28 results on '"Verdone, G"'
Search Results
2. Sequence-specific backbone NMR assignments for the C-terminal globular domain of EMILIN-1
- Author
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Verdone, G., Colebrooke, S. A., Viglino, Paolo, Corazza, Alessandra, Doliana, R., Mungiguerra, G., Colombatti, A., Esposito, Gennaro, and Campbell, I. D.
- Subjects
Partially deuterated proteins ,Genetics and Molecular Biology (all) ,Elastic fibres ,Triple resonance experiments ,C1q-like domain ,EMILIN ,Heteronuclear NMR ,TROSY ,Spectroscopy ,Biochemistry, Genetics and Molecular Biology (all) ,Biochemistry - Published
- 2004
3. The solution structure of human beta2-microglobulin reveals the prodromes of its amyloid transition
- Author
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Verdone, G., Corazza, Alessandra, Viglino, Paolo, Pettirossi, F., Giorgetti, S., Mangione, P, Andreola, A., Stoppini, M., Bellotti, V., and Esposito, Gennaro
- Published
- 2002
4. Structure of EMILIN-1 C1Q-like domain
- Author
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Verdone, G., primary, Corazza, A., additional, Colebrooke, S.A., additional, Cicero, D.O., additional, Eliseo, T., additional, Boyd, J., additional, Doliana, R., additional, Fogolari, F., additional, Viglino, P., additional, Colombatti, A., additional, Campbell, I.D., additional, and Esposito, G., additional
- Published
- 2008
- Full Text
- View/download PDF
5. Improved method for pulse width calibration in indirectly detected experiments
- Author
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Esposito, G., primary, Nadalin, L., additional, Verdone, G., additional, Corazza, A., additional, Viglino, P., additional, and Fedrigo, M., additional
- Published
- 2001
- Full Text
- View/download PDF
6. Removal of the N-terminal hexapeptide from human β2-microglobulin facilitates protein aggregation and fibril formation
- Author
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Esposito, G., primary, Michelutti, R., additional, Verdone, G., additional, Viglino, P., additional, ÁNdez, H. Hern, additional, Robinson, C. V., additional, Amoresano, A., additional, Piaz, F. Dal, additional, Monti, M., additional, Pucci, P., additional, Mangione, P., additional, Stoppini, M., additional, Merlini, G., additional, Ferri, G., additional, and Bellotti, V., additional
- Published
- 2000
- Full Text
- View/download PDF
7. Search for nuclearites using the MACRO detector
- Author
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Ahlen, S., primary, Ambrosio, M., additional, Antolini, R., additional, Auriemma, G., additional, Baker, R., additional, Baldini, A., additional, Barbarino, G. C., additional, Barish, B. C., additional, Battistoni, G., additional, Bellotti, R., additional, Bemporad, C., additional, Bernardini, P., additional, Bilokon, H., additional, Bisi, V., additional, Bloise, C., additional, Bussino, S., additional, Cafagna, F., additional, Calicchio, M., additional, Campana, P., additional, Campana, D., additional, Carboni, M., additional, Cecchini, S., additional, Cei, F., additional, Chiarella, V., additional, Chiera, C., additional, Cobis, A., additional, Cormack, R., additional, Corona, A., additional, Coutu, S., additional, DeCataldo, G., additional, Dekhissi, H., additional, DeMarzo, C., additional, De Vincenzi, M., additional, Di Credico, A., additional, Diehl, E., additional, Erriquez, O., additional, Favuzzi, C., additional, Ficenec, D., additional, Forti, C., additional, Foti, L., additional, Fusco, P., additional, Giacomelli, G., additional, Giannini, G., additional, Giglietto, N., additional, Giubellino, P., additional, Grassi, M., additional, Green, P., additional, Grillo, A., additional, Guarino, F., additional, Gustavino, C., additional, Habig, A., additional, Heinz, R., additional, Hong, J. T., additional, Iarocci, E., additional, Katsavounidis, E., additional, Kearns, E., additional, Klein, S., additional, Kyriazopoulou, S., additional, Lamanna, E., additional, Lane, C., additional, Lee, C., additional, Levin, D., additional, Lipari, P., additional, Liu, G., additional, Liu, R., additional, Longo, M. J., additional, Ludlam, G., additional, Mancarella, G., additional, Mandrioli, G., additional, Margiotta-Neri, A., additional, Marin, A., additional, Marini, A., additional, Martello, D., additional, Martellotti, G., additional, Marzari Chiesa, A., additional, Masera, M., additional, Matteuzzi, P., additional, Michael, D. G., additional, Miller, L., additional, Monacelli, P., additional, Monteno, M., additional, Mufson, S., additional, Musser, J., additional, Nutter, S., additional, Okada, C., additional, Osteria, G., additional, Palamara, O., additional, Parlati, S., additional, Patera, V., additional, Patrizii, L., additional, Pazzi, R., additional, Peck, C. W., additional, Petrakis, J., additional, Petrera, S., additional, Pignatano, N. D., additional, Pistilli, P., additional, Predieri, F., additional, Ramello, L., additional, Reynoldson, J., additional, Ronga, F., additional, Rosa, G., additional, Satriano, C., additional, Satta, L., additional, Scapparone, E., additional, Scholberg, K., additional, Sciubba, A., additional, Serra Lugaresi, P., additional, Severi, M., additional, Sitta, M., additional, Spinelli, P., additional, Spinetti, M., additional, Spurio, M., additional, Steele, J., additional, Steinberg, R., additional, Stone, J. L., additional, Sulak, L. R., additional, Surdo, A., additional, Tarlé, G., additional, Togo, V., additional, Valente, V., additional, Verdone, G. R., additional, Walter, C. W., additional, Webb, R., additional, and Worstell, W., additional
- Published
- 1992
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- View/download PDF
8. Study of the ultrahigh-energy primary-cosmic-ray composition with the MACRO experiment
- Author
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Ahlen, S., primary, Ambrosio, M., additional, Antolini, R., additional, Auriemma, G., additional, Baldini, A., additional, Bam, B. B., additional, Barbarino, G. C., additional, Barish, B. C., additional, Battistom, G., additional, Bellotti, R., additional, Bemporad, C., additional, Bernardini, P., additional, Bilokon, H., additional, Bisi, V., additional, Bloise, C., additional, Bussino, S., additional, Cafagna, F., additional, Calicchio, M., additional, Campana, P., additional, Campana, D., additional, Carboni, M., additional, Cecchini, S., additional, Cei, F., additional, Chiarella, V., additional, Chiera, C., additional, Cobis, A., additional, Cormack, R., additional, Corona, A., additional, Coutu, S., additional, DeCataldo, G., additional, DeMarzo, C., additional, De Vincenzi, M., additional, Di Credico, A., additional, Diehl, E., additional, Erriquez, O., additional, Favuzzi, C., additional, Ficenec, D., additional, Forti, C., additional, Foti, L., additional, Fusco, P., additional, Giacomelli, G., additional, Giannini, G., additional, Giglietto, N., additional, Giubellino, P., additional, Grassi, M., additional, Green, P., additional, Grillo, A., additional, Guarino, F., additional, Gustavino, C., additional, Habig, A., additional, Heinz, R., additional, Hong, J. T., additional, Iarocci, E., additional, Katsavounidis, E., additional, Kearns, E., additional, Klein, S., additional, Kyriazopoulou, S., additional, Lamanna, E., additional, Lane, C., additional, Lee, C., additional, Levin, D., additional, Lipari, P., additional, Liu, G., additional, Liu, R., additional, Longo, M. J., additional, Ludlam, G., additional, Mancarella, G., additional, Mandrioli, G., additional, Margiotta-Neri, A., additional, Marin, A., additional, Marini, A., additional, Martello, D., additional, Martellotti, G., additional, Chiesa, A. Marzari, additional, Masera, M., additional, Matteuzzi, P., additional, Michael, D. G., additional, Miller, L., additional, Monacelli, P., additional, Monteno, M., additional, Mufson, S., additional, Musser, J., additional, Nutter, S., additional, Okada, C., additional, Osteria, G., additional, Palamara, O., additional, Parlati, S., additional, Patera, V., additional, Patrizii, L., additional, Pazzi, R., additional, Peck, C. W., additional, Petrakis, J., additional, Petrera, S., additional, Pignatano, N. D., additional, Pistilli, P., additional, Predieri, F., additional, Ramello, L., additional, Reynoldson, J., additional, Ronga, F., additional, Rosa, G., additional, Satriano, C., additional, Satta, L., additional, Scapparone, E., additional, Scholberg, K., additional, Sciubba, A., additional, Lugaresi, P. Serra, additional, Severi, M., additional, Sitta, M., additional, Spinelli, P., additional, Spinetti, M., additional, Spurio, M., additional, Steele, J., additional, Steinberg, R., additional, Stone, J. L., additional, Sulak, L. R., additional, Surdo, A., additional, Tarlé, G., additional, Togo, V., additional, Valente, V., additional, Verdone, G. R., additional, Walter, C. W., additional, Webb, R., additional, and Worstell, W., additional
- Published
- 1992
- Full Text
- View/download PDF
9. Removal of the N-terminal hexapeptide from human ²2-microglobulin facilitates protein aggregation and fibril formation.
