178 results on '"Martorana, V."'
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2. Physics and biophysics of solvent induced forces: hydrophobic interactions and context-dependent hydration
- Author
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San Biagio, P. L., Bulone, D., Martorana, V., Palma-Vittorelli, M. B., and Palma, M. U.
- Published
- 1998
- Full Text
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3. K + and Na + effects on the gelation properties of κ-Carrageenan
- Author
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Mangione, M.R., Giacomazza, D., Bulone, D., Martorana, V., Cavallaro, G., and San Biagio, P.L.
- Published
- 2005
- Full Text
- View/download PDF
4. Thermoreversible gelation of κ-Carrageenan: relation between conformational transition and aggregation
- Author
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Mangione, M.R, Giacomazza, D, Bulone, D, Martorana, V, and San Biagio, P.L
- Published
- 2003
- Full Text
- View/download PDF
5. Contributory presentations/posters
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Gries, A., Singh, Balwinder, Nakazawal, Chicko, Genest, D., Getzoff, E. D., Matsuo, H., Kaur, Harpreet, Borst, J. W., Chadha, K. C., Tingyun, Kuang, Jagannadham, M. V., Leijon, Mikael, Sato, S., Bhakuni, Vlnod, Vijayan, M., Surolia, A., Suguna, K., Manoj, N., Srinivas, V. R., Ravishankar, R., Laggner, P., Prassl, R., Schwarzenbacher, R., Zeth, K., Kostner, G. M., Taylor, Susan S., Xuong, Nguyen-huu, Akamine, Pearl, Sagar, Bidva M., Saikrishnan, K., Purnapatre, K., Handa, P., Roy, S., Varshney, U., Biswal, B. K., Sukumar, N., Rao, J. K. Mohana, Johnson, A., Pattabhi, Vasantha, Murthy, M. R. N., Krishna, Sri S., Savithri, H. S., Sastri, Mira, Hosur, M. V., Pillai, Bindu, Kannan, K. K., Kumar, Mukesh, Patwardhan, Swati, Padmanabhaa, B., Sasaki-Sugio, S., Matsuzaki, T., Nukaga, M., Singh, T. P., Sharma, A. K., Srinivasan, A., Khan, J. A., Paramasivam, M., Kumar, P., Karthikevan, S., Sharma, S., Yadav, S., Srintvasan, A., Alam, Neelima, Gourinath, S., Kaur, Punit, Chandra, Vikas, Betzel, Ch., Ghosh, S., Bera, A. K., Pal, A. K., Baneriee, Asok, Mukhopadhyay, B. P., Bhattacharya, S., Chakraborty, S., Haldar, U., Dey, I., Solovicova, Adriana, Sevcik, Jozef, Sekar, K., Sundaralingam, M., Genov, N., Liang, Dong-cai, Zhang, Ji-ping, Jiang, Tao, Chang, Wen-rui, Blommers, Marcel, Jahnke, Wolfgang, Hosur, R. V., Panchal, S. C., Pillay, Bindu, Jaganathan, N. R., Mathur, Puniti, Srivatsun, S., Joshi, Ratan Mani, Chauhan, V. S., Govil, Girjesh, Atreya, H. S., Sahu, S. C., Quinjou, Éric, Adjadj, Elisabeth, Mispelter, Joël, Izadi-Pruneyre, Nadia, Blouquit, Yves, Heyd, Bernadette, Lerat, Guilhem, Desmadreil, Michel, Milnard, Philippe, Lin, Y., Rao, B. D. Nageswara, Raghunathan, Vidva, Chau, Mei H., Coutinho, Evans, Pesais, Prashant, Srivastava, Sudha, Saran, Anil, Srikrishnan, Thamarapu, Lijima, Herbert, Gesme, Jayson, Sapico, Leizl