The role of copper(II) in the aggregation of human amylin (492 views)
Metallomics (ISSN: 1756-5901, 1756-591x), 2014 Oct; 6(10): 1841-1852.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 3.585, 5-year impact factor: 3.98
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84907659448&partnerID=40&md5=45025b6b5331134d91f82421df3e169c
Keywords: Amylin, Chymotrypsin, Copper Ion, Elastase, Subtilisin, Thioflavine, Article, Carbon Nuclear Magnetic Resonance, Cell Viability, Circular Dichroism, Conformational Transition, Controlled Study, Deuterium Hydrogen Exchange, High Performance Liquid Chromatography, Human, Human Cell, Human Cell Culture, In Vitro Study, Mass Spectrometry, Molecular Weight, Mtt Assay, Protein Conformation, Protein Degradation, Protein Secondary Structure, Amino Acid Sequence, Cell Line, Tumor, Cell Survival, Metabolism, Islet Amyloid Polypeptide, Chemistry, Models, Molecular Sequence Data, Protein Aggregates, Protein Structure, Proteolysis,
Affiliations:
*** IBB - CNR ***
Dottorato Internazionale in Biomedicina Traslazionale, Universita degli Studi di Catania, Viale Andrea Doria 6, 95125, Catania, Italy.,
Istituto Biostrutture e Bioimmagini, CNR, Via P. Gaifami 18Catania, Italy
Dipartimento di Scienze Chimiche, Università Degli Studi di Catania, Viale Andrea Doria 6Catania, Italy
School of Chemistry, University of Nottingham, University ParkNottingham, United Kingdom
Istituto Nazionale di Biostrutture e Biosistemi (INBB) - Sez. Biomolecole, Consorzio Interuniversitario, Viale medaglie d'Oro 305Rome, Italy
References:
Giuffrida, M.L., Caraci, F., Pignataro, B., Cataldo, S., De Bona, P., Bruno, V., Molinaro, G., Copani, A., Beta-amyloid monomers are neuroprotective (2009) J. Neurosci., 29, pp. 10582-1058
De Toma, A.S., Salamekh, S., Ramamoorthy, A., Lim, M.H., Misfolded proteins in Alzheimer's disease and type II diabetes (2012) Chem. Soc. Rev., 41, pp. 608-621
Phillips, L.K., Horowitz, M., Amylin (2006) Curr. Opin. Endocrinol. Diabetes, 13, pp. 191-198
Cao, P., Abedini, A., Raleigh, D.P., Aggregation of islet amyloid polypeptide: From physical chemistry to cell biology (2013) Curr. Opin. Struct. Biol., 23, pp. 82-89
Westermark, P., Andersson, A., Westermark, G.T., Islet amyloid polypeptide, islet amyloid and diabetes mellitus (2011) Physiol. Rev., 91, pp. 795-826
Westermark, P., Engström, U., Johnson, K.H., Westermark, G.T., Betsholtz, C., Islet amyloid polypeptide: Pinpointing amino acid residues linked to amyloid fibril formation (1990) Proc. Natl. Acad. Sci. U. S. A., 87, pp. 5036-5040
Konarkowska, B., Aitken, J.F., Kistler, J., Zhang, S., Cooper, G.J., The aggregation potential of human amylin determines its cytotoxicity towards islet beta-cells (2006) FEBS J., 273, pp. 3614-3624
Dupuis, N.F., Wu, C., Shea, J.-E., Bowers, M.T., The amyloid formation mechanism in human IAPP: Dimers have β-strand monomer-monomer interfaces (2011) J. Am. Chem. Soc., 133, pp. 7240-7243
Sedman, V.L., Allen, S., Chan, W.C., Davies, M.C., Roberts, C.J., Tendler, S.J., Williams, P.M., Atomic force microscopy study of human amylin (20-29) fibrils (2005) Protein Pept. Lett., 12, pp. 79-83
Pappalardo, G., Milardi, D., Magrì, A., Attanasio, F., Impellizzeri, G., La Rosa, C., Grasso, D., Rizzarelli, E., Environmental factors differently affect human and rat IAPP: Conformational preferences and membrane interactions of IAPP17-29 peptide derivatives (2007) Chemistry, 13, pp. 10204-10215
Alexandrescu, A.T., Amyloid accomplices and enforcers (2005) Protein Sci., 14, pp. 1-12
Jha, S., Patil, S.M., Gibson, J., Nelson, C.E., Alder, N.N., Alexandrescu, A.T., Mechanism of amylin fibrillization enhancement by heparin (2011) J. Biol. Chem., 286, pp. 22894-22904
Mirhashemi, S.M., Aarabi, M.H., Effect of two herbal polyphenol compounds on human amylin amyloid formation and destabilization (2012) J. Med. Plants Res., 6, pp. 3207-3212
Chien, V., Aitken, J.F., Zhang, S., Buchanan, C.M., Hickey, A., Brittain, T., Cooper, G.J.S., Loomes, K.M., The chaperone proteins HSP70, HSP40/DnaJ and GRP78/BiP suppress misfolding and formation of β-sheet-containing aggregates by human amylin: A potential role for defective chaperone biology in type 2 diabetes (2010) Biochem. J., 432, pp. 113-121
Cheng, B., Gong, H., Li, X., Sun, Y., Zhang, X., Chen, H., Liu, X., Huang, K., Silibinin inhibits the toxic aggregation of human islet amyloid polypeptide (2012) Biochem. Biophys. Res. Commun., 419, pp. 495-499
Tu, L.H., Raleigh, D.P., Role of aromatic interactions in amyloid formation by islet amyloid polypeptide (2013) Biochemistry, 52, pp. 333-342
Kamihira-Ishijima, M., Nakazawa, H., Kira, A., Naito, A., Nakayama, T., Inhibitory mechanism of pancreatic amyloid fibril formation: Formation of the complex between tea catechins and the fragment of residues 22-27 (2012) Biochemistry, 51, pp. 10167-10174
Cao, P., Raleigh, D.P., Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanols (2012) Biochemistry, 51, pp. 2670-2683
Cheng, B., Liu, X., Gong, H., Huang, L., Chen, H., Zhang, X., Li, C., Huang, K., Coffee components inhibit amyloid formation of human islet amyloid polypeptide in vitro: Possible link between coffee consumption and diabetes mellitus (2011) J. Agric. Food Chem., 59, pp. 13147-13155
Pannuzzo, M., Raudino, A., Milardi, D., La Rosa, C., Karttunen, M., α-helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes (2013) Sci. Rep., 3, p. 2781
Sciacca, M.F.M., Milardi, D., Messina, G.M.L., Marletta, G., Brender, J.R., Ramamoorthy, A., La Rosa, C., Cations as switches of amyloid-mediated membrane disruption mechanisms: Calcium and IAPP (2013) Biophys. J., 104, pp. 173-184