- Author
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ESPOSITO, G., MICHELUTTI, R., VERDONE, G., VIGLINO, P., HERNÁNDEZ, H., ROBINSON, C.V., AMORESANO, A., PIAZ, F. DAL, MONTI, M., PUCCI, P., MANGIONE, P., STOPPINI, M., MERLINI, G., FERRI, G., and BELLOTTI, V.
- Abstract
The solution structure and stability of N-terminally truncated ²2-microglobulin (”N6²2-m), the major modification in ex vivo fibrils, have been investigated by a variety of biophysical techniques. The results show that ”N6²2-m has a free energy of stabilization that is reduced by 2.5 kcal/mol compared to the intact protein. Hydrogen exchange of a mixture of the truncated and full-length proteins at ¼M concentrations at pH 6.5 monitored by electrospray mass spectrometry reveals that ”N6²2-m is significantly less protected than its wild-type counterpart. Analysis of ”N6²2-m by NMR shows that this loss of protection occurs in ² strands I, III, and part of II. At mM concentration gel filtration analysis shows that ”N6²2-m forms a series of oligomers, including trimers and tetramers, and NMR analysis indicates that strand V is involved in intermolecular interactions that stabilize this association. The truncated species of ²2-microglobulin was found to have a higher tendency to self-associate than the intact molecule, and unlike wild-type protein, is able to form amyloid fibrils at physiological pH. Limited proteolysis experiments and analysis by mass spectrometry support the conformational modifications identified by NMR and suggest that ”N6²2-m could be a key intermediate of a proteolytic pathway of ²2-microglobulin. Overall, the data suggest that removal of the six residues from the N-terminus of ²2-microglobulin has a major effect on the stability of the overall fold. Part of the tertiary structure is preserved substantially by the disulfide bridge between Cys25 and Cys80, but the pairing between ²-strands far removed from this constrain is greatly perturbed. [ABSTRACT FROM PUBLISHER]
- Published
- 2000
10. Multiple muons and primary cosmic composition studies with MACRO
- Author
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Palamara, Ornella, Bellotti, R., Cafagna, F., Calicchio, M., Cataldo, G., Marzo, C., Erriquez, O., Favuzzi, C., Fusco, P., Giglietto, N., Spinelli, P., Petrakis, J., Antolini, R., Bam, B. B., Cecchini, S., Giacomelli, G., Mandrioli, G., Margiotta-Neri, A., Matteuzzi, P., Patrizii, L., Predieri, F., Scapparone, E., Serra Lugaresi, P., Spurio, M., Togo, V., Ahlen, S. P., Cormack, R., Kearns, E., Klein, S., Ludlam, G., Marin, A., Okada, C., Stone, J. L., Sulak, L. R., Worstell, W., Barish, B., Coutu, S., Hong, J. T., Katsuvounidis, E., Kyriazopoulou, S., Liu, G., Liu, R., Michael, D., Peck, C., Pignatano, N., Scholberg, K., Steele, J., Walter, C. W., Lane, Charles E., Steinberg, R., Battistoni, G., Bilokon, H., Bloise, C., Campana, P., Carboni, M., Cavallo, P., Chiarella, V., Cobis, A., Forti, C., Grillo, A., Iarocci, E., Marini, A., Patera, V., Ronga, F., Satta, L., Spinetti, M., Valente, V., Gustavino, C., Reynoldson, J., Habig, Alec, Heinz, R., Miller, L., Mufson, Stuart L., Musser, J., Nutter, S., Di Credico, Alessandra, Monacelli, Piero, Bernardini, P., Mancarella, G., Martello, D., Petrera, S., Pistilli, P., Surdo, A., Diehl, E., Levin, D., Longo, M., Smith, C., Tarle, G., Ambrosio, M., Barbarino, G. C., Campagna, D., Guarino, F., Osteria, G., Baldini, A., Bemporad, C., Cei, F., Giannini, G., Grassi, M., Pazzi, R., Auriemma, G., Bussino, S., Chiera, C., Chrysicopoulou, P., Corona, A., Devincenzi, M., Foti, L., Ernesto Lamanna, Lipari, P., Martellotti, G., Rosa, G., Satriano, C., Sciubba, A., Severi, M., Verdone, G. R., Green, P., Webb, R., Bisi, V., Giubellino, P., Marzari Chiesa, A., Masera, M., Monteno, M., Parlati, S., Ramello, L., Sitta, M., Palamara, O, Bellotti, R, Cafagna, F, Calicchio, M, De Cataldo, G, De Marzo, C, Erriquez, O, Favuzzi, C, Fusco, P, Giglietto, N, Spinelli, P, Petrakis, J, Antolini, R, Bam, Bb, Cecchini, S, Giacomelli, G, Mandrioli, G, Margiotta Neri, A, Matteuzzi, P, Patrizii, L, Predieri, F, Scapparone, E, Serra Lugaresi, P, Spurio, M, Togo, V, Ahlen, Sp, Cormack, R, Kearns, E, Klein, S, Ludlam, G, Marin, A, Okada, C, Stone, Jl, Sulak, Lr, Worstell, W, Barish, B, Coutu, S, Hong, Jt, Katsuvounidis, E, Kyriazopoulou, S, Liu, G, Liu, R, Michael, D, Peck, C, Pignatano, N, Scholberg, K, Steele, J, Walter, Cw, Lane Charles, E, Steinberg, R, Battistoni, G, Bilokon, H, Bloise, C, Campana, P, Carboni, M, Cavallo, P, Chiarella, V, Cobis, A, Forti, C, Grillo, A, Iarocci, E, Marini, A, Patera, V, Ronga, F, Satta, L, Spinetti, M, Valente, V, Gustavino, C, Reynoldson, J, Habig, Alec, Heinz, R, Miller, L, Mufson Stuart, L, Musser, J, Nutter, S, Di Credico, Alessandra, Monacelli, Piero, Bernardini, P, Mancarella, G, Martello, D, Petrera, S, Pistilli, P, Surdo, A, Diehl, E, Levin, D, Longo, M, Smith, C, Tarle, G, Ambrosio, M, Barbarino, Gc, Campagna, D, Guarino, F, Osteria, G, Baldini, A, Bemporad, C, Cei, F, Giannini, G, Grassi, M, Pazzi, R, Auriemma, G, Bussino, Severino Angelo Maria, Chiera, C, Chrysicopoulou, P, Corona, A, Devincenzi, M, Foti, L, Lamanna, E, Lipari, P, Martellotti, G, Rosa, G, Satriano, C, Sciubba, A, Severi, M, Verdone, Gr, Green, P, Webb, R, Bisi, V, Giubellino, P, Marzari Chiesa, A, Masera, M, Monteno, M, Parlati, S, Ramello, L, and Sitta, M.