F., Paxton, Raymond, Grace, C. R., Nagenagowda, G., Lynn, A. M., Cowsik, Sudha M., Govil, G., Sahu, Sarata C., Bhattacharya, A., Chauhan, S., Kumar, Anil, Zuiderweg, Erik R. P., Pellecchia, Maurizio, Nitta, Katsutoshi, Ohnishi, Atsushi, Kawano, Keiichi, Hikichi, Kunio, Fujitani, Naoki, Ohkubo, Tadayasu, Aizawa, Tomoyasu, Kumaki, Yasuhiro, Hayakawa, Yoichi, Parvathy, Rani V., Kini, R. M., Nakagawa, Astushi, Tanaka, Isao, Demura, Makoto, Yao, Min, Koshiba, Takumi, Kobashigawa, Yoshihiro, Kuwajima, Kunihiro, Linge, Jens, Nilges, Michael, Donoghue, Seán O., Chakshusmathi, G., Ratnaparkhi, Girish S., Madhu, P. K., Varadarajan, R., Tetreau, C., Tourbez, M., Lavalette, D., Bulone, D., Manno, M., Emanuele, A., Palma-Vittorelli, M. B., Palma, M. U., Vaiana, S. M., Martorana, V., Biagio, P. L. San, Chang, D. K., Cheng, S. F., Yang, S. H., Francis, S., Trivedi, V. D., Chien, W. J., Manstein, Dietmar J., Batra, Renn, Geeves, Michael A., Geller, Maciej, Trvlska, Joanna, Grochowski, Pawel, Lesyng, B., Ginalski, K., Grochowski, P., Lavalette, P., Blouquit, Y., Roccatano, D., Berendsen, H. J. C., Amadei, A., Nola, Di A., Ho, Bosco, Curmi, P. M. G., Berry, H., Pelta, J., Pauthe, E., Lairez, D., Srinivasan, M., Sahi, Shakti, Kothekar, V., Madhusudnan, Kartha S., Nandel, Fateh S., Jain, D. V. S., Berendsen, Herman J. C., Feenstra, Anton K., Tama, F., Sanejouand, Y.-H., Go, N., Sharma, Deepak, Pasha, Santosh, Sharma, Sunita, Brahmachari, Samir K., Makker, Jyoti, Viiavaraghavan, R., Kumar, S., Dey, Sharmisllia, Krishnamoorthy, G., Lakshmikanth, G. S., Zaitseva, E. M., Mazhul, V. M., Kierdaszuk, Borys, Widengren, J., Rigler, R., Terry, B., Mets, Ü., Swaminathan, R., Yathindra, N., Thamotharan, S., Chosrowjan, H., Mataga, N., Shibata, Y., Morisima, I., Xiao, Ming, Selvin, Paul, Chakraharty, Tania, Cooke, Roger, Faraone, A., Branca, C., Maisano, G., Migliardo, P., Magazù, S., Villari, V., Behere, Digambar V., Deva, Sharique Zahida Waheed M., Vallone, B., Savino, C., Travaglini-Allocatelli, C., Cutruzzolà, F., Brunori, M., Gibson, Q. H., Mazumdar, Shyamalava, Mitra, Samaresh, Prasad, Swati, Soto, P., Fayad, R., Tyulkova, N. A., Sukovataya, I. E., Mamedov, Sh. V., Aksakal, B., Canturk, M., Aktas, B., Yilgin, R., Bogutska, K. I., Miroshnichenko, N. S., Wein, A. J., Hypolite, J. A., DiSanto, M., Chacko, S., Zheng, Y-M., Antosiewicz, J., Wojciechowski, M., Grycuk, T., Di Nola, Alfredo, Ceruso, Marc A., Chatterjee, Bishnu P., Bandvopadhvay, Subhasis, Choudhury, Devapriva, Khight, Stefan, Thompson, Andrew, Stojanoff, Vivian, Pinkner, Jerome, Hultgren, Scott, Flatters, Delphine, Goodfellow, Julia, Takazawatt, Fumi, Kanehisa, Minoru, Sasai, Masaki, Nakamura, Hironori, Wang, Bao Han, Pan, xin Min, Zheng, Yuan, Wang, Zhi