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1,198 results on '"Lamberti, C."'

9. Is pizza sutable to type 1 diabetes? A real life identification of best compromise between taste and low glycemic index in patients on insulin pump

Author

Brancato, C., Corigliano, M., Cozzolino, G., Fasolino, A., Improta, M.R., Lambersi, C., Martino, C., Mosca, C., Oliva, D., Stile, L.A., Vecchiato, A., Vetrano, A., Visconti, E., Battipaglia, D., Cecco, I., Della Monica, E., Di Capua, M.G., Palmieri, C., Procida, R., Romano, C., Viesti, F., Gentile, S., Della-Corte, T., Di Blasi, V., Guarino, G., Lamberti, C., Vaia, S., Satta, E., Alfarone, C., and Strollo, F.

Published
2020
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12. Why are so huge differences reported in the occurrence rate of skin lipohypertrophy? Does it depend on method defects or on lack of interest?

Author

Brancario, C., Corigliano, M., Cozzolino, G., Improta, M.R., Fasolino, A., Lamberti, C., Lapice, M., Martino, C., Oliva, D., Raffaele, A., Selleri, A., Simonetti, R., Stile, A., Vecchiato, A., Vetrano, A., Volpe, P., Caputo, G., Del Sorbo, A., Di Capua, M.G., Durazzo, G., Egidio, M., Garofalo, G., Grasso, L., Meo, A., Murano, A., Perillo, L., Procida, R., Vietsi, F., Gentile, S., Strollo, F., and Guarino, G.

Published
2019
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13. Evidence of ion diffusion at room temperature in microcrystals of the Bi2Sr2CaCu2O8+delta superconductor

Author

Truccato, M., Lamberti, C., Prestipino, C., and Agostino, A.

Subjects
Condensed Matter - Superconductivity, Condensed Matter - Materials Science
Abstract

We have studied Bi-2212 microcrystals aged at ambient conditions for 40 days. Combined x-ray absorption near edge structure and x-ray fluorescence measurements with micrometer space resolution show both an increase of Cu$^{+}$ with respect to Cu$^{2+}$ and an enrichment in Cu vs Bi and Sr cation content near the sample edges in the b-axis direction. A parallel study on an electrically contacted sample has indirectly detected the O loss, observing both a resistivity increase and an increase in sample thickness near the edges. We conclude that the O out-diffusion along the b-axis is accompanied by Cu cation migration in the same direction., Comment: RevTeX 4, 10 pages, 3 figures

Published
2005
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36. Correction:High-risk additional chromosomal abnormalities at low blast counts herald death by CML (Leukemia, (2020), 34, 8, (2074-2086), 10.1038/s41375-020-0826-9)