- Subjects
Physics ,Nuclear and High Energy Physics ,Particle physics ,Muon ,COSMIC cancer database ,Physics::Instrumentation and Detectors ,Detector ,Multiplicity (mathematics) ,Cosmic ray ,Atomic and Molecular Physics, and Optics ,Nuclear physics ,Primary (astronomy) ,Physics::Accelerator Physics ,High Energy Physics::Experiment ,Supermodule ,Macro ,Mathematics::Representation Theory - Abstract
The analysis of multiple muon events collected with one MACRO supermodule and two supermodules is described. Muon pair separation distributions as corrected for the bias of the finite detector size are presented. Muon multiplicity distributions are compared with two primary cosmic ray composition models.
11. Widely separated muons in the MACRO detector
- Author
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Cormack, R., Ahlen, S. P., Ficenec, D., Edward Kearns, Klein, S., Ludlam, G., Marin, A., Okada, C., Stone, J. L., Sulak, L. R., Worstell, W., Bellotti, R., Cafagna, F., Cecchini, S., Calicchio, M., Cataldo, G., Marzo, C., Erriquez, O., Favuzzi, C., Fusco, P., Giglietto, N., Spinelli, P., Petrakis, J., Antolini, R., Bam, B. B., Giacomelli, G., Mandrioli, G., Margiotta-Neri, A., Matteuzzi, P., Patrizii, L., Predieri, F., Scapparone, E., Serra Lugaresi, P., Spurio, M., Togo, V., Barish, B. C., Coutu, S., Hong, J. T., Katsavounidis, E., Kyriazopoulou, S., Liu, G., Liu, R., Michael, D. G., Peck, C. W., Pignatano, N. D., Scholberg, K., Steele, J., Walter, C. W., Lane, Charles E., Steinberg, R., Battistoni, G., Bilokon, H., Bloise, C., Campana, P., Carboni, M., Chiarella, V., Cobis, A., Forti, C., Grillo, A., Iarocci, E., Marini, A., Patera, V., Ronga, F., Satta, L., Spinetti, M., Valente, V., Gustavino, C., Parlati, S., Reynoldson, J., Habig, Alec, Heinz, R., Miller, L., Mufson, Stuart L., Musser, J., Nutter, S., Di Credico, Alessandra, Monacelli, Piero, Bernardini, P., Mancarella, G., Martello, D., Palamara, O., Petrera, S., Pistilli, P., Surdo, A., Diehl, E., Lee, C., Levin, D., Longo, M. J., Tarle, G., Ambrosio, M., Barbarino, G. C., Campana, D., Guarino, F., Osteria, G., Baldini, A., Bemporad, C., Cei, F., Giannini, G., Grassi, M., Pazzi, R., Auriemma, G., Bussino, S., Chiera, C., Corona, A., Vincenzi, M., Foti, L., Lamanna, E., Lipari, P., Martellotti, G., Rosa, G., Satriano, C., Sciubba, A., Severi, M., Verdone, G. R., Green, P., Webb, R., Bisi, V., Giubellino, P., Marzari-Chiesa, A., Masera, M., Monteno, M., Ramello, L., and Sitta, M.
- Subjects
Cosmic-rays ,multimuon ,MACRO
12. Removal of the N-terminal hexapeptide from human β2-microglobulin facilities protein aggregation and fibril formation
- Author
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Esposito, G., Michelutti, R., Verdone, G., Viglino, P., Hernández, H., Robinson, C. V., Amoresano, A., Dal Piaz, F., Maria MONTI, Pucci, P., Mangione, P., Stoppini, M., Merlini, G., Ferri, G., and Bellotti, V.
13. Strange quark matter search using the MACRO detector
- Author
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Liu, G., Ahlen, S. P., Ambrosio, M., Antolini, R., Auriemma, G., Baker, R., Baldini, A., Barbarino, G. C., Barish, B. C., Battistoni, G., Bellotti, R., Bemporad, C., Bernardini, P., Bilokon, H., Bisi, V., Bloise, C., Bussino, S., Cafagna, F., Calicchio, M., Campana, P., Campana, D., Carboni, M., Cecchini, S., Cei, F., Chiarella, V., Chiera, C., Cobis, A., Cormack, R., Corona, A., Coutu, S., Cataldo, G., Dekhissi, H., Marzo, C., Vincenzi, M., Di Credico, Alessandra, Diehl, E., Erriquez, O., Favuzzi, C., Ficenec, D., Forti, C., Foti, L., Fusco, P., Giacomelli, G., Giannini, G., Giglietto, N., Giubellino, P., Grassi, M., Green, P., Grillo, A., Guarino, F., Gustavino, C., Habig, Alec, Heinz, R., Hong, J. T., Iarocci, E., Katsavounidis, E., Kearns, E., Klein, S., Kyriazopoulou, S., Lamanna, E., Lane, Charles E., Lee, C., Levin, D., Lipari, P., Liu, R., Longo, M. J., Ludlam, G., Mancarella, G., Mandrioli, G., Margiotta-Neri, A., Marin, A., Marini, A., Martello, D., Martellotti, G., Marzari Chiesa, A., Masera, M., Matteuzzi, P., Michael, D. G., Miller, L., Monacelli, Piero, Monteno, M., Mufson, Stuart L., Musser, J., Nutter, S., Okada, C., Osteria, G., Palamara, O., Parlati, S., Patera, V., Patrizii, L., Pazzi, R., Peck, C. W., Petrakis, J., Petrera, S., Pignatano, N. D., Pistilli, P., Predieri, F., Ramello, L., Reynoldson, J., Ronga, F., Rosa, G., Satriano, C., Satta, L., Scapparone, E., Scholberg, K., Sciubba, A., Serra Lugaresi, P., Severi, M., Sitta, M., Spinelli, P., Spinetti, M., Maurizio Spurio, Steele, J., Steinberg, R., Stone, J. L., Sulak, L. R., Surdo, A., Tarle, G., Togo, V., Valente, V., Verdone, G. R., Walter, C. W., Webb, R., and Worstell, W.
14. UAV-to-Ground Multi-Hop Communication Using Backpressure and FlashLinQ-Based Algorithms
- Author
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Chiara Buratti, Charles Jumaa Katila, Giuseppe Caire, Benjamin Okolo, Roberto Verdone, C.J. Katila, B. Okolo, C. Buratti, R. Verdone, G. Caire, Katila, Charles Jumaa, Okolo, Benjamin, Buratti, Chiara, Verdone, Roberto, and Caire, Giuseppe
- Subjects
Backpressure ,Scheduling ,Computer science ,Wireless ad hoc network ,020209 energy ,FlashLinQ ,Throughput ,Unmanned Aerial Vehicle ,02 engineering and technology ,Multi-Hop ,Hop (networking) ,Scheduling (computing) ,0202 electrical engineering, electronic engineering, information engineering ,Electrical and Electronic Engineering ,Algorithm - Abstract
The use of Unmanned Aerial Vehicles (UAVs) for remote sensing and surveillance applications has become increasingly popular in the last decades. This paper investigates the communication between a UAV and a final control center (CC), using static relays located on the ground, to overcome the intermittent connectivity between the two end points, due to the UAV flight. Backpressure and FlashLinQ routing and scheduling algorithms are jointly applied to this scenario. Backpressure has been shown to be able stabilize any input traffic within the network capacity region without requiring knowledge of traffic arrival rates and channel state probabilities. FlashLinQ is used in the scheduling phase to derive a maximal feasible subset of links which can coexist on a given slot without causing harmful interference to each other. Moreover, to overcome the limit on long end-to-end delays of backpressure, we propose a modified algorithm, where relays are selected depending on their proximity to the CC and on the UAV trajectory. Through extensive simulations, we demonstrate that, compared to the benchmark solution based on backpressure, the proposed algorithm is able to reduce delay significantly without any loss in throughput gain.