Xin, Ahmad, Atta, Kulkarni, Sangeeta, Prakash, Koodathingal, Prajapati, Shashi, Surin, Alexey, Kihara, Hiroshi, Yang, Li, Matsumoto, Tomoharu, Nakagawa, Yuki, Semisotnov, Gennady V., Kimura, Kazumoto, Amemiya, Yoshiyuki, Tayyab, Saad, Muzammil, Salman, Kumar, Yogesh, Bhakuni, Vinod, Sundd, Monica, Kundu, Suman, Jagannadham, Medicherla V., Chandani, Bina, Warrier, Deepti, Sinha, Lalankumar, Dhar, Ruby, Mehrotra, Sonam, Khandelwal, Purnima, Seth, Subhendu, Gidwani, Arun, Prabha, Ratna C., Sasidhar, Y. U., Madhusudan, K. P., Nishikawa, Ken, Kinjo, Akira R., Varadarajan, Raghavan, Chakravarty, Suvobrata, Van Dael, H., Noyelle, K., Joniau, M., Haezebrouck, P., Jha, Indra Brata, Bhat, Rajiv, Dash, Sheffali, Mohanty, Prasanna, Bandyopadhyay, A. K., Sonawat, H. M., Rao, Ch. Mohan, Datta, Siddhartha, Raman, B., Rajaraman, K., Ramakrishna, T., Pande, A., Benedek, G., King, J., Betts, S., Pande, J., Asherie, N., Ogun, O., Kalacheva, G. S., Sokolova, I. V., Mitaku, Shigeki, Sonoyama, Masashi, Taira, Kunihiro, Yokoyama, Yasunori, Sasakil, Takanori, Kamo, Naoki, Mukai, Yuri, Dalal, Seema, Regan, Lynne, Mituku, Shigeki, Kumar, Devesh, Roychoudhury, Mihir, Lőrinczv, Dénes, Könczöl, Franciska, Farkas, László, Belagyi, Joseph, Schick, Christoph, Thomson, Christy A., Ananthanarayanan, Vettai S., Alirzayeva, E. G., Baba-Zade, S. N., Sarai, A., Kono, H., Uedaira, H., An, J., Gromiha, Michael M., Oobatake, M., Yutani, Katsuhide, Takano, Kazufumi, Yamagata, Yuriko, Jas, Gouri S., Hofrichter, James, Muñoz, Victor, Eaton, William A., Penoyar, Jonathan, Lo Verde, Philip T., Bódi, Á., Venekei, I., Kardos, J., Gráf, L., Závodszky, P., Szilágyi, András, Závodszky, Péter, Woolfson, D. N., Walshaw, J., Allan, R. D., Funahashi, Jun, Gupta, Savan, Di Nola, A., Mangoni, M., Roccatano, P., Ramachandraiah, Gosu, Chandra, Nagasuma R., Ciani, Barbara, Woolfson, Derek N., Nair, Usha B., Salunke, Dinakar M., Kaur, Kanwal J., Swaminathan, Chittoor P., Surolia, Avadhesha, Pramanik, A., Jörnvall, H., Nygren, P.-Å., Jonasson, P., Ståhl, S., Johansson, B.-L., Kratz, G., Wahren, J., Ekberg, K., Uhlén, M., Jansson, O. T., Uhlén, S., Misselwitz, Rolf, Welfle, Heinz, Welfle, Karin, Höhne, Wolfgang, Kurganov, B. I., Mitskevich, L. G., Fedurkina, N. V., Jarori, Gotam K., Maity, Haripada, Guharay, J., Sengupta, P. K., Sengupta, B., Sridevi, K., Kasturi, S. R., Gupta, S. P., Agarwal, Gunjan, Briehl, Robin W., Kwong, Suzanne, Tyulkova, N A., Ismailova, O. I., Parola, A. H., Yayon, A., Hariharan, C., Pines, D., Pines, E., Zamai, M., Cohen-Luria, R., Woolfeon, D. N., Spooner, G. A., Padya, M. J., Bharadwaj, D. K., Bakshi, Panchan, Jagannathan, N. R., Sharma, U., Srivastava, N., Barthwal, R., Matsuda, Keiko, Nishioka, Takaaki, Go, Nobuhiro, Urata, S., Aita, T., Husimi, Y., Majumder, Mainak, Subirana, Juan A., Malinina, Lucy, Abrescia, Nicola G. A., Aymami, Juan, Coll, Miquel, Eritxa, Ramón, Premraj, B. J., Thenmalarchelvi, R., Gautham, N., Kumar, Satheesh