Author

Hehlmann, Rüdiger, Voskanyan, Astghik, Lauseker, Michael, Pfirrmann, Markus, Kalmanti, Lida, Rinaldetti, Sebastien, Kohlbrenner, Katharina, Haferlach, Claudia, Schlegelberger, Brigitte, Fabarius, Alice, Seifarth, Wolfgang, Spieß, Birgit, Wuchter, Patrick, Krause, Stefan, Kolb, Hans Jochem, Neubauer, Andreas, Hossfeld, Dieter K., Nerl, Christoph, Gratwohl, Alois, Baerlocher, Gabriela M., Burchert, Andreas, Brümmendorf, Tim H., Hasford, Jörg, Hochhaus, Andreas, Saußele, Susanne, Baccarani, Michele, von Weikersthal, L. Fischer, Hahn, M., Schlimok, G., Reichert, D., Janssen, J., Martens, U., Majunke, P., Reichert, Peter, Neben, K., Korsten, S., Scholz, Ch, Oldenkott, B., Heßling, J., Kingreen, D., Sperling, C., Schelenz, C., Blau, I., Urmersbach, A., Ludwig, W., Le Coutre, P., Arnold, R., de Wit, M., Pezzutto, A., Schäfer, E., Schroers, R., Lochter, A., Behringer, D., Ko, Y., Weidenhöfer, S., Verbeek, W., Brossart, P., Trenn, G., Pommerien, W., Krauter, J., Doering, G., Munzinger, H., Diekmann, C., Hertenstein, B., Stier, S., Möller-Faßbender, F., Hänel, M., Zöller, T., Lamberti, C., Koch, B., Henzel, A., Wagner, S., Schmalenbach, A., Hoffknecht, M., Ehninger, G., Kiani, A., Illmer, T., Aul, C., Flaßhove, M., Henneke, F., Simon, M., Müller, L., Becker, H., Janz, R., Eckart, M. J., Fuchs, R., Schlegel, F., Wattad, M., Rudolph, R., Beelen, D. W., Lindemann, A., Linck, D., Wassman, Jäger, E., Al-Batran, S., Reiber, T., Waller, C. F., Hoeffkes, H., Schulz, L., Tajrobehkar, K., Mittermüller, J., Pralle, H., Runde, V., Hoyer, A., Tessen, H., Trümper, L., Schmidt, C., Sieber, M., Eschenburg, H., Depenbusch, R., Rösel, S., Lindemann, H. W., Wolf, H., Spohn, C., Moeller, R., Hossfeld, D., Zander, A., Schafhausen, P., Köster, H., Hollburg, W., Schmitz, N., Dürk, H., Hemeier, M., Grote-Metke, A., Weischer, H., Bechtel, B., Balleisen, L., Sosada, M., Ho, A., Petersen, V., Dengler, J., Bildat, S., Hahn, L., Dietzfelbinger, H., Gröschel, W., Bartholomäus, A., Freier, W., Sievers, B., Pfreundschuh, I. M., Herrmann, T., Fauser, A., Menzel, J., Kemmerling, M., Hansen, R., Link, H., Schatz, M., Bentz, M., Prümmer, O., Kneba, M., Heymanns, J., Schmitz, S., Scheid, C., Lollert, A., Neise, M., Planker, M., Stauch, M., Schröder, M., Kempf, B., Vehling-Kaiser, U., Kremers, S., Köchling, G., Hartmann, F., Neuhaus, T., Fetscher, S., Kämpfe, D., Heil, G., Uppenkamp, M., Goldmann, B., Huber, T. Fischer, Hieber, U., Plöger, C., Griesshammer, M., Lange, C., Göttler, B., Lunscken, C., Schiel, X., Scheidegger, C., Stötzer, O., Hitz, H., Schick, H., Völkl, S., Spiekermann, K., Berdel, W., Hebart, H., Ladda, E., Schmidt, P., Burkhardt, U., Hentschke, S., Falge, C., Reschke, D., Köhne, C. A., Müller-Naendrup, C., Sauer, M., Frühauf, S., Ranft, K., Dencausse, Y., Sandritter, B., Baake, G., Hofknecht, M., Dengler, R., Edinger, M., Schenk, M., Wehmeier, A., Weidelich, H. P., Pihusch, R., Stahlhut, K., Baldus, M., Matzdorff, A., Geer, T., Schanz, S., Käfer, G., Gassmann, W., Priebe-Richter, C., Demandt, M., Springer, G., Fiechtner, H., Denzlinger, C., Schleicher, J., Assman, D., Gaeckler, R., Adam, G., Waladkhani, A., Rendenbach, B., Forstbauer, H., Kanz, L., Jacki, S., Stegelmann, F., Kalhori, N., Nusch, A., Langer, W., Müller, F., Brettner, S., Uebelmesser, B., Kamp, T., Schadeck-Gressel, C., Josten, K., Klein, O., Schwerdtfeger, R., Baurmann, H., Strotkötter, H., Fett, W., Raghavachar, A., Maintz, C., Goebler, M. C., Schlag, R., Elsel, W., Wernli, M., Heim, D., Wuillemin, W., Hess, U., Gmür, J., and Mayer, J.

Abstract

An amendment to this paper has been published and can be accessed via a link at the top of the paper.

Published
2020
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37. Effect of thermal processing on IgE cross-recognition of insect proteins in Italian patients allergic to house dust mite, shrimp and mealworm

Author

Cirrincione S, Lamberti C, Nebbia S, Brussino L, Giorgis V, Giuffrida MG, Rolla G, and Cavallarin L

Subjects
crossallergenicity, food allergy, fungi, edible insects
Abstract

INTRODUCTION. Edible insects are considered a promising and sustainable alternative protein source for humans, able to meet the increasing world's nutritional needs. The possible diffusion of insect farming and commercialization in Europe, has prompted the scientific community to investigate the allergenicity risk associated to insect consumption (1,2). Considering that edible insects are generally consumed after thermal processing, it is crucial to assess how processing may modify the protein structure, thus altering the protein cross-reactivity. In this study, we present one of the first investigations on insect cross-allergenicity, in three groups of Italian patients with a convincing history of house dust mite and shrimp allergy and with primary respiratory and food sensitization to mealworm. METHODS. We investigated by immunoblotting, the effect of boiling (5 min at 100 °C) and frying (3 min at 180 °C in sunflower oil) on the IgE-binding capacities towards both soluble and insoluble proteins fractions from five edible insects (mealworm, buffalo worm, silkworm, cricket and grasshopper). The immune-reactive proteins were identified by LC-MS/MS. RESULTS. Our data suggest that, depending on the nature of the reactive protein, the cross-reactivity resulted to be affected in different ways according to the different types of processing. In general, thermal processing influences the protein solubility, resulting in a protein shift from water-soluble to water-insoluble fractions, a shift that is more marked after frying than after boiling. Among the immune-reactive proteins, tropomyosin shows to have an important role as a cross-allergen for house dust mite and shrimp allergic patients and to be heat-stable in both fried and boiled samples. Actually, tropomyosin is considered a pan-allergen in crustaceans, mollusks, mites and insects, due to the high similarity of its amino acid sequences among species (3,4). The larval cuticle protein seems to play a major role in the cross-reactivity of patients primarily sensitized to mealworm. CONCLUSION. On the basis of our results, the effects of processing appeared to be protein-, species- and treatment-specific. Therefore, for patients allergic to house dust mite, shrimp and mealworm the consumption of insects, even after thermal processing, requires some caution.