- Published
- 2018
- Full Text
- View/download PDF
15. First supermodule of the MACRO detector at Gran Sasso
- Author
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Paolo Giubellino, M. Severi, G. Pellizzoni, Fausto Guarino, S. L. Nutter, V. Valente, G. Battistoni, V. Bisi, C. W. Walter, A. Frani, G. R. Verdone, E. Hazen, Gianfranca De Rosa, J. L. Stone, L. Satta, D. Cosson, Marco Grassi, N. De Seriis, V. Chiarella, Mario Sitta, C. Gustavino, D. Campana, G. Mancarella, S. P. Ahlen, R. Antolini, Michael J. Longo, G. Liu, P. Spinelli, J. Reynoldson, A. Corona, G. Giannini, C. Bloise, Robert A. Cormack, C. Chiera, C. Favuzzi, Frederic Jean Ronga, E. Iarocci, N. Giglietto, Severino Angelo Maria Bussino, G. Tarle, L. Foti, Erik Katsavounidis, S. L. Mufson, P. Pistilli, R. Pazzi, G. de Cataldo, Marco Monteno, Edward Diehl, G. Martellotti, Sergio Petrera, Stefan Klein, F. Gherarducci, A. Mengucci, P. Monacelli, Paolo Lipari, Maurizio Spurio, A. Surdo, F. Predieri, P. Bernardini, R.M. Heinz, G.L. Sanzani, M. Ambrosio, C. Lee, D. Ficenec, F. Cei, R. Diotallevi, P. Serra Lugaresi, D. Martello, Ana Maria Marin, Pierluigi Campana, S. Cecchini, Alec Habig, F. Welte, C. Satriano, G. Auriemma, Roberto Bellotti, A. Boiano, L. Miller, D. Levin, M. Carboni, C. Bemporad, N. D. Pignatano, G. C. Barbarino, S. Coutu, Alexander Grillo, I. D'Antone, J. Petrakis, Eugenio Scapparone, A. Baldini, Luciano Ramello, S. Parlati, J. Steele, G. Ludlam, S. Merritt, V. Togo, C. Forti, Massimo Masera, P. Matteuzzi, G. Giacomelli, M. Perchiazzi, M. Calicchio, Vincenzo Patera, Halina Bilokon, C. Pinto, A. Tazzioli, W. A. Worstell, A. Sciubba, O. Palamara, G. Osteria, P. Parascandalo, M. Spinetti, A. Candela, F. Cafagna, Kate Scholberg, R. Liu, D. G. Michael, C. R. Bower, A. Sacchetti, A. Marzari Chiesa, O. Erriquez, C. De Marzo, A. Cobis, Patrick Green, J. A. Musser, A. Di Credico, M. Devincenzi, Barry C. Barish, S. Kyriazopoulou, R. C. Webb, R. Steinberg, C. W. Peck, P. Fusco, Andrea Carlo Marini, L. Patrizii, G. Mandrioli, Lawrence Sulak, J. T. Hong, C. E. Lane, J. Hanson, M. Mongelli, C. Okada, E. Kearns, U. Denni, E. Lamanna, Ahlen S., Ambrosio M., Antolini R., Auriemma G., Baldini A., Barbarino G.C., Barish B., Battistoni G., Bellotti R., Bemporad C., Bernardini P., Bilokon H., Bisi V., Bloise C., Boiano A., Bower C., Bussino S., Cafagna F., Calicchio M., Campana P., Campana D., Candela A., Carboni M., Cecchini S., Cei F., Chiarella V., Chiera C., Cobis A., Cormack R., Corona A., Cosson D., Coutu S., D'Antone I., De Cataldo G., De Marzo C., Denni U., De Seriis N., DeVincenzi M., Di Credico A., Diehl E., Diotallevi R., Erriquez O., Favuzzi C., Ficenec D., Forti C., Foti L., Frani A., Fusco P., Gherarducci F., Giacomelli G., Giannini G., Giglietto N., Giubellino P., Grassi M., Green P., Grillo A., Guarino F., Gustavino C., Habig A., Hanson J., Hazen E., Heinz R., Hong J.T., Iarocci E., Katsavounidis E., Kearns E., Klein S., Kyriazopoulou S., Lamanna E., Lane C., Lee C., Levin D., Lipari P., Liu G., Liu R., Longo M.J., Ludlam G., Mancarella G., Mandrioli G., Marin A., Marini A., Martello D., Martellotti G., Marzari Chiesa A., Masera M., Matteuzzi P., Mengucci A., Merritt S., Michael D.G., Miller L., Monacelli P., Mongelli M., Monteno M., Mufson S., Musser J., Nutter S., Okada C., Osteria G., Palamara O., Parascandalo P., Parlati S., Patera V., Patrizii L., Pazzi R., Peck C.W., Pellizzoni G., Perchiazzi M., Petrakis J., Petrera S., Pignatano N.D., Pinto C., Pistilli P., Predieri F., Ramello L., Reynoldson J., Ronga F., Rosa G., Sacchetti A., Sanzani G., Satriano C., Satta L., Scapparone E., Scholberg K., Sciubba A., Serra Lugaresi P., Severi M., Sitta M., Spinelli P., Spinetti M., Spurio M., Steele J., Steinberg R., Stone J.L., Sulak L.R., Surdo A., Tarle G., Tazzioli A., Togo V., Valente V., Verdone G.R., Walter C.W., Webb R., Welte F., Worstell W., Ahlen, S., Ambrosio, M., Antolini, R., Auriemma, G., Baldini, A., Barbarino, G. C., Barish, B., Battistoni, G., Bellotti, R., Bemporad, C., Bernardini, P., Bilokon, H., Bisi, V., Bloise, C., Boiano, A., Bower, C., Bussino, S., Cafagna, F., Calicchio, M., Campana, P., Campana, D., Candela, A., Carboni, M., Cecchini, S., Cei, F., Chiarella, V., Chiera, C., Cobis, A., Cormack, R., Corona, A., Cosson, D., Coutu, S., D'Antone, I., De Cataldo, G., De Marzo, C., Denni, U., De Seriis, N., Devincenzi, M., Di Credico, A., Diehl, E., Diotallevi, R., Erriquez, O., Favuzzi, C., Ficenec, D., Forti, C., Foti, L., Frani, A., Fusco, P., Gherarducci, F., Giacomelli, G., Giannini, G., Giglietto, N., Giubellino, P., Grassi, M., Green, P., Grillo, A., Guarino, F., Gustavino, C., Habig, A., Hanson, J., Hazen, E., Heinz, R., Hong, J. T., Iarocci, E., Katsavounidis, E., Kearns, E., Klein, S., Kyriazopoulou, S., Lamanna, E., Lane, C., Lee, C., Levin, D., Lipari, P., Liu, G., Liu, R., Longo, M. J., Ludlam, G., Mancarella, Giovanni, Mandrioli, G., Marin, A., Marini, A., Martello, Daniele, Martellotti, G., Marzari Chiesa, A., Masera, M., Matteuzzi, P., Mengucci, A., Merritt, S., Michael, D. G., Miller, L., Monacelli, P., Mongelli, M., Monteno, M., Mufson, S., Musser, J., Nutter, S., Okada, C., Osteria, G., Palamara, O., Parascandalo, P., Parlati, S., Patera, V., Patrizii, L., Pazzi, R., Peck, C. W., Pellizzoni, G., Perchiazzi, M., Petrakis, J., Petrera, S., Pignatano, N. D., Pinto, C., Pistilli, P., Predieri, F., Ramello, L., Reynoldson, J., Ronga, F., Rosa, G., Sacchetti, A., Sanzani, G., Satriano, C., Satta, L., Scapparone, E., Scholberg, K., Sciubba, A., Serra Lugaresi, P., Severi, M., Sitta, M., Spinelli, P., Spinetti, M., Spurio, M., Steele, J., Steinberg, R., Stone, J. L., Sulak, L. R., Surdo, A., Tarlé, G., Tazzioli, A., Togo, V., Valente, V., Verdone, G. R., Walter, C. W., Webb, R., Welte, F., Worstell, W., Barbarino, Giancarlo, and Guarino, Fausto
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Physics ,Nuclear and High Energy Physics ,Physics::Instrumentation and Detectors ,business.industry ,Detector ,ComputingMethodologies_IMAGEPROCESSINGANDCOMPUTERVISION ,MACRO ,Gran Sasso ,Data acquisition ,Scintillation counter ,High Energy Physics::Experiment ,Supermodule ,Macro ,Mathematics::Representation Theory ,business ,Instrumentation ,Computer hardware - Abstract
In this paper the design, construction and performance of the lower part of the first supermodule of the MACRO detector is described.