P., Kan, Lou-Sing, Hou, Ming, Lin, Shwu-Bin, Roy, Kanal B., Sana, Tapas, Bruant, N., Flatters, D., Lavery, R., Sklenar, Heinz, Rons, Remo, Lavery, Richard, Thakur, Ashoke Ranjan, Kundu, Sudip, Bandyopadhyay, Debashree, Bhattacharyya, Dhananjay, Majumdar, Rabi, Barceló, F., Portugal, J., Rao, B. J., Ramanathan, Sunita, Gliosli, Mahua, Varshney, Umesh, Kumar, Vinay N., Pataskar, Shashank S., Sarojini, R., Selvasekarapandian, S., Kolandaivel, P., Sukumar, S., Kolmdaivel, P., Maiti, Motilal, Das, Suman, Sen, Anjana, Xodo, Luigi, Suraci, Chiara, Del Terra, Elisa, Quadrifoglio, Franco, Diviacco, Silvia, Ray, Arghya, Rao, Basuthkar J., Karthikeyan, G., Chary, Kandala V. R., Mujeeb, Anwer, James, Thomas L., Bogdanov, A., Zanina, A., Haya, E. E. F., Kasyanenko, N., Cornélio, M. L., Bugs, M. R., Tolstorukov, Ye. M., Sanval, Nitish K., Tiwari, S. N., Sanyal, Nitish K., Choudhury, Mihir Roy, Patel, P. K., Bhavesh, Neel S., Gabrielian, Anna, Rigler, Rudolf, Edman, Lars, Wennmalm, Stefan, Constantinescu, B., Gazdaru, D., Radulcscu, I., Radu, L., Wärmländer, Sebastian, Aoki, Setsuyuki, Ishiura, Masahiro, Kondo, Takao, Pashinskaya, V. A., Kosevich, M. V., Shelkovsky, V. S., Blagoy, Yu. P., Wang, Ji-hua, Malathi, R., Chandrasekhar, K., Kandimalla, E. R., Agrawal, S., Rastogi, V. K., Palafox, Alcolea M., Singh, Chatar, Beniaminov, A. D., Minyat, E. E., Zdobnov, E. M., Ulyanov, N. B., Bondarenko, S. A., Ivanov, V. I., Singh, J. S., Tewari, Ravindra, Sonawane, Kailas D., Grosjean, Henri, Sonavane, Uddhavesh B., Morin, Annie, Doherty, Elizabeth A., Doudna, Jennifer A., Tochio, H., Shirakawa, M., Kyogoku, Y., Das, Achintya, Javaram, B., Kalra, Parul, Shukla, Piyush, Dixit, Surjit B., Beveridge, David L., McConnell, Kevin, Davidson, B. E., Chan, R. Y. S., Sawyer, W. H., Eccelston, J. F., Yan, Yuling, Norden, Bengt, Tuite, Eimer, Nielsen, Peter, Takahashi, Masayuki, Ghosh, Anirban, Bansal, Manju, Pingoud, Alfred, Christ, Frauke, Thole, Hubert, Pingoud, Vera, Wende, Wolfgang, Luthra, Pratibha Mehta, Chandra, Ramesh, Sen, Ranjan, Weisberg, Robert, King, Rodney, Gobets, Bas, van Amerongen, Herbert, van Stokkum, Ivo H. M., Larsen, Olaf F. A., van Grondelle, Rienk, Hilbers, Cornelis W., Heus, Hans A., Berends, Jos, Sngrvan, H E., Khudaverdian, N. V., Babayan, Yu. S., Pichierri, F., Gromiha, M., Prabakaran, P., Aida, M., Sayano, K., Merkienė, Eglė, Vilkaitis, Giedrius, Klimašauskas, Saulius, Serva, Saulius, Weinhold, Elmar, Bandiera, Antonella, Marsich, Eleonora, Manzini, Giorgio, Potikyan, G., Arakelyan, V., Babayan, Yu., Ninaber, Alex, Goodfellow, Julia M., Ohta, Shigeru, Ito, Yoichiro, Husimi, Yuzuru, Usukura, J., Aiba, H., Tagami, H., Nunes, Elia, Suarez, Mougli, Candreva, Carmen