor: 187.521 (183.506 excluding Abstracts).
Total impact factor: 184.68 (181.146 excluding Abstracts).
Total 5 year impact factor: 187.521 (183.506 excluding Abstracts).
435 views. Last view on Wednesday 29 March 2023, 10:19:09
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