16. Muon astronomy with the MACRO detector
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V. Chiarella, G. Mandrioli, B. B. Bam, R. Pazzi, P. Monacelli, A. Marin, Maurizio Spurio, A. Surdo, M. De Vincenzi, S. Coutu, J. L. Stone, L. Satta, A. Di Credico, D. G. Michael, C. Satriano, G. Auriemma, S. Cecchini, S. Kyriazopoulou, F. Predieri, C. Favuzzi, Pierluigi Campana, M. J. Longo, P. Serra Lugaresi, S. L. Nutter, V. Bisi, G. Tarle, C. W. Walter, Steven Ahlen, Paolo Giubellino, P. Spinelli, M. Severi, E. Kearns, A. A. Grillo, R. C. Webb, G. C. Barbarino, Roberto Bellotti, A. Marzari Chiesa, L. Patrizii, S. Klein, C. Okada, V. Valente, F.J. Ronga, D. Martello, G. Mancarella, J. Reynoldson, Edward Diehl, Paolo Lipari, Eugenio Scapparone, G. DeCataldo, Mario Sitta, C. Gustavino, J. Petrakis, Giuseppe Osteria, V. Togo, S. Parlati, M. Ambrosio, R. Steinberg, F. Cafagna, Pio Pistilli, Erik Katsavounidis, C. Bemporad, S. L. Mufson, Lawrence Sulak, Severino Angelo Maria Bussino, P. Matteuzzi, P. Green, A. Corona, A. Margiotta-Neri, D. Levin, R.M. Heinz, Gianfranca De Rosa, Fabrizio Cei, C. Chiera, G. R. Verdone, E. Lamanna, O. Palamara, C. W. Peck, L. Ramello, M. Grassi, N. D. Pignatano, D. Ficenec, Kate Scholberg, O. Erriquez, A. Cobis, P. Bernardini, E. Iarocci, F. Guarino, J. A. Musser, R. Liu, M. Calicchio, G. Battistoni, M. Spinetti, Halina Bilokon, G. Liu, J. T. Hong, J. L. Miller, C. E. Lane, Alec Habig, Barry C. Barish, H. Dekhissi, C. Forti, Massimo Masera, G. Giacomelli, Marco Monteno, C. Bloise, P. Fusco, W. A. Worstell, S. Petrera, Andrea Carlo Marini, C. Lee, N. Giglietto, L. Foti, G. Martellotti, D. Campana, Robert A. Cormack, C. DeMarzo, M. Carboni, G. Giannini, Vincenzo Patera, R. Antolini, A. Sciubba, A. Baldini, J. Steele, G. Ludlam, Barbarino, Giancarlo, Guarino, Fausto, Ahlen, S, Ambrosio, M, Antolini, R, Auriemma, G, Baldini, A, Bam, B, Barbarino, G, Barish, B, Battistoni, G, Bellotti, R, Bemporad, C, Bernardini, P, Bilokon, H, Bisi, V, Bloise, C, Bussino, Severino Angelo Maria, Cafagna, F, Calicchio, M, Campana, P, Campana, D, Carboni, M, Cecchini, S, Cei, F, Chiarella, V, Chiera, C, Cobis, A, Cormack, R, Corona, A, Coutu, S, Decataldo, G, Dekhissi, H, Demarzo, C, Devincenzi, M, Dicredico, A, Diehl, E, Erriquez, O, Favuzzi, C, Ficenec, D, Forti, C, Foti, L, Fusco, P, Giacomelli, G, Giannini, G, Giglietto, N, Giubellino, P, Grassi, M, Green, P, Grillo, A, Guarino, F, Gustavino, C, Habig, A, Heinz, R, Hong, J, Iarocci, E, Katsavounidis, E, Kearns, E, Klein, S, Kyriazopoulou, S, Lamanna, E, Lane, C, Lee, C, Levin, D, Lipari, P, Liu, G, Liu, R, Longo, M, Ludlam, G, Mancarella, G, Mandrioli, G, Margiottaneri, A, Marin, A, Marini, A, Martello, D, Martellotti, G, Chiesa, Am, Masera, M, Matteuzzi, P, Michael, D, Miller, Jl, Monacelli, P, Monteno, M, Mufson, Sl, Musser, J, Nutter, S, Okada, C, Osteria, G, Palamara, O, Parlati, S, Patera, V, Patrizii, L, Pazzi, R, Peck, C, Petrakis, J, Petrera, S, Pignatano, N, Pistilli, P, Predieri, F, Ramello, L, Reynoldson, J, Ronga, F, Rosa, G, Satriano, C, Satta, L, Scapparone, E, Scholberg, K, Sciubba, A, Lugaresi, P, Severi, M, Sitta, M, Spinelli, P, Spinetti, M, Spurio, M, Steele, J, Steinberg, R, Stone, J, Sulak, L, Surdo, A, Tarle, G, Togo, V, Valente, V, Verdone, G, Walter, C, Webb, R, Worstell, W., Ahlen S., Ambrosio M., Antolini R., Auriemma G., Baldini A., Bam B., Barbarino G., Barish B., Battistoni G., Bellotti R., Bemporad C., Bernardini P., Bilokon H., Bisi V., Bloise C., Bussino S., Cafagna F., Calicchio M., Campana P., Campana D., Carboni M., Cecchini S., Cei F., Chiarella V., Chiera C., Cobis A., Cormack R., Corona A., Coutu S., DeCataldo G., Dekhissi H., DeMarzo C., De Vincenzi M., Di Credico A., Diehl E., Erriquez O., Favuzzi C., Ficenec D., Forti C., Foti L., Fusco P., Giacomelli G., Giannini G., Giglietto N., Giubellino P., Grassi M., Green P., Grillo A., Guarino F., Gustavino C., Habig A., Heinz R., Hong J., Iarocci E., Katsavounidis E., Kearns E., Klein S., Kyriazopoulou S., Lamanna E., Lane C., Lee C., Levin D., Lipari P., Liu G., Liu R., Longo M., Ludlam G., Mancarella G., Mandrioli G., Margiotta-Neri A., Marin A., Marini A., Martello D., Martellotti G., Marzari Chiesa A., Masera M., Matteuzzi P., Michael D., Miller J.L., Monacelli P., Monteno M., Mufson S.L., Musser J., Nutter S., Okada C., Osteria G., Palamara O., Parlati S., Patera V., Patrizii L., Pazzi R., Peck C., Petrakis J., Petrera S., Pignatano N., Pistilli P., Predieri F., Ramello L., Reynoldson J., et al, S., Ahlen, M., Ambrosio, R., Antolini, G., Auriemma, A., Baldini, B., Bam, G., Barbarino, B., Barish, G., Battistoni, R., Bellotti, C., Bemporad, P., Bernardini, H., Bilokon, V., Bisi, C., Bloise, S., Bussino, F., Cafagna, M., Calicchio, P., Campana, D., Campana, M., Carboni, S., Cecchini, F., Cei, V., Chiarella, C., Chiera, A., Cobi, R., Cormack, A., Corona, S., Coutu, G., Decataldo, H., Dekhissi, C., Demarzo, M., de Vincenzi, A., di Credico, E., Diehl, O., Erriquez, C., Favuzzi, D., Ficenec, C., Forti, L., Foti, P., Fusco, G., Giacomelli, G., Giannini, N., Giglietto, P., Giubellino, M., Grassi, P., Green, A., Grillo, F., Guarino, C., Gustavino, A., Habig, R., Heinz, J., Hong, E., Iarocci, E., Katsavounidi, E., Kearn, S., Klein, S., Kyriazopoulou, E., Lamanna, C., Lane, C., Lee, D., Levin, P., Lipari, G., Liu, R., Liu, M., Longo, G., Ludlam, Mancarella, Giovanni, G., Mandrioli, A., Margiotta Neri, A., Marin, A., Marini, Martello, Daniele, G., Martellotti, A., Marzari Chiesa, M., Masera, P., Matteuzzi, D., Michael, J. L., Miller, P., Monacelli, M., Monteno, S. L., Mufson, J., Musser, S., Nutter, C., Okada, G., Osteria, O., Palamara, S., Parlati, V., Patera, L., Patrizii, R., Pazzi, C., Peck, J., Petraki, S., Petrera, N., Pignatano, P., Pistilli, F., Predieri, L., Ramello, J., Reynoldson, F., Ronga, G., Rosa, C., Satriano, L., Satta, E., Scapparone, K., Scholberg, A., Sciubba, P., Serra Lugaresi, M., Severi, M., Sitta, P., Spinelli, M., Spinetti, M., Spurio, J., Steele, R., Steinberg, J., Stone, L., Sulak, A., Surdo, G., Tarle, V., Togo, V., Valente, G., Verdone, C., Walter, R., Webb, W., Worstell, and The MACRO, Collaboration
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Physics ,Muon ,Elementary Particles ,Gamma Rays, Observations ,Detector ,Solid angle ,Astronomy and Astrophysics ,Cosmic ray ,Gamma rays: observations ,Declination ,Elementary particle ,Particle detector ,Nuclear physics ,Gamma Rays ,Space and Planetary Science ,Nuclear astrophysics ,Observations ,Lepton - Abstract
We have analyzed a sample of 1.8 x 10(6) muons with E(mu) greater-than-or-similar-to 1.3 TeV collected by the first and second supermodules of the MACRO detector at Gran Sasso during the period 1989 February to 1991 February. We have searched for an excess of muons of celestial origin over cosmic-ray background. Our search for steady sources in solid angle bins of DELTAOMEGA almost-equal-to 3.0-degrees x 3.0-degrees in the declination range -5-degrees less-than-or-equal-to delta less-than-or-equal-to 90-degrees was negative; the upper limit with 95% C.L. to the muon flux at mid-latitudes (delta approximately 45-degrees) is J(mu)steady less-than-or-similar-to 2 x 10(-12) cm-2 s-1. In addition, we have searched for muon excesses modulated by the orbital period of selected X-ray sources, including Cyg X-3, Cyg X-1, Her X-1, 4U 0115+63, and 4U 1907+09. For Cyg X-3 we obtained an upper limit with 95% C.L. of J(mu)mod less-than-or-equal-to 8.8 x 10(-13) cm-2 s-1. Further, we have no evidence of any bursting activity from Cyg X-3, during our search period, which includes the radio outburst of 1991 January.