E., Keszenman, Deborah, Thyberg, Per, Földes-Papp, Zeno, Joshi, Amita, Singh, Dinesh, Rajeswari, M. R., Amenitsch, H., Pregetter, M., Chapman, J., Mishra, K. P., Pandev, B. N., Tonevitsky, A. G., Pohl, E. E., Agapov, I. I., Sun, J., Pohl, P., Dennison, S. M., Gorbeako, G. P., Dynbko, T. S., Mishra, A. K., Pappavee, N., Luis, Loura, Rodrigo, Almeida, Manuel, Prieto, Gendel, Ya. L., Kleszczyńska, H., Kuczera, J., Przestalski, S., Kral, T., Chernitsky, E. A., Senkovich, O. A., Rosin, V. V., Gasanov, R. A., Allakhverdieva, Y. M., Papageorgiou, G. C., Savopol, Tudor, Apetrei, Calin, Balea, Marius, Cucu, D., Mihailescu, D., Ramanathan, K. V., Bačić, Goran, Genest, Monique, Sajot, Nicolas, Garnier, Norbert, Crouzy, Serge, Zsiros, O., Várkonyi, Z. S., Combos, Z., Farkas, T., Cribier, Sophie, de Paula, F., Fraceto, I. F., Schreier, S., Spisni, A., Sevšek, F., Žekš, B., Gomišček, G., Svetina, S., Arrigler, V., Hotani, Hirokazu, Nomura, Fumimasa, Takiguchi, Kingo, Nagata, Miki, Panicker, Lata, Parvathanathan, P. S., Hotani, H., Takiguchi, K., Ishino, A., Saitoh, A., Afonin, S., Takahashi, A., Takizawa, T., Nakato, Y., Marathe, Dipti, Jørgensen, Kent, Chattopadhyay, Amitabha, Rukmini, R., Rawat, Satinder S., Pečar, S., Štrancar, J., Šentiurc, M., Stolič, Z., Filipin, K., Biswas, S. C., Samanta, Anunay, Sana, Satyen, Kinoshita, Koji, Yamazaki, Masahito, Ohki, Kazuo, Goto, Akira, Kiuchi, Tai, Kumeta, Takaaki, Ohba, Tetsuhiko, Sugar, I. P., Thompson, K. K., Biltonen, R. L., Thompson, T. E., Ichinose, H., Suezaki, Y., Akivama, M., Matuoka, S., Tsuchihashi, K., Gasa, S., Pike, H. M., Mattjus, P., Brown, R. E., Molotkovsky, J. G., Arora, Ashish, Kleinschmidt, Jörg H., Tamm, Lukas K., Kruglyakova, K. E., Luneva, O. G., Fedin, V. A., Kuptsoya, O. S., Visser, A. J. W. G., Visser, N. V., Dyubko, T. S., Ogihara, Toshihiko, Mishima, Kiyoshi, Shvaleva, A. L., Radenović, Č. N., Jeremić, M. G., Radenović, N. Č., Minić, P. M., Salakhutdinov, B. A., Aripov, T. F., Tadjibaeva, E. T., Zamaraeva, M. V., Vagina, O. N., Basak, A. K., Cole, A., Naylor, C., Poppofl, M., Titball, R., Naylor, C. E., Moss, D. S., Eaton, J. T., Justin, N., Titball, R. W., Nomura, F., Nagata, M., Ishjkawa, S., Takahashi, S., Obuchi, Kaoru, Staudegger, Erich, Lohner, Karl, Kriechbaum, Manfred, Waring, Alan J., Lehrer, Robert I., Mayer, Bernd, Köhler, Gottfried, Gangl, Susanne, Shobini, J., Hu, B., Lortz, B., Sackmann, E., Guttenberg, Z., Antonovich, A. N., Slobozhanina, E. I., Lukyanenko, L. M., Kozlova, N. M., Krylov, Andrey V., Kotova, Elena A., Antonenko, Yuri N., Yaroslavov, Alexander A., Ghosh, Subhendu, Bera, Amal K., Das, Sudipto, Urbánková, Eva, Freeman, Karl, Jelokhani-Niaraki, Masood, Jezek, Petr, Usmanov, P. B., Tonkikh, A. K., Ongarbaev, A., Pohl, Peter, Saparov, Sapar M., Harikumar, P., Reeves, J. P., Sikdar, S. K., Rao, S., Ghatpande, A. S., Corsso, C., Varanda, W. A., ElHamel, C., Dé, E., Molle, G., Saint, N., Varshney, Anurae, Mathew, M. K., Isacoff, E. Y., Loots, E., Kasai, Michiki, Yamaguchi, Naohiro, Ghosh, Paramita, Tigyi, Joseph, Miledi, Ricardo, Tigyi, Gabor, Liliom, Karoly, Djurisic, Maja