Brender, J.R., Hartman, K., Nanga, R.P., Popovych, N., De La Salud Bea, R., Vivekanandan, S., Marsh, E.N., Ramamoorthy, A., Role of zinc in human islet amyloid polypeptide aggregation (2010) J. Am. Chem. Soc., 132, pp. 8973-8983
Ward, B., Walker, K., Exley, C., Copper(ii) inhibits the formation of amylin amyloid in vitro (2008) J. Inorg. Biochem., 102, pp. 371-375
Yu, Y.P., Lei, P., Hu, J., Wu, W.H., Zhao, Y.F., Li, Y.M., Copper-induced cytotoxicity: Reactive oxygen species or islet amyloid polypeptide oligomer formation (2010) Chem. Commun., 46, pp. 6909-6911
Kállay, C., Dávid, A., Timári, S., Nagy, E.M., Sanna, D., Garribba, E., Micera, G., Sóvágó, I., Copper(ii) complexes of rat amylin fragments (2011) Dalton Trans., 40, pp. 9711-9721
Lemaire, K., Ravier, M.A., Schraenen, A., Creemers, J.W.M., Van De Plas, R., Granvik, M., Van Lommel, L., Schuit, F.C., Insulin crystallization depends on zinc transporter ZnT8 expression, but is not required for normal glucose homeostasis in mice (2009) Proc. Natl. Acad. Sci. U. S. A., 106, pp. 14872-14877
Masad, A., Hayes, L., Tabner, B.J., Turnbull, S., Cooper, L.J., Fullwood, N.J., German, M.J., Allsop, D., Copper-mediated formation of hydrogen peroxide from the amylin peptide: A novel mechanism for degeneration of islet cells in type-2 diabetes mellitus? (2007) FEBS Lett., 581, pp. 3489-3493
House, C.E.E., Patel, T., Wu, L., Fraser, P.E., Human pro-islet amyloid polypeptide (ProIAPP1-48) forms amyloid fibrils and amyloid spherulites in vitro (2010) J. Inorg. Biochem., 104, pp. 1125-1129
Bellia, F., Grasso, G., The role of copper(ii) and zinc(ii) in the degradation of human and murine IAPP by insulin-degrading enzyme (2014) J. Mass Spectrom., 49, pp. 274-279
Kim, M.J., Kim, H.T., Investigation of the copper binding site on the human islet amyloid polypeptide hormone (2012) Eur. J. Mass Spectrom., 18, pp. 51-58
Bennett, R.G., Duckworth, W.C., Hamel, F.G., Degradation of amylin by insulin-degrading enzyme (2000) J. Biol. Chem., 275, pp. 36621-36625
Guan, H., Chow, K.M., Shah, R., Rhodes, C.J., Hersh, L.B., Degradation of islet amyloid polypeptide by neprilysin (2012) Diabetologia, 55, pp. 2989-2998
Aston-Mourney, K., Zraika, S., Udayasankar, J., Subramanian, S.L., Green, P.S., Kahn, S.E., Hull, R.L., Matrix metalloproteinase-9 reduces islet amyloid formation by degrading islet amyloid polypeptide (2013) J. Biol. Chem., 288, pp. 3553-3559
Grasso, G., Salomone, F., Tundo, G.R., Pappalardo, G., Ciaccio, C., Spoto, G., Pietropaolo, A., Rizzarelli, E., Metal ions affect insulin-degrading enzyme activity (2012) J. Inorg. Biochem., 117, pp. 351-358
Grasso, G., Giuffrida, M.L., Rizzarelli, E., Metal ions and proteolytic enzymes in Alzheimer's disease (2012) Metallomics, 4, pp. 937-949
Grasso, G., Pietropaolo, A., Spoto, G., Pappalardo, G., Tundo, G.R., Ciaccio, C., Coletta, M., Rizzarelli, E., Copper(i) and copper(ii) inhibit Aβ peptides proteolysis by insulin-degrading enzyme differently: Implications for metallostasis alteration in Alzheimer's disease (2011) Chemistry, 17, pp. 2752-2762
Ralat, L.A., Kalas, V., Zheng, Z.Z., Goldman, R.D., Sosnick, T.R., Tang, W.-J., Ubiquitin is a novel substrate for human insulin-degrading enzyme (2011) J. Mol. Biol., 406, pp. 454-466
Bellia, F., Pietropaolo, A., Grasso, G., Formation of insulin fragments by insulin-degrading enzyme: The role of zinc(ii) and cystine bridges (2013) J. Mass Spectrom., 48, pp. 135-140
Grasso, G., Rizzarelli, E., Spoto, G., How the binding and degrading capabilities of insulin degrading enzyme are affected by ubiquitin (2008) Biochim. Biophys. Acta, Proteins Proteomics, 1784, pp. 1122-1126
Ciaccio, C., Tundo, G.F., Grasso, G., Spoto, G., Marasco, D., Ruvo, M., Gioia, M., Coletta, M., Somatostatin: A novel substrate and a modulator of insulin degrading enzyme activity (2009) J. Mol. Biol., 385, pp. 1556-1567
Shen, Y., Joachimiak, A., Rosner, M.R., Tang, W.-J., Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism (2006) Nature, 443, pp. 870-874
Guo, Q., Manolopoulou, M., Bian, Y., Schilling, A.B., Tang, W.-J., Molecular basis for the recognition and cleavages of IGF-II, TGF-α, and amylin by human insulin-degrading enzyme (2010) J. Mol. Biol., 395, pp. 430-443
Williams, N.R., Rajput-Williams, J., West, J.A., Nigdikar, S.V., Foote, J.W., Howard, A.N., Plasma, granulocyte and mononuclear cell copper and zinc in patients with diabetes mellitus (1995) Analyst, 120, pp. 887-890
Fu, W., Patel, A., Jhamandas, J.H., Amylin receptor: A common pathophysiological target in Alzheimer's disease and diabetes mellitus (2013) Front. Aging Neurosci., 42, pp. 1-4
Madine, J., Jack, E., Stockley, P.G., Radford, S.E., Serpell, L.C., Middleton, D.A., Structural insights into the polymorphism of amyloid-like fibrils formed by region 20-29 of amylin revealed by solid-state NMR and x-ray fiber diffraction (2008) J. Am. Chem. Soc., 130, pp. 14990-15001
Giuffrida, M. L., Caraci, F., Pignataro, B., Cataldo, S., De Bona, P., Bruno, V., Molinaro, G., Copani, A., Beta-amyloid monomers are neuroprotective (2009) J. Neurosci., 29, pp. 10582-1058
De Toma, A. S., Salamekh, S., Ramamoorthy, A., Lim, M. H., Misfolded proteins in Alzheimer's disease and type II diabetes (2012) Chem. Soc. Rev., 41, pp. 608-621
Phillips, L. K., Horowitz, M., Amylin (2006) Curr. Opin. Endocrinol. Diabetes, 13, pp. 191-198
Dupuis, N. F., Wu, C., Shea, J. -E., Bowers, M. T., The amyloid formation mechanism in human IAPP: Dimers have -strand monomer-monomer interfaces (2011) J. Am. Chem. Soc., 133, pp. 7240-7243
Sedman, V. L., Allen, S., Chan, W. C., Davies, M. C., Roberts, C. J., Tendler, S. J., Williams, P. M., Atomic force microscopy study of human amylin (20-29) fibrils (2005) Protein Pept. Lett., 12, pp. 79-83