17. Scalable microfluidic method for tunable liposomal production by a design of experiment approach.
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Buttitta G, Bonacorsi S, Barbarito C, Moliterno M, Pompei S, Saito G, Oddone I, Verdone G, Secci D, and Raimondi S
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- Doxorubicin chemistry, Doxorubicin analogs & derivatives, Phosphatidylethanolamines chemistry, Particle Size, Chemistry, Pharmaceutical methods, Sphingomyelins chemistry, Technology, Pharmaceutical methods, Drug Compounding methods, Phosphatidylcholines chemistry, Drug Delivery Systems, Liposomes, Cholesterol chemistry, Polyethylene Glycols chemistry, Microfluidics methods
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Liposomes constitute a widespread drug delivery platform, gaining more and more attention from the pharmaceutical industry and process development scientists. Their large-scale production as medicinal products for human use is all but trivial, especially when parenteral administration is required. In this study an off-the-shelf microfluidic system and a methodological approach are presented for the optimization, validation and scale-up of highly monodisperse liposomes manufacturing. Starting from a Doxil®-like formulation (HSPC, MPEG-DSPE and cholesterol), a rational approach (Design of Experiments, DoE) was applied for the screening of the process parameters affecting the quality attributes of the product (mainly size and polydispersity). Additional DoEs were conducted to determine the effect of critical process parameters "CPPs" (cholesterol concentration, total flow rate "TFR" and flow rate ratio "FRR"), thus assessing the formulation and process robustness. A scale-up was then successfully accomplished. The procedure was applied to a Marqibo®-like formulation as well (sphingomyelin and cholesterol) to show the generality of the proposed formulation, process development and scale-up approach. The application of the system and method herein presented enables the large-scale manufacturing of liposomes, in compliance with the internationally recognized regulatory standards for pharmaceutical development (Quality by Design)., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier B.V. All rights reserved.)
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- 2024
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18. A systematic review of variations in circadian rhythm genes and type 2 diabetes.
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Stevens H, Verdone G, Lang L, Graham C, Pilic L, and Mavrommatis Y
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- Male, Female, Humans, Receptors, Melatonin, Circadian Rhythm genetics, Sleep genetics, Diabetes Mellitus, Type 2 genetics, Melatonin
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Background: Type 2 diabetes is a chronic disease that has severe individual and societal consequences, which is forecast to worsen in the future. A new field of investigation is variations in circadian rhythm genes, in conjunction with diet and sleep variables, associations with, and effects on, type 2 diabetes development., Objective: This systematic review aimed to analyse all current literature regarding circadian rhythm gene variations and type 2 diabetes, and explore their interplay with diet and sleep variables on type 2 diabetes outcomes. This review was registered with PROSPERO (CRD42021259682)., Methodology: Embase and Pubmed were searched on 6/8/2021/11/8/2021 for studies of all designs, including participants from both sexes, all ethnicities, ages, and geographic locations. Participants with risk alleles/genotypes were compared with the wildtype regarding type 2 diabetes outcomes. Studies risk of bias were scored according to the risk of bias in non-randomised studies - interventions/exposures criteria., Results: In total, 31 studies were found (association n = 29/intervention n = 2) including >600,000 participants from various ethnicities, sexes, and ages. Variations in the melatonin receptor 1B, brain and muscle arnt-like 1 and period circadian regulator (PER) genes were consistently associated with type 2 diabetes outcomes., Conclusions: Individuals with variations in melatonin receptor 1B, brain and muscle arnt-like 1 and PER may be at higher risk of type 2 diabetes. Further research is needed regarding other circadian rhythm genes. More longitudinal studies and randomised trials are required before clinical recommendations can be made., Competing Interests: Declaration of conflicting interestsThe authors disclosed receipt of the following financial support for the research, authorship, and/or publication of this article: LP is the founder of Optimyse Nutrition LTD, a personalised nutrition company offering genetic testing to clients.
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- 2024
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19. Personalized Nutrition in the Management of Female Infertility: New Insights on Chronic Low-Grade Inflammation.
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Fabozzi G, Verdone G, Allori M, Cimadomo D, Tatone C, Stuppia L, Franzago M, Ubaldi N, Vaiarelli A, Ubaldi FM, Rienzi L, and Gennarelli G
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- Animals, Female, Humans, Inflammation, Metabolomics, Nutrigenomics methods, Nutritional Status, Infertility, Female therapy
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Increasing evidence on the significance of nutrition in reproduction is emerging from both animal and human studies, suggesting a mutual association between nutrition and female fertility. Different "fertile" dietary patterns have been studied; however, in humans, conflicting results or weak correlations are often reported, probably because of the individual variations in genome, proteome, metabolome, and microbiome and the extent of exposure to different environmental conditions. In this scenario, "precision nutrition", namely personalized dietary patterns based on deep phenotyping and on metabolomics, microbiome, and nutrigenetics of each case, might be more efficient for infertile patients than applying a generic nutritional approach. In this review, we report on new insights into the nutritional management of infertile patients, discussing the main nutrigenetic, nutrigenomic, and microbiomic aspects that should be investigated to achieve effective personalized nutritional interventions. Specifically, we will focus on the management of low-grade chronic inflammation, which is associated with several infertility-related diseases.