R., Andjus, Pavle R., Shrivastava, Indira H., Sansom, M. S. P., Barrias, C., Oliveira, P. F., Lopes, I. A., Mauricio, A. C., Fedorovich, S. V., Konev, S. V., Sholukh, M. V., Chubanov, V. S., Klevets, M., Fedirko, N., Shvinka, N., Manko, V., Prabhananda, B. S., Kombrabail, Mamata H., Aravamudhan, S., Venegas-Cotero, Berenice, Blake, Ivan Ortega, Zhou, Han-qing, Hu, Xiao-jian, Zhang, Zhi-hong, Feng, Hang-fang, Cheng, Wei-ying, Zalyvsky, I. A., Dubitsky, L. O., Vovkanvch, L. S., Savio-Galimberti, E., Ponce-Homos, J. E., Bonazzola, P., Capurro, Claudia, Parisi, Mario, Toriano, Roxana, Thomas, David D., Ready, Laxma G., Jones, Larry R., Tashmukhamedov, B. A., Sagdullaev, B. T., Heitzmann, D., Bleich, M., Warth, R., Ferreira, H. G., Ferreira, K. T. G., Greger, R., Parola, Abraham H., Alfahel, Essa, Zagoory, Orna, Priel, Zvi, Hama-Inaba, H., Ohyama, H., Hayata, I., Choi, K., Haginoya, K., Mori, M., Wang, R., Yukawa, O., Nakajima, T., Joshi, Nanda B., Kannurpatti, Sridhar K., Sinha, Mau, Joshi, Preeti G., Bei, Ling, Hu, Tianhui, Shen, Xun, Knetsch, Menno L. W., Schäfers, Nicole, Sandblom, John, Galvanovskis, Juris, Kovacs, Eugenia, Dinu, Alexandra, Pologea-Moraru, Roxana, Sanghvi, S. H., Jazbinšek, V., Tronteli, Z., Thiel, G., Wübeller, G., Müller, W., Brumen, Milan, Fajmut, Leš, Marhl, Marko, Volotovski, I. D., Sokolovski, S. G., Knight, M. R., Chalyi, Alexander V., Vasilʼev, Alexei N., Sharma, P., Pant, H. C., Sharma, M., Amin, N. D., Albers, R. W., Steinbach, P. J., Barchir, J., Balasubramanyam, M., Gardner, J. P., Condrescu, M., Pilarczyk, Gotz, Greulich, K. O., Monajembashi, Shamci, El-Awadi, A. I., El-Refaei, F. M., Talaat, M. M., Ali, F. M., Zahradniková, Alexandra, Tahradník, Ivan, Pavelková, Jana, Zhorov, Boris S., Ananthanaravanan, Vettai S., Weiss, D. G., Martin, D., Gornik, E., Neu, E., Michailov, Ch. M., Welscher, U., Seidenbusch, W., Jellali, A., Pattnaik, B. R., Hicks, D., Dreyfus, H., Sahel, J., Picaud, S., Forster, V., Wang, Hong-Wei, Sui, Sen-fang, Luther, Pradeep K., Morris, Ed, Barry, John, Squire, John, Sundari, Sivakama C., Balasubramanian, D., Christlet, Hema Thanka T., Veluraia, K., Suresh, Xavier M., Laretta-Garde, V., Krilov, Dubravka, Herak, Janko N., Stojanović, Nataša, Ferrone, Frank A., Ivanova, Maria, Jasuja, Ravi, Mirchev, Rossen, Stopar, David, Wolfs, Cor J. A. M., Hemminga, Marcus A., Spruijt, Ruud B., Arcovito, G., De Spirito, M., Frank, Joachim, Heagle, Amy B., Grassucci, Robert, Penczek, Pawel, Agrawal, Rajendra K., Sharma, Manjuli R., Wagenknecht, Terence, Jeyakumar, Loice H., Fleischer, Sidney, Knupp, Carlo, Squire, John M., Ezra, Eric, Munro, Peter M. G., Kitazawa, Hidefumi, Ichihara, Koji, Itoh, Tomohiko J., Iguchi, Yusuke, Pifat, Greta, Kveder, Marina, Pečar, Slavko, Schara, Milan, Nair, Deepak, Singh, Kavita, Rao, Kanury