Alexandrescu, A. T., Amyloid accomplices and enforcers (2005) Protein Sci., 14, pp. 1-12
Jha, S., Patil, S. M., Gibson, J., Nelson, C. E., Alder, N. N., Alexandrescu, A. T., Mechanism of amylin fibrillization enhancement by heparin (2011) J. Biol. Chem., 286, pp. 22894-22904
Mirhashemi, S. M., Aarabi, M. H., Effect of two herbal polyphenol compounds on human amylin amyloid formation and destabilization (2012) J. Med. Plants Res., 6, pp. 3207-3212
Tu, L. H., Raleigh, D. P., Role of aromatic interactions in amyloid formation by islet amyloid polypeptide (2013) Biochemistry, 52, pp. 333-342
Sciacca, M. F. M., Milardi, D., Messina, G. M. L., Marletta, G., Brender, J. R., Ramamoorthy, A., La Rosa, C., Cations as switches of amyloid-mediated membrane disruption mechanisms: Calcium and IAPP (2013) Biophys. J., 104, pp. 173-184
Brender, J. R., Hartman, K., Nanga, R. P., Popovych, N., De La Salud Bea, R., Vivekanandan, S., Marsh, E. N., Ramamoorthy, A., Role of zinc in human islet amyloid polypeptide aggregation (2010) J. Am. Chem. Soc., 132, pp. 8973-8983
Yu, Y. P., Lei, P., Hu, J., Wu, W. H., Zhao, Y. F., Li, Y. M., Copper-induced cytotoxicity: Reactive oxygen species or islet amyloid polypeptide oligomer formation (2010) Chem. Commun., 46, pp. 6909-6911
K llay, C., D vid, A., Tim ri, S., Nagy, E. M., Sanna, D., Garribba, E., Micera, G., S v g, I., Copper (ii) complexes of rat amylin fragments (2011) Dalton Trans., 40, pp. 9711-9721
House, C. E. E., Patel, T., Wu, L., Fraser, P. E., Human pro-islet amyloid polypeptide (ProIAPP1-48) forms amyloid fibrils and amyloid spherulites in vitro (2010) J. Inorg. Biochem., 104, pp. 1125-1129
Kim, M. J., Kim, H. T., Investigation of the copper binding site on the human islet amyloid polypeptide hormone (2012) Eur. J. Mass Spectrom., 18, pp. 51-58
Bennett, R. G., Duckworth, W. C., Hamel, F. G., Degradation of amylin by insulin-degrading enzyme (2000) J. Biol. Chem., 275, pp. 36621-36625
Guan, H., Chow, K. M., Shah, R., Rhodes, C. J., Hersh, L. B., Degradation of islet amyloid polypeptide by neprilysin (2012) Diabetologia, 55, pp. 2989-2998
Ralat, L. A., Kalas, V., Zheng, Z. Z., Goldman, R. D., Sosnick, T. R., Tang, W. -J., Ubiquitin is a novel substrate for human insulin-degrading enzyme (2011) J. Mol. Biol., 406, pp. 454-466
Williams, N. R., Rajput-Williams, J., West, J. A., Nigdikar, S. V., Foote, J. W., Howard, A. N., Plasma, granulocyte and mononuclear cell copper and zinc in patients with diabetes mellitus (1995) Analyst, 120, pp. 887-890
Metallomics (ISSN: 1756-5901, 1756-591x), 2014 Oct; 6(10): 1841-1852.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 3.585, 5-year impact factor: 3.98
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84907659448&partnerID=40&md5=45025b6b5331134d91f82421df3e169c
Keywords: Amylin, Chymotrypsin, Copper Ion, Elastase, Subtilisin, Thioflavine, Article, Carbon Nuclear Magnetic Resonance, Cell Viability, Circular Dichroism, Conformational Transition, Controlled Study, Deuterium Hydrogen Exchange, High Performance Liquid Chromatography, Human, Human Cell, Human Cell Culture, In Vitro Study, Mass Spectrometry, Molecular Weight, Mtt Assay, Protein Conformation, Protein Degradation, Protein Secondary Structure, Amino Acid Sequence, Cell Line, Tumor, Cell Survival, Metabolism, Islet Amyloid Polypeptide, Chemistry, Models, Molecular Sequence Data, Protein Aggregates, Protein Structure, Proteolysis,
Affiliations:
*** IBB - CNR ***
Dottorato Internazionale in Biomedicina Traslazionale, Universita degli Studi di Catania, Viale Andrea Doria 6, 95125, Catania, Italy.,
Istituto Biostrutture e Bioimmagini, CNR, Via P. Gaifami 18Catania, Italy
Dipartimento di Scienze Chimiche, Università Degli Studi di Catania, Viale Andrea Doria 6Catania, Italy
School of Chemistry, University of Nottingham, University ParkNottingham, United Kingdom
Istituto Nazionale di Biostrutture e Biosistemi (INBB) - Sez. Biomolecole, Consorzio Interuniversitario, Viale medaglie d'Oro 305Rome, Italy
References:
Giuffrida, M.L., Caraci, F., Pignataro, B., Cataldo, S., De Bona, P., Bruno, V., Molinaro, G., Copani, A., Beta-amyloid monomers are neuroprotective (2009) J. Neurosci., 29, pp. 10582-1058
De Toma, A.S., Salamekh, S., Ramamoorthy, A., Lim, M.H., Misfolded proteins in Alzheimer's disease and type II diabetes (2012) Chem. Soc. Rev., 41, pp. 608-621
Phillips, L.K., Horowitz, M., Amylin (2006) Curr. Opin. Endocrinol. Diabetes, 13, pp. 191-198
Cao, P., Abedini, A., Raleigh, D.P., Aggregation of islet amyloid polypeptide: From physical chemistry to cell biology (2013) Curr. Opin. Struct. Biol., 23, pp. 82-89
Westermark, P., Andersson, A., Westermark, G.T., Islet amyloid polypeptide, islet amyloid and diabetes mellitus (2011) Physiol. Rev., 91, pp. 795-826
Westermark, P., Engström, U., Johnson, K.H., Westermark, G.T., Betsholtz, C., Islet amyloid polypeptide: Pinpointing amino acid residues linked to amyloid fibril formation (1990) Proc. Natl. Acad. Sci. U. S. A., 87, pp. 5036-5040
Konarkowska, B., Aitken, J.F., Kistler, J., Zhang, S., Cooper, G.J., The aggregation potential of human amylin determines its cytotoxicity towards islet beta-cells (2006) FEBS J., 273, pp. 3614-3624
Dupuis, N.F., Wu, C., Shea, J.-E., Bowers, M.T., The amyloid formation mechanism in human IAPP: Dimers have β-strand monomer-monomer interfaces (2011) J. Am. Chem. Soc., 133, pp. 7240-7243
Sedman, V.L., Allen, S., Chan, W.C., Davies, M.C., Roberts, C.J., Tendler, S.J., Williams, P.M., Atomic force microscopy study of human amylin (20-29) fibrils (2005) Protein Pept. Lett., 12, pp. 79-83