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- 2022
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20. NMR-based homology model for the solution structure of the C-terminal globular domain of EMILIN1.
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Verdone G, Corazza A, Colebrooke SA, Cicero D, Eliseo T, Boyd J, Doliana R, Fogolari F, Viglino P, Colombatti A, Campbell ID, and Esposito G
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- Amides chemistry, Complement C1q chemistry, Complement C1q genetics, Computer Simulation, Crystallography, X-Ray, Humans, Membrane Glycoproteins genetics, Models, Molecular, Protein Conformation, Sequence Alignment, Sequence Homology, Amino Acid, Membrane Glycoproteins chemistry, Nuclear Magnetic Resonance, Biomolecular methods, Protein Structure, Tertiary, Structural Homology, Protein
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EMILIN1 is a glycoprotein of elastic tissues that has been recently linked to the pathogenesis of hypertension. The protein is formed by different independently folded structural domains whose role has been partially elucidated. In this paper the solution structure, inferred from NMR-based homology modelling of the C-terminal trimeric globular C1q domain (gC1q) of EMILIN1, is reported. The high molecular weight and the homotrimeric structure of the protein required the combined use of highly deuterated (15)N, (13)C-labelled samples and TROSY experiments. Starting from a homology model, the protein structure was refined using heteronuclear residual dipolar couplings, chemical shift patterns, NOEs and H-exchange data. Analysis of the gC1q domain structure of EMILIN1 shows that each protomer of the trimer adopts a nine-stranded beta sandwich folding topology which is related to the conformation observed for other proteins of the family. Distinguishing features, however, include a missing edge-strand and an unstructured 19-residue loop. Although the current data do not allow this loop to be precisely defined, the available evidence is consistent with a flexible segment that protrudes from each subunit of the globular trimeric assembly and plays a key role in inter-molecular interactions between the EMILIN1 gC1q homotrimer and its integrin receptor alpha4beta1.
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- 2009
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21. The solution structure of EMILIN1 globular C1q domain reveals a disordered insertion necessary for interaction with the alpha4beta1 integrin.
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Verdone G, Doliana R, Corazza A, Colebrooke SA, Spessotto P, Bot S, Bucciotti F, Capuano A, Silvestri A, Viglino P, Campbell ID, Colombatti A, and Esposito G
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- Blood Pressure physiology, Cell Adhesion physiology, Female, Glycoproteins chemistry, Glycoproteins genetics, Glycoproteins metabolism, Homeostasis physiology, Humans, Integrin alpha4beta1 genetics, Jurkat Cells, Membrane Glycoproteins genetics, Mutagenesis, Site-Directed, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Quaternary physiology, Protein Structure, Secondary physiology, Protein Structure, Tertiary physiology, Structure-Activity Relationship, Trophoblasts metabolism, Uterus metabolism, Cell Movement physiology, Integrin alpha4beta1 chemistry, Integrin alpha4beta1 metabolism, Membrane Glycoproteins chemistry, Membrane Glycoproteins metabolism, Models, Molecular
- Abstract
The extracellular matrix protein EMILIN1 (elastin microfibril interface located protein 1) is implicated in maintaining blood pressure homeostasis via the N-terminal elastin microfibril interface domain and in trophoblast invasion of the uterine wall via the globular C1q (gC1q) domain. Here, we describe the first NMR-based homology model structure of the human 52-kDa homotrimer of the EMILIN1 gC1q domain. In contrast to all of the gC1q (crystal) structures solved to date, the 10-stranded beta-sandwich fold of the gC1q domain is reduced to nine beta strands with a consequent increase in the size of the central cavity lumen. An unstructured loop, resulting from an insertion unique to EMILIN1 and EMILIN2 family members and located at the trimer apex upstream of the missing strand, specifically engages the alpha4beta1 integrin. Using both Jurkat T and EA.hy926 endothelial cells as well as site-directed mutagenesis, we demonstrate that the ability of alpha4beta1 integrins to recognize the trimeric EMILIN1 gC1q domain mainly depends on a single glutamic acid residue (Glu(933)). Static and flow adhesion of T cells and haptotactic migration of endothelial cells on gC1q is fully dependent on this residue. Thus, EMILIN1 gC1q-alpha4beta1 represents a unique ligand/receptor system, with a requirement for a 3-fold arrangement of the interaction site.
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- 2008
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22. Gene synthesis, expression, purification, and characterization of human Jagged-1 intracellular region.
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Popovic M, Coglievina M, Guarnaccia C, Verdone G, Esposito G, Pintar A, and Pongor S
- Subjects
- Calcium-Binding Proteins chemistry, Calcium-Binding Proteins genetics, Chromatography, Liquid, Circular Dichroism, Drosophila Proteins, Escherichia coli genetics, Gene Expression genetics, Humans, Intercellular Signaling Peptides and Proteins chemistry, Intercellular Signaling Peptides and Proteins genetics, Jagged-1 Protein, Membrane Proteins chemistry, Membrane Proteins genetics, Protein Binding genetics, Protein Structure, Tertiary genetics, Receptors, Notch genetics, Recombinant Proteins chemistry, Recombinant Proteins genetics, Serrate-Jagged Proteins, Calcium-Binding Proteins biosynthesis, Calcium-Binding Proteins isolation & purification, Genes, Synthetic genetics, Intercellular Signaling Peptides and Proteins biosynthesis, Intercellular Signaling Peptides and Proteins isolation & purification, Membrane Proteins biosynthesis, Membrane Proteins isolation & purification, Recombinant Proteins biosynthesis, Recombinant Proteins isolation & purification
- Abstract
Notch signaling plays a key role in cell differentiation and is very well conserved from Drosophila to humans. Ligands of Notch receptors are type I, membrane spanning proteins composed of a large extracellular region and a 100-150 residue cytoplasmic tail. We report here, for the first time, the expression, purification, and characterization of the intracellular region of a Notch ligand. Starting from a set of synthetic oligonucleotides, we assembled a synthetic gene optimized for Escherichia coli codon usage and encoding the cytoplasmic region of human Jagged-1 (residues 1094-1218). The protein containing a N-terminal His(6)-tag was over-expressed in E. coli, and purified by affinity and reversed phase chromatography. After cleavage of the His(6)-tag by a dipeptidyl aminopeptidase, the protein was purified to homogeneity and characterized by spectroscopic techniques. Far-UV circular dichroism, fluorescence emission spectra, fluorescence anisotropy measurements, and (1)H nuclear magnetic resonance spectra, taken together, suggest that the cytoplasmic tail of human Jagged-1 behaves as an intrinsically unstructured domain in solution. This result was confirmed by the high susceptibility of the recombinant protein to proteolytic cleavage. The significance of this finding is discussed in relation to the recently proposed role of the intracellular region of Notch ligands in bi-directional signaling.