Published
2020

38. Different roasting hazelnut procedures alter the structure of the protein bodies and affect the binding capacities of IgEs from allergic children

Author

Lamberti C, Nebbia S, Cirrincione S, Antoniazzi S, Manfredi M, Balestrini R, Monti G, Giuffrida MG, and Cavallarin L.

Subjects
food allergy, hazelnut, processing
Abstract

INTRODUCTION Thermal processing, commonly used during food production, may affect food allergenicity by inducing physical and/or chemical changes in proteins and lipids. However, due to the lack of detailed information on processing procedures, available evidences on this topic are presently contradictory. The aim of this study was to investigate how two different roasting techniques, hot air (HA) and infrared (IR), could modify the hazelnut seed structure, the protein profiles and solubility. Moreover, the ability of the IgEs from hazelnut allergic children to bind hazelnut proteins before and after roasting was evaluated. METHODS Experiments were designed on an Italian variety of C. avellana (Cv. Tonda Gentile delle Langhe) obtained from experimental fields. Two pilot-scale ovens infrared (IR) and hot air (HA) and two combinations of time and temperature for each oven were considered: 140 °C for 25 min (low temperature (LT)) and 170 °C for 17 min (high temperature (HT)) in HA; 140 °C for 12 min (LT) and 170 °C for 10 min (HT) in IR. RESULTS A decrease in hazelnut protein solubility was detectable following LT-IR roasting and it became more evident after HT processing, for both roasting types. The immuno-recognition decreased progressively from raw to high temperature processes. The IR-HT processing caused a quite complete disappearance of immune-recognition of hazelnut proteins. Interestingly, different allergens showed different responses to heat processing. The immune-reactivity of Cor a 9, Cor a 11 and Cor a 14 resulted to be stable until 140 °C, while Cor a 8 immuno-recognition was already reduced at 140 °C and completely lost at 170 °C. Differently, oil body (OB) associated protein immuno-recognition was increased after HA roasting at 140 °C whereas was reduced in the remaining treatments and disappeared in the IR-HT. At structural level, microscopical observations showed a cytoplasmic network disruption with an alteration of the structure of the protein bodies and of the cell wall organization. CONCLUSION IR oven is the least conservative processing, especially at high temperatures, both considering protein solubility and immuno-recognition. Our results could be useful for the development of clinical protocols for the process of oral desensitization of hazelnut allergic patients.

Published
2020

48. Thermal reduction of Cu(super 2+) -mordenite and re-oxidation upon interaction with H2O, O2, and NO

Author

F.X. Llabres i Xamena, Fisicaro, P., Berlier, G., Zecchina, A., Palomino, G. Turnes, Prestipino, C., Bordiga, S., Giamello, E., and Lamberti, C.

Subjects
Electron paramagnetic resonance spectroscopy -- Usage, Copper -- Research, Copper -- Chemical properties, Copper -- Structure, Chemistry, Physical and theoretical -- Research, Chemicals, plastics and rubber industries
Abstract

A multitechnique [electron paramagnetic resonance (EPR), XANES, EXAFS and IR of absorbed NO] study of the coordination and oxidation chemistry of copper species hosted in mordenite (MOR) zeolite under different conditions is presented. The differences observed between these two systems are explained in terms of the different structural characteristics.

Published
2003

49. Structural determination of copper species on the alumina-supported copper chloride catalyst: a detailed EXAFS study

Author

Pretipino, C, Vidotto, S, Bordiga, S, Garilli, M., Lamberti, C., Cremaschi, B., Marsella, A, Leofanti, G., Fisicaro, P., Spoto, G, and Zecchina, A.

Subjects
Chemistry, Physical and theoretical -- Research, Copper compounds -- Chemical properties, Copper compounds -- Structure, Aluminum compounds -- Chemical properties, Aluminum compounds -- Research, Chemicals, plastics and rubber industries
Abstract

A case study of the CuCl (sub 2)/Al (sub 2) O (sub 3) material was used, which represents the basic catalyst for the ethylene oxychlorination reaction, to describe a generalization of the standard EXAFS procedure that can be of general interest in all cases, where the absorbing species is present in more than one phase. This method helps to quantify the fraction of copper species in the Cu-aluminate, copper chloride, and paratacamite (Cu2(OH)3Cl) phases as a function of copper loading and activation temperatures.

Published
2003

50. Growth of NiO on Ag(001): Atomic environment, strain, and interface relaxation studied by polarization dependent extended x-ray absorption fine structure

Author

Groppo, E., Boscherini, F., Prestipino, C., Lamberti, C., Luches, P., and Giovanardi, C.

Subjects
Monomolecular films -- Research, Silver -- Atomic properties, Nitrogen oxide -- Atomic properties, Chemicals, plastics and rubber industries
Abstract

A structural study of three to ten monolayer (ML) thick NiO films grown on Ag(001) is reported. The polarization-dependent X-ray absorption spectroscopy at the Ni K edge allowed to obtain an accurate description of the local atomic environment of the Ni atoms up to the seventh coordination shell, including the determination of the in-plane and out-of-plane strains for the NiO films.

Published
2003

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