Pappalardo, G., Milardi, D., Magrì, A., Attanasio, F., Impellizzeri, G., La Rosa, C., Grasso, D., Rizzarelli, E., Environmental factors differently affect human and rat IAPP: Conformational preferences and membrane interactions of IAPP17-29 peptide derivatives (2007) Chemistry, 13, pp. 10204-10215
Alexandrescu, A.T., Amyloid accomplices and enforcers (2005) Protein Sci., 14, pp. 1-12
Jha, S., Patil, S.M., Gibson, J., Nelson, C.E., Alder, N.N., Alexandrescu, A.T., Mechanism of amylin fibrillization enhancement by heparin (2011) J. Biol. Chem., 286, pp. 22894-22904
Mirhashemi, S.M., Aarabi, M.H., Effect of two herbal polyphenol compounds on human amylin amyloid formation and destabilization (2012) J. Med. Plants Res., 6, pp. 3207-3212
Chien, V., Aitken, J.F., Zhang, S., Buchanan, C.M., Hickey, A., Brittain, T., Cooper, G.J.S., Loomes, K.M., The chaperone proteins HSP70, HSP40/DnaJ and GRP78/BiP suppress misfolding and formation of β-sheet-containing aggregates by human amylin: A potential role for defective chaperone biology in type 2 diabetes (2010) Biochem. J., 432, pp. 113-121
Cheng, B., Gong, H., Li, X., Sun, Y., Zhang, X., Chen, H., Liu, X., Huang, K., Silibinin inhibits the toxic aggregation of human islet amyloid polypeptide (2012) Biochem. Biophys. Res. Commun., 419, pp. 495-499
Tu, L.H., Raleigh, D.P., Role of aromatic interactions in amyloid formation by islet amyloid polypeptide (2013) Biochemistry, 52, pp. 333-342
Kamihira-Ishijima, M., Nakazawa, H., Kira, A., Naito, A., Nakayama, T., Inhibitory mechanism of pancreatic amyloid fibril formation: Formation of the complex between tea catechins and the fragment of residues 22-27 (2012) Biochemistry, 51, pp. 10167-10174
Cao, P., Raleigh, D.P., Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanols (2012) Biochemistry, 51, pp. 2670-2683
Cheng, B., Liu, X., Gong, H., Huang, L., Chen, H., Zhang, X., Li, C., Huang, K., Coffee components inhibit amyloid formation of human islet amyloid polypeptide in vitro: Possible link between coffee consumption and diabetes mellitus (2011) J. Agric. Food Chem., 59, pp. 13147-13155
Pannuzzo, M., Raudino, A., Milardi, D., La Rosa, C., Karttunen, M., α-helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes (2013) Sci. Rep., 3, p. 2781
Sciacca, M.F.M., Milardi, D., Messina, G.M.L., Marletta, G., Brender, J.R., Ramamoorthy, A., La Rosa, C., Cations as switches of amyloid-mediated membrane disruption mechanisms: Calcium and IAPP (2013) Biophys. J., 104, pp. 173-184
Brender, J.R., Hartman, K., Nanga, R.P., Popovych, N., De La Salud Bea, R., Vivekanandan, S., Marsh, E.N., Ramamoorthy, A., Role of zinc in human islet amyloid polypeptide aggregation (2010) J. Am. Chem. Soc., 132, pp. 8973-8983
Ward, B., Walker, K., Exley, C., Copper(ii) inhibits the formation of amylin amyloid in vitro (2008) J. Inorg. Biochem., 102, pp. 371-375
Yu, Y.P., Lei, P., Hu, J., Wu, W.H., Zhao, Y.F., Li, Y.M., Copper-induced cytotoxicity: Reactive oxygen species or islet amyloid polypeptide oligomer formation (2010) Chem. Commun., 46, pp. 6909-6911
Kállay, C., Dávid, A., Timári, S., Nagy, E.M., Sanna, D., Garribba, E., Micera, G., Sóvágó, I., Copper(ii) complexes of rat amylin fragments (2011) Dalton Trans., 40, pp. 9711-9721
Lemaire, K., Ravier, M.A., Schraenen, A., Creemers, J.W.M., Van De Plas, R., Granvik, M., Van Lommel, L., Schuit, F.C., Insulin crystallization depends on zinc transporter ZnT8 expression, but is not required for normal glucose homeostasis in mice (2009) Proc. Natl. Acad. Sci. U. S. A., 106, pp. 14872-14877
Masad, A., Hayes, L., Tabner, B.J., Turnbull, S., Cooper, L.J., Fullwood, N.J., German, M.J., Allsop, D., Copper-mediated formation of hydrogen peroxide from the amylin peptide: A novel mechanism for degeneration of islet cells in type-2 diabetes mellitus? (2007) FEBS Lett., 581, pp. 3489-3493
House, C.E.E., Patel, T., Wu, L., Fraser, P.E., Human pro-islet amyloid polypeptide (ProIAPP1-48) forms amyloid fibrils and amyloid spherulites in vitro (2010) J. Inorg. Biochem., 104, pp. 1125-1129
Bellia, F., Grasso, G., The role of copper(ii) and zinc(ii) in the degradation of human and murine IAPP by insulin-degrading enzyme (2014) J. Mass Spectrom., 49, pp. 274-279
Kim, M.J., Kim, H.T., Investigation of the copper binding site on the human islet amyloid polypeptide hormone (2012) Eur. J. Mass Spectrom., 18, pp. 51-58
Bennett, R.G., Duckworth, W.C., Hamel, F.G., Degradation of amylin by insulin-degrading enzyme (2000) J. Biol. Chem., 275, pp. 36621-36625
Guan, H., Chow, K.M., Shah, R., Rhodes, C.J., Hersh, L.B., Degradation of islet amyloid polypeptide by neprilysin (2012) Diabetologia, 55, pp. 2989-2998
Aston-Mourney, K., Zraika, S., Udayasankar, J., Subramanian, S.L., Green, P.S., Kahn, S.E., Hull, R.L., Matrix metalloproteinase-9 reduces islet amyloid formation by degrading islet amyloid polypeptide (2013) J. Biol. Chem., 288, pp. 3553-3559
Grasso, G., Salomone, F., Tundo, G.R., Pappalardo, G., Ciaccio, C., Spoto, G., Pietropaolo, A., Rizzarelli, E., Metal ions affect insulin-degrading enzyme activity (2012) J. Inorg. Biochem., 117, pp. 351-358
Grasso, G., Giuffrida, M.L., Rizzarelli, E., Metal ions and proteolytic enzymes in Alzheimer's disease (2012) Metallomics, 4, pp. 937-949
Grasso, G., Pietropaolo, A., Spoto, G., Pappalardo, G., Tundo, G.R., Ciaccio, C., Coletta, M., Rizzarelli, E., Copper(i) and copper(ii) inhibit Aβ peptides proteolysis by insulin-degrading enzyme differently: Implications for metallostasis alteration in Alzheimer's disease (2011) Chemistry, 17, pp. 2752-2762
Ralat, L.A., Kalas, V., Zheng, Z.Z., Goldman, R.D., Sosnick, T.R., Tang, W.-J., Ubiquitin is a novel substrate for human insulin-degrading enzyme (2011) J. Mol. Biol., 406, pp. 454-466