V. S., Sundaravadivel, B., Jain, Deepti, Kaur, Kanwaljeet, Salunke, D. M., Goel, Manisha, Kovalenko, E. I., Semenkova, G. N., Cherenkevich, S. N., Loganathan, D., Lakshmanan, T., Sriram, D., Srinivasan, S., Lebrón, J. A., Bjorkman, P. J., Ramalingam, T. S., Singh, A. K., Gayatri, T. N., Bisch, Paulo M., Caffarena, Ernesto R., Grigera, Raul J., Fromherz, P., Kiessling, V., Suresh, C. G., Rao, K. N., Khan, M. I., Gaikwad, S. M., Elanthiraiyan, M., Kaliannan, P., Payne, J., Chadha, K., Ambrus, J. L., Nair, M. P. N., Nair, Madhavan P. N., Hewitt, R., Schwartz, S. A., Mahajan, S., Macherel, D., Bourguignon, J., Neuburger, M., Douce, R., Cohen-Addad, C., Faure, M., Ober, R., Sieker, L., Gurumurthy, D. S., Velmurugan, S., Lobo, Z., Phadke, Ratna S., Desai, Prashant, Alieva, D. R., Guseinova, I. M., Zulfugarov, I. S., Aliev, J. A., Ismayilov, M. A., Novruzova, S. N., Savchenko, T. V., Suleimanov, Yu. S., Bartošková, Hana, Nauš, Jan, Ilík, Petr, Kouřil, Roman, Vidyasagar, P. B., Thomas, Sarah, Gaikwad, Jvoti U., Cseh, Z., Mustárdy, L., Garab, G., Simidjiev, I., Rajagopal, S., Várkonyi, Zs., Holzenburg, A., Stoylova, S., Papp, E., Millar, D. P., Bruder, R., Woo, T. T., Genick, U. K., Gerwert, K., Jávorfí, Tamás, Garab, Győző, Naqvi, Razi K., Gaikwad, Jyoti, Kalimullah, Md., Semwal, Manoj, Naus, Man, Ilik, Petr, Kouril, Roman, Horváth, Gábor, Bernard, Gary D., Pomozi, István, Wehner, Rüdiger, Damjanović, Ana, Schulten, Klaus, Ritz, Thorsten, Yandao, Gong, Jushuo, Wang, Nanming, Zhao, Jixiu, Shan, Freiberg, Arvi, Timpmann, Kõu, Woodbury, Neal W., Ruus, Rein, Nemtseva, E. V., Kudryasheva, N. S., Sizykh, A. G., Tikhomirov, A. A., Nesterenko, T. V., Shikhov, V. N., Forti, Giorgio, Furia, Alberto, Finazzi, Giovanni, Barbagallo, Romina Paola, Agalarov, R., Gasanov, R., Iskenderova, S., Nobuhiro, G. O., Osamu, Miyashita, Ramrakhiani, M., Soni, R. K., Yoshida, Masasuke, Akutsu, Hideo, Yagi, Hiromasa, Tozawa, Kacko, Sekino, Nobuaki, Iwabuchi, Tomoyuki, Kaulen, A. D., Avetisyan, A. V., Feniouk, B. A., Skulachev, V. P., Breyton, Cécile, Kühlbrandt, Werner, Gräslund, Astrid, Assarsson, Maria, Libisch, B., Horváth, G., Gombos, Z., Budagovskaya, N. V., Kudryasheva, N., Fukunishi, Arima, Harada, Erisa, Fukuoka, Yuki, Ohmura, Tomoaki, Kawai, Gota, Watanabe, Kimitsuna, Žekš, Boštjan, Božič, Bojan, Derganc, Jure, Svetina, Saša, Hoh, J. F. Y., Li, Z. B., Rossmanith, G. H., Frederix, P. L. T. M., de Beer, E. L., Treijtel, B. W., Blangè, T., Galtet, F., Hénon, S., Isabey, D., Planus, E., Laurent, V., Rath, L. S., Raval, M. K., Dash, P. K., Ramakrishnan, C., Balaram, R., Basak, Kanika, Balaban, Alexandra T., Nandy, Ashesh, Grunwald, Gregory D., Vracko, Marjan, Randic, Milan, Basak, Subhash C., Amic, Dragan, Beslo, Drago, Trinajstic, Nenad, Nikolic, Sonja, Walahaw, J., Lensink, Marc F. J., Reddy, Boojala V. B., Shindylov, Ilya N., Bourne, Philip E., Grigera, J. R., de