- Published
- 2006
- Full Text
- View/download PDF
23. Solution structure of beta(2)-microglobulin and insights into fibrillogenesis.
- Author
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Esposito G, Corazza A, Viglino P, Verdone G, Pettirossi F, Fogolari F, Makek A, Giorgetti S, Mangione P, Stoppini M, and Bellotti V
- Subjects
- Crystallography, X-Ray, Drug Stability, Evolution, Molecular, Humans, Models, Molecular, Mutation, Nuclear Magnetic Resonance, Biomolecular, Solutions, Thermodynamics, beta 2-Microglobulin genetics, Amyloid chemistry, Protein Conformation, beta 2-Microglobulin chemistry
- Abstract
The solution structure of human beta(2)-microglobulin (beta(2)-m) was determined by (1)H NMR spectroscopy and restrained modeling calculations. Compared to the crystal structure of type I major histocompatibility complex (MHC-I), where the protein is associated to the heavy-chain component, several differences are observed, i.e., increased separation between strands A and B, displacements of strand C' and loop DE, shortening of strands D and E. These modifications can be considered as the prodromes of the amyloid transition. Even minor charge changes in response to pH, as is the case with H31 imidazole protonation, trigger the transition that starts with unpairing of strand A. The same mechanism accounts for the partial unfolding and fiber formation subsequent to Cu(2+) binding which is shown to occur primarily at H31. Solvation of the protected regions in MHC-I decreases the tertiary packing by breaking the contiguity of the surface hydrophobic patches via surface charge cluster. Mutants or truncated forms of beta(2)-m can be designed to remove the instability from H31 titration or to enhance the instability through surface charge suppression. By monitoring the conformational evolution of wild-type protein and variants thereof, either in response or absence of external perturbation, valuable insights into intermediate structure and fibrillogenesis mechanisms are gained.
- Published
- 2005
- Full Text
- View/download PDF
24. Sequence-specific backbone NMR assignments for the C-terminal globular domain of EMILIN-1.
- Author
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Verdone G, Colebrooke SA, Boyd J, Viglino P, Corazza A, Doliana R, Mungiguerra G, Colombatti A, Esposito G, and Campbell ID
- Subjects
- Carbon chemistry, Humans, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Recombinant Proteins chemistry, Magnetic Resonance Spectroscopy methods, Membrane Glycoproteins chemistry
- Published
- 2004
- Full Text
- View/download PDF
25. Properties of some variants of human beta2-microglobulin and amyloidogenesis.
- Author
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Corazza A, Pettirossi F, Viglino P, Verdone G, Garcia J, Dumy P, Giorgetti S, Mangione P, Raimondi S, Stoppini M, Bellotti V, and Esposito G
- Subjects
- Amyloid metabolism, Amyloidosis metabolism, Humans, Models, Molecular, Mutation, Protein Conformation, Protein Denaturation, Structure-Activity Relationship, beta 2-Microglobulin genetics, beta 2-Microglobulin metabolism, beta 2-Microglobulin chemistry
- Abstract
Three variants of human beta(2)-microglobulin (beta(2)-m) were compared with wild-type protein. For two variants, namely the mutant R3Abeta(2)-m and the form devoid of the N-terminal tripeptide (DeltaN3beta(2)-m), a reduced unfolding free energy was measured compared with wild-type beta(2)-m, whereas an increased stability was observed for the mutant H31Ybeta(2)-m. The solution structure could be determined by (1)H NMR spectroscopy and restrained modeling only for R3Abeta(2)-m that showed the same conformation as the parent species, except for deviations at the interstrand loops. Analogous conclusions were reached for H31Ybeta(2)-m and DeltaN3beta(2)-m. Precipitation and unfolding were observed over time periods shorter than 4-6 weeks with all the variants and, sometimes, with wild-type protein. The rate of structured protein loss from solution as a result of precipitation and unfolding always showed pseudo-zeroth order kinetics. This and the failure to observe an unfolded species without precipitation suggest that a nucleated conformational conversion scheme should apply for beta(2)-m fibrillogenesis. The mechanism is consistent with the previous and present results on beta(2)-m amyloid transition, provided a nucleated oligomeric species be considered the stable intermediate of fibrillogenesis, the monomeric intermediate being the necessary transition step along the pathway from the native protein to the nucleated oligomer.
- Published
- 2004
- Full Text
- View/download PDF
26. The solution structure of human beta2-microglobulin reveals the prodromes of its amyloid transition.
- Author
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Verdone G, Corazza A, Viglino P, Pettirossi F, Giorgetti S, Mangione P, Andreola A, Stoppini M, Bellotti V, and Esposito G
- Subjects
- Amino Acid Sequence, Humans, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Protein Structure, Secondary, Protein Structure, Tertiary, Solutions, Amyloid chemistry, beta 2-Microglobulin chemistry
- Abstract
The solution structure of human beta2-microglobulin (beta2-m), the nonpolymorphic component of class I major histocompatibility complex (MHC-I), was determined by (1)H NMR spectroscopy and restrained modeling calculations. Compared to previous structural data obtained from the NMR secondary structure of the isolated protein and the crystal structure of MHC-I, in which the protein is associated to the heavy-chain component, several differences are observed. The most important rearrangements were observed for (1) strands V and VI (loss of the C-terminal and N-terminal end, respectively), (2) interstrand loop V-VI, and (3) strand I, including the N-terminal segment (displacement outward of the molecular core). These modifications can be considered as the prodromes of the amyloid transition. Solvation of the protected regions in MHC-I decreases the tertiary packing by breaking the contiguity of the surface hydrophobic patches at the interface with heavy chain and the nearby region at the surface charge cluster of the C-terminal segment. As a result, the molecule is placed in a state in which even minor charge and solvation changes in response to pH or ionic-strength variations can easily compromise the hydrophobic/hydrophilic balance and trigger the transition into a partially unfolded intermediate that starts with unpairing of strand I and leads to polymerization and precipitation into fibrils or amorphous aggregates. The same mechanism accounts for the partial unfolding and fiber formation subsequent to Cu(2+) binding, which is shown to occur primarily at His 31 and involve partially also His 13, the next available His residue along the partial unfolding pathway.
- Published
- 2002
- Full Text
- View/download PDF
27. Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation.
- Author
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Esposito G, Michelutti R, Verdone G, Viglino P, Hernández H, Robinson CV, Amoresano A, Dal Piaz F, Monti M, Pucci P, Mangione P, Stoppini M, Merlini G, Ferri G, and Bellotti V
- Subjects
- Amino Acid Sequence, Amyloid ultrastructure, Benzothiazoles, Chromatography, Gel, Circular Dichroism, DNA, Complementary metabolism, Humans, Hydrogen Bonding, Hydrogen-Ion Concentration, Light, Magnetic Resonance Spectroscopy, Mass Spectrometry, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Structure, Secondary, Recombinant Proteins chemistry, Scattering, Radiation, Temperature, Thermodynamics, Thiazoles metabolism, Time Factors, Amyloid chemistry, beta 2-Microglobulin chemistry
- Abstract
The solution structure and stability of N-terminally truncated beta2-microglobulin (deltaN6beta2-m), the major modification in ex vivo fibrils, have been investigated by a variety of biophysical techniques. The results show that deltaN6beta2-m has a free energy of stabilization that is reduced by 2.5 kcal/mol compared to the intact protein. Hydrogen exchange of a mixture of the truncated and full-length proteins at microM concentrations at pH 6.5 monitored by electrospray mass spectrometry reveals that deltaN6beta2-m is significantly less protected than its wild-type counterpart. Analysis of deltaN6beta2-m by NMR shows that this loss of protection occurs in beta strands I, III, and part of II. At mM concentration gel filtration analysis shows that deltaN6beta2-m forms a series of oligomers, including trimers and tetramers, and NMR analysis indicates that strand V is involved in intermolecular interactions that stabilize this association. The truncated species of beta2-microglobulin was found to have a higher tendency to self-associate than the intact molecule, and unlike wild-type protein, is able to form amyloid fibrils at physiological pH. Limited proteolysis experiments and analysis by mass spectrometry support the conformational modifications identified by NMR and suggest that deltaN6beta2-m could be a key intermediate of a proteolytic pathway of beta2-microglobulin. Overall, the data suggest that removal of the six residues from the N-terminus of beta2-microglobulin has a major effect on the stability of the overall fold. Part of the tertiary structure is preserved substantially by the disulfide bridge between Cys25 and Cys80, but the pairing between beta-strands far removed from this constrain is greatly perturbed.
- Published
- 2000
- Full Text
- View/download PDF
28. The senior citizen - a community responsibility.
- Author
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VERDONE GF
- Subjects
- Humans, North Carolina, Geriatrics, Insurance, Health, Residence Characteristics
- Published
- 1961
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