Bellia, F., Pietropaolo, A., Grasso, G., Formation of insulin fragments by insulin-degrading enzyme: The role of zinc(ii) and cystine bridges (2013) J. Mass Spectrom., 48, pp. 135-140
Grasso, G., Rizzarelli, E., Spoto, G., How the binding and degrading capabilities of insulin degrading enzyme are affected by ubiquitin (2008) Biochim. Biophys. Acta, Proteins Proteomics, 1784, pp. 1122-1126
Ciaccio, C., Tundo, G.F., Grasso, G., Spoto, G., Marasco, D., Ruvo, M., Gioia, M., Coletta, M., Somatostatin: A novel substrate and a modulator of insulin degrading enzyme activity (2009) J. Mol. Biol., 385, pp. 1556-1567
Shen, Y., Joachimiak, A., Rosner, M.R., Tang, W.-J., Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism (2006) Nature, 443, pp. 870-874
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The role of copper(II) in the aggregation of human amylin
Amylin is a 37-residue peptide hormone produced by the islet beta-cells of pancreas and the formation of amylin aggregates is strongly associated with beta-cell degeneration in type 2 diabetes, as demonstrated by more than 95% of patients exhibiting amylin amyloid upon autopsy. It is widely recognized that metal ions such as copper(II) have been implicated in the aggregation process of amyloidogenic peptides such as Abeta and alpha-synuclein and there is evidence that amylin self-assembly is also largely affected by copper(II). For this reason, in this work, the role of copper(II) in the aggregation of amylin has been investigated by several different experimental approaches. Mass spectrometric investigations show that copper(II) induces significant changes in the amylin structure, which decrease the protein fibrillogenesis as observed by ThT measurements. Accordingly, solid-state NMR experiments together with computational analysis carried out on a model amylin fragment confirmed the non-fibrillogenic nature of the copper(II) induced aggregated structure. Finally, the presence of copper(II) is also shown to have a major influence on amylin proneness to be degraded by proteases and cytotoxicity studies on different cell cultures are reported.
Amylin is a 37-residue peptide hormone produced by the islet beta-cells of pancreas and the formation of amylin aggregates is strongly associated with beta-cell degeneration in type 2 diabetes, as demonstrated by more than 95% of patients exhibiting amylin amyloid upon autopsy. It is widely recognized that metal ions such as copper(II) have been implicated in the aggregation process of amyloidogenic peptides such as Abeta and alpha-synuclein and there is evidence that amylin self-assembly is also largely affected by copper(II). For this reason, in this work, the role of copper(II) in the aggregation of amylin has been investigated by several different experimental approaches. Mass spectrometric investigations show that copper(II) induces significant changes in the amylin structure, which decrease the protein fibrillogenesis as observed by ThT measurements. Accordingly, solid-state NMR experiments together with computational analysis carried out on a model amylin fragment confirmed the non-fibrillogenic nature of the copper(II) induced aggregated structure. Finally, the presence of copper(II) is also shown to have a major influence on amylin proneness to be degraded by proteases and cytotoxicity studies on different cell cultures are reported.
The role of copper(II) in the aggregation of human amylin
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The role of copper(II) in the aggregation of human amylin
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Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2000 Nov 17; 6(22): 4195-4202.
Impact Factor: 4.698
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Conato C, Contino A, Maccarrone G, Magrì A, Remelli M, Tabbì G
Copper(II) complexes with L-lysine and L-ornithine: Is the side-chain involved in the coordination? A thermodynamic and spectroscopic study (312 views)
Thermochim Acta (ISSN: 0040-6031), 2000 Nov 13; 362(1-2): 13-23.
Impact Factor: 0.807
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Lombardi A, Marasco D, Maglio O, Di Costanzo L, Nasti F, Pavone V
Miniaturized metalloproteins: Application to iron-sulfur proteins (653 views)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2000 Oct 24; 97(22): 11922-11927.
Impact Factor: 10.789
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Cucinotta V, Grasso D, Grasso G, Milardi D
Calorimetric evidences for Copper(II)-regulated chiral recognition between decanucleotide 5'd(CTGGATCCAG)2 and Ala-Trp dipeptides (394 views)
Nucleosides Nucleotides (ISSN: 0732-8311), 1997; 16(10-11): 1847-1854.
Impact Factor: 0.905
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Bonomo RP, Marchelli R, Tabbì G
Study of H2O2 interaction with copper(II) complexes with diamino-diamide type ligands, diastereoisomeric dipeptides, and tripeptides (512 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 1995 Nov 15; 60(3): 205-218.
Impact Factor: 1.342
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Fattorusso R, Morelli G, Lombardi A, Nastri F, maglio O, D'Auria G, Pedone C, Pavone V
Design of metal ion binding peptides (614 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1995; 37(6): 401-410.
Impact Factor: 2.425
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Pavone V, Lombardi A, D'Auria G, Saviano M, Nastri F, Paolillo L, Di Blasio B, Pedone C
β-Alanine containing peptides: A novel molecular tool for the design of γ-turns (813 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1992 Feb; 32(2): 173-184.
Impact Factor: 2.425
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Marchetti P, Benzi L, Trischitta V, Brunetti A, Cecchetti P, Ciccarone AM, Pezzino V, Vigneri R, Navalesi R
Complementary use of gel permeation and reversed-phase liquid chromatography for the analysis of A14-[125I]insulin and its degradation products in isolated human monocytes (1719 views)
J Chromatogr B Biomed Sci Appl (ISSN: 0378-4347), 1986 Apr 25; 377(C): 339-344.
Impact Factor: 1.588
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* Ultra-rapid glutathionylation of chymotrypsinogen in its molten globule-like conformation: A comparison to archaeal proteins (62 views)
Sci Rep (ISSN: 2045-2322linking, 2045-2322electronic), 2020 Jun 2; 10(1): 8943-8943.
Impact Factor: 3.998
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Bonaccorso C, Grasso G, Musso N, Barresi V, Condorelli DF, La Mendola D, Rizzarelli E
* Water soluble glucose derivative of thiocarbohydrazone acts as ionophore with cytotoxic effects on tumor cells (317 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 1873-3344electronic), 2018; 182: 92-102.
Impact Factor: 3.317
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Oliveri V, Lanza V, Milardi D, Viale M, Maric I, Sgarlata C, Vecchio G
* Amino- and chloro-8-hydroxyquinolines and their copper complexes as proteasome inhibitors and antiproliferative agents (462 views)
Metallomics (ISSN: 1756-5901, 1756-591x), 2017 Oct 18; 9(10): 1439-1446.
Impact Factor: 4.069
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Magrì A, Tabbì G, Breglia R, De Gioia L, Fantucci P, Bruschi M, Bonomo RP, La Mendola D
* Copper ion interaction with the RNase catalytic site fragment of the angiogenin protein: an experimental and theoretical investigation (389 views) (PDF 179 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9226linking), 2017 Jul 04; 46(26): 8524-8538.
Impact Factor: 4.099
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Mishra CB, Kumari S, Angeli A, Monti SM, Buonanno M, Tiwari M, Supuran CT
* Discovery of Benzenesulfonamides with Potent Human Carbonic Anhydrase Inhibitory and Effective Anticonvulsant Action: Design, Synthesis, and Pharmacological Assessment (831 views)
J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2017 Mar 23; 60(6): 2456-2469.
Impact Factor: 6.253
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Caporale A, Mascanzoni F, Farina B, Sturlese M, Di Sorbo G, Fattorusso R, Ruvo M, Doti N
* FRET-Protease-Coupled Peptidyl-Prolyl cis-trans Isomerase Assay: New Internally Quenched Fluorogenic Substrates for High-Throughput Screening (261 views)
J Biomol Screen (ISSN: 1087-0571, 1552-454x), 2016 Aug; 21(7): 701-712.
Impact Factor: 2.444
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Barresi V, Spampinato G, Musso N, Trovato Salinaro A, Rizzarelli E, Condorelli DF
* ATOX1 gene silencing increases susceptibility to anticancer therapy based on copper ionophores or chelating drugs (720 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2016; 156: 145-152.
Impact Factor: 3.348
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Giuffrida ML, Tomasello MF, Pandini G, Caraci F, Battaglia G, Busceti C, Di Pietro P, Pappalardo G, Attanasio F, Chiechio S, Bagnoli S, Nacmias B, Sorbi S, Vigneri R, Rizzarelli E, Nicoletti F, Copani A
* Monomeric ss-amyloid interacts with type-1 insulin-like growth factor receptors to provide energy supply to neurons (526 views)
Front Cell Neurosci (ISSN: 1662-5102), 2015 Aug 7; 9(AUGUST): 297-297.
Impact Factor: 4.609
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Giacomelli C, Trincavelli ML, Satriano C, Hansson O, La Mendola D, Rizzarelli E, Martini C
* Copper (II) ions modulate Angiogenin activity in human endothelial cells (422 views)
Int J Biochem Cell B (ISSN: 1357-2725), 2015 Mar; 60: 185-196.
Impact Factor: 3.905
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Tabbì G, Magrì A, Giuffrida A, Lanza V, Pappalardo G, Naletova I, Nicoletti VG, Attanasio F, Rizzarelli E
* Semax, an ACTH4-10 peptide analog with high affinity for copper(II) ion and protective ability against metal induced cell toxicity (462 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2015 Jan; 142: 39-46.
Impact Factor: 3.205
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Di Lorenzo F, Silipo A, Bianconi I, Lore' NI, Scamporrino A, Sturiale L, Garozzo D, Lanzetta R, Parrilli M, Bragonzi A, Molinaro A
* Persistent cystic fibrosis isolate Pseudomonas aeruginosa strain RP73 exhibits an under-acylated LPS structure responsible of its low inflammatory activity (364 views)
Mol Immunol (ISSN: 0161-5890), 2015; 63(2): 166-175.
Impact Factor: 3.375
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Altieri F, Di Stadio CS, Severino V, Sandomenico A, Minopoli G, Miselli G, Di Maro A, Ruvo M, Chambery A, Quagliariello V, Masullo M, Rippa E, Arcari P
* Anti-amyloidogenic property of human gastrokine (527 views)
Biochimie (ISSN: 0300-9084, 1638-6183, 0300-9084linking), 2014 Nov; 106C: 91-100.
Impact Factor: 2.963
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Bellia F, GrassoG
* The role of copper(II) and zinc(II) in the degradation of human and murine IAPP by insulin-degrading enzyme (535 views)
J Mass Spectrom (ISSN: 1076-5174, 1096-9888), 2014; 49(4): 274-279.
Impact Factor: 2.379
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Montefusco S, Esposito R, D'Andrea L, Monti MC, Dunne C, Dolan B, Tosco A, Marzullo L, Clyne M
* Copper promotes TFF1-mediated Helicobacter pylori colonization (518 views)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2013 Nov 13; 8(11): e79455-e79455.
Impact Factor: 3.534
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Roviello GN, Musumeci D, D'Alessandro C, Pedone C
* Synthesis of a thymine-functionalized nucleoamino acid for the solid phase assembly of cationic nucleopeptides (485 views)
Amino Acids (ISSN: 1438-2199, 0939-4451, 1438-2199electronic), 2013 Oct; 45(4): 779-784.
Impact Factor: 3.653
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Satriano C, Sfrazzetto GT, Amato ME, Ballistreri FP, Copani A, Giuffrida ML, Grasso G, Pappalardo A, Rizzarelli E, Tomaselli GA, Toscano RM
* A ratiometric naphthalimide sensor for live cell imaging of copper(i) (455 views)
Chem Commun (ISSN: 1359-7345, 1364-548x, 1364-548xelectronic), 2013 Jun 21; 49(49): 5565-5567.
Impact Factor: 6.718
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Attanasio F, Convertino M, Magno A, Caflisch A, Corazza A, Haridas H, Esposito G, Cataldo S, Pignataro B, Milardi D, Rizzarelli E
* Carnosine Inhibits Abeta(42) Aggregation By Perturbing The H-Bond Network In And Around The Central Hydrophobic Cluster (699 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2013 Mar 18; 14(5): 583-592.
Impact Factor: 3.06
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Attanasio F, De Bona P, Cataldo S, Sciacca MFM, Milardi D, Pignataro B, Pappalardo G
* Copper(II) and zinc(II) dependent effects on A beta 42 aggregation: a CD, Th-T and SFM study (456 views)
New J Chem (ISSN: 1144-0546), 2013; 37(4): 1206-1215.
Impact Factor: 3.159
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Grasso G, Salomone F, Tundo GR, Pappalardo G, Ciaccio C, Spoto G, Pietropaolo A, Coletta M, Rizzarelli E
* Metal ions affect insulin-degrading enzyme activity (479 views)
J Chem Res (ISSN: 1873-3344, 0162-0134, 0162-0134print), 2012 Dec; 117: 351-358.
Impact Factor: 3.197
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Roviello GN, Roviello G, Musumeci D, Bucci EM, Pedone C
* Dakin-West reaction on 1-thyminyl acetic acid for the synthesis of 1, 3-bis(1-thyminyl)-2-propanone, a heteroaromatic compound with nucleopeptide-binding properties (431 views)
Amino Acids (ISSN: 1438-2199, 0939-4451, 1438-2199electronic), 2012 Oct; 43(4): 1615-1623.
Impact Factor: 3.914
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Travaglia A, Pietropaolo A, La Mendola D, Nicoletti VG, Rizzarelli E
* The inorganic perspectives of neurotrophins and Alzheimer's disease (538 views)
J Chem Res (ISSN: 1873-3344, 0162-0134, 0162-0134print), 2012 Jun; 111: 130-137.
Impact Factor: 3.197
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Mercurio FA, Marasco D, Pirone L, Pedone E, Pellecchia M, Leone M
* Solution Structure of the First Sam Domain of Odin and Binding Studies with the EphA2 Receptor (465 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2012 Mar 13; 51(10): 2136-2145.
Impact Factor: 3.377
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Kállay C, Dávid A, Timári S, Nagy EM, Sanna D, Garribba E, Micera G, De Bona P, Pappalardo G, Rizzarelli E, Sóvágó I
* Copper(II) complexes of rat amylin fragments (357 views)
Dalton T (ISSN: 1477-9234, 1477-9226, 1477-9234electronic), 2011 Oct 14; 40(38): 9711-9721.
Impact Factor: 3.838
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Roviello GN, Musumeci D, Bucci EM, Pedone C
* Synthesis and characterization of a novel ester-based nucleoamino acid for the assembly of aromatic nucleopeptides for biomedical applications (529 views)
Int J Pharm (ISSN: 0378-5173, 1873-3476), 2011 Sep 30; 415(1-2): 206-210.
Impact Factor: 3.35
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La Mendola D, Magrì A, Vagliasindi LI, Hansson Ö, Bonomo RP, Rizzarelli E
* Copper(II) complex formation with a linear peptide encompassing the putative cell binding site of angiogenin (448 views)
Dalton T (ISSN: 1477-9234, 1477-9226, 1477-9234electronic), 2010 Nov 28; 39(44): 10678-10684.
Impact Factor: 3.647
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Di Natale G, Pappalardo G, Milardi D, Sciacca MF, Attanasio F, La Mendola D, Rizzarelli E
* Membrane interactions and conformational preferences of human and avian prion N-terminal tandem repeats: The role of copper(II) ions, pH, and membrane mimicking environments (494 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2010 Nov 4; 114(43): 13830-13838.
Impact Factor: 3.603
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Józsa E, Osz K, Kállay C, de Bona P, Damante CA, Pappalardo G, Rizzarelli E, Sóvágó I
* Nickel(ii) and mixed metal complexes of amyloid-β N-terminus (448 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2010 Sep 14; 39(30): 7046-7053.
Impact Factor: 3.647
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Roviello GN, Crescenzo C, Capasso D, Di Gaetano S, Franco S, Bucci EM, Pedone C
* Synthesis of a novel Fmoc-protected nucleoaminoacid for the solid phase assembly of 4-piperidyl glycine/L-arginine-containing nucleopeptides and preliminary RNA interaction studies (464 views)
Amino Acids (ISSN: 0939-4451, 1438-2199, 1438-2199electronic), 2010 Sep; 39(3): 795-800.
Impact Factor: 4.106
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La Mendola D, Magrì A, Campagna T, Campitiello MA, Raiola L, Isernia C, Hansson O, Bonomo RP, Rizzarelli E
* A doppel alpha-helix peptide fragment mimics the copper(II) interactions with the whole protein (1115 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2010 Jun 1; 16(21): 6212-6223.
Impact Factor: 5.476
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Sciacca MFM, Pappalardo M, Attanasio F, Milardi D, La Rosa C, Grasso DM
* Are fibril growth and membrane damage linked processes? An experimental and computational study of IAPP(12-18) and IAPP(21-27) peptides (401 views)
New J Chem (ISSN: 1144-0546), 2010; 34(2): 200-207.
Impact Factor: 2.631
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Jozsa E, Hosz K, Kallay C, De Bona P, Damante CA, Pappalardo G, Rizzarelli E, Sovago I
* Nickel (ii) And Mixed Metal Complexes Of Amyloid-B N-Terminus. Results Of Potentiometric And Spectroscopic Studies On The Binary Nickel (ii) And Mixed Metal Nickel (ii)-Copper (ii) And Nickel (ii)-Copper (ii)-Zinc (ii) Complexes Of Peptide Fragments (489 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2010; 39(30): 7046-7053.
Impact Factor: 3.647
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Palmieri G, Catara G, Saviano M, Langella E, Gogliettino M, Rossi M
* First archaeal PEPB-serine protease inhibitor from sulfolobus solfataricus with noncanonical amino acid sequence in the reactive-site loop (396 views)
J Proteome Res (ISSN: 1535-3893), 2009 Jan; 8(1): 327-334.
Impact Factor: 5.132
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Pappalardo M, Sciacca MFM, Milardi D, Grasso DM, La Rosa C
* Thermodynamics Of Azurin Folding: The Role Of The Copper Ion (318 views)
Journal Of Thermal Analysis And Calorimetry (ISSN: 1388-6150), 2008 Sep; 93(2): 575-581.
Impact Factor: 1.63
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Bellia F, Amorini AM, La Mendola D, Vecchio G, Tavazzi B, Giardina B, Di Pietro V, Lazzarino G, Rizzarelli E
* New glycosidic derivatives of histidine-containing dipeptides with antioxidant properties and resistant to carnosinase activity (444 views)
Eur J Med Chem (ISSN: 0223-5234, 1768-3254, 1768-3254electronic), 2008 Feb; 43(2): 373-380.
Impact Factor: 2.882
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Barone V, De Rienzo F, Langella E, Menziani MC, Rega N, Sola M
* A computational protocol to probe the role of solvation effects on the reduction potential of azurin mutants (272 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2006 Jan 1; 62(1): 262-269.
Impact Factor: 3.73
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Mineo P, Vitalini D, La Mendola D, Rizzarelli E, Scamporrino E, Vecchio G
* Coordination Features Of Difunctionalized Beta-Cyclodextrins With Carnosine: Esi-Ms And Spectroscopic Investigations On 6a, 6d-Di-(beta-Alanyl-L-Histidine)-6a, 6d-Dideoxy-Beta-Cyclodextrin And 6a, 6c-Di-(beta-Alanyl-L-Histidine)-6a, 6c-Dideoxy-Beta-Cyclodextrin And Their Copper (ii) Complexes (459 views)
J Chem Res (ISSN: 1873-3344, 0162-0134, 0162-0134print), 2004 Feb; 98(2): 254-265.
Impact Factor: 2.225
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Grasso D, Milardi D, La Rosa C, Rizzarelli E
* The different role of Cu++ and Zn++ ions in affecting the interaction of prion peptide PrP106-126 with model membranes (283 views)
Chem Commun (ISSN: 1359-7345, 1364-548x, 1364-548xelectronic), 2004 Jan 21; 10(2): 246-247.
Impact Factor: 3.997
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D'Auria G, Flores G, Falcigno L, Oliva R, Vacatello M, Corsaro MM, Parrilli M, Paolillo L
* Hyaluronate tetrasaccharide-Cu(II) interaction: A NMR study (311 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2003 Oct; 70(2): 260-269.
Impact Factor: 2.733
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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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Milardi D, Grasso DM, Verbeet MP, Canters GW, La Rosa C
* Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: Synergism among multiple depletions (330 views)
Arch Bioch Bioph (ISSN: 0003-9861, 0003-9861linking), 2003 Jun 1; 414(1): 121-127.
Impact Factor: 2.338
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Cucinotta V, Giuffrida A, Grasso G, Maccarrone G, Vecchio G
* Ligand exchange chiral separations by cyclodextrin derivatives in capillary electrophoresis (425 views)
Analyst (ISSN: 0003-2654), 2003; 128(2): 134-136.
Impact Factor: 2.251
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Marino M, Rossi M, Ruvo M, Fassina G
* Novel molecular targets for systemic lupus erythematosus (369 views)
Curr Drug Targets (ISSN: 1389-4501), 2002 Jun; 3(3): 223-228.
Impact Factor: 3.597
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Oliva R, Leone M, Falcigno L, D'Auria G, Dettin M, Scarinci C, Di Bello C, Paolillo L
* Structural investigation of the HIV-1 envelope glycoprotein gp160 cleavage site (489 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2002 Mar 15; 8(6): 1467-1473.
Impact Factor: 4.238
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Pappalardo G, Impellizzeri G, Bonomo RP, Campagna T, Grasso G, Saita MG
* Copper(II) and nickel(II) binding modes in a histidine-containing model dodecapeptide (331 views)
New J Chem (ISSN: 1144-0546), 2002; 26(5): 593-600.
Impact Factor: 2.06
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De Falco S, Ruvoletto MG, Verdoliva A, Ruvo M, Raucci A, Marino M, Senatore S, Cassani G, Alberti A, Pontisso P, Fassina G
* Cloning and Expression of a Novel Hepatitis B Virus-binding Protein from HepG2 Cells (622 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2001 Sep 28; 276(39): 36613-36623.
Impact Factor: 7.258
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Bonomo RP, Imperllizzeri G, Pappalardo G, Rizzarelli E, Tabbì G
Copper(II) binding modes in the prion octapeptide PHGGGWGQ: A spectroscopic and voltammetric study (502 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2000 Nov 17; 6(22): 4195-4202.
Impact Factor: 4.698
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Conato C, Contino A, Maccarrone G, Magrì A, Remelli M, Tabbì G
Copper(II) complexes with L-lysine and L-ornithine: Is the side-chain involved in the coordination? A thermodynamic and spectroscopic study (312 views)
Thermochim Acta (ISSN: 0040-6031), 2000 Nov 13; 362(1-2): 13-23.
Impact Factor: 0.807
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Lombardi A, Marasco D, Maglio O, Di Costanzo L, Nasti F, Pavone V
Miniaturized metalloproteins: Application to iron-sulfur proteins (653 views)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2000 Oct 24; 97(22): 11922-11927.
Impact Factor: 10.789
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Cucinotta V, Grasso D, Grasso G, Milardi D
Calorimetric evidences for Copper(II)-regulated chiral recognition between decanucleotide 5'd(CTGGATCCAG)2 and Ala-Trp dipeptides (394 views)
Nucleosides Nucleotides (ISSN: 0732-8311), 1997; 16(10-11): 1847-1854.
Impact Factor: 0.905
View Export to BibTeX Export to EndNote
Bonomo RP, Marchelli R, Tabbì G
Study of H2O2 interaction with copper(II) complexes with diamino-diamide type ligands, diastereoisomeric dipeptides, and tripeptides (512 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 1995 Nov 15; 60(3): 205-218.
Impact Factor: 1.342
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Fattorusso R, Morelli G, Lombardi A, Nastri F, maglio O, D'Auria G, Pedone C, Pavone V
Design of metal ion binding peptides (614 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1995; 37(6): 401-410.
Impact Factor: 2.425
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Pavone V, Lombardi A, D'Auria G, Saviano M, Nastri F, Paolillo L, Di Blasio B, Pedone C
β-Alanine containing peptides: A novel molecular tool for the design of γ-turns (813 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1992 Feb; 32(2): 173-184.
Impact Factor: 2.425
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Marchetti P, Benzi L, Trischitta V, Brunetti A, Cecchetti P, Ciccarone AM, Pezzino V, Vigneri R, Navalesi R
Complementary use of gel permeation and reversed-phase liquid chromatography for the analysis of A14-[125I]insulin and its degradation products in isolated human monocytes (1719 views)
J Chromatogr B Biomed Sci Appl (ISSN: 0378-4347), 1986 Apr 25; 377(C): 339-344.
Impact Factor: 1.588
View Export to BibTeX Export to EndNote
54 Records (54 excluding Abstracts).
Total impact factor: 191.68 (191.68 excluding Abstracts).
Total 5 year impact factor: 201.415 (201.415 excluding Abstracts).
Total impact factor: 191.68 (191.68 excluding Abstracts).
Total 5 year impact factor: 201.415 (201.415 excluding Abstracts).
492 views. Last view on Saturday 14 January 2023, 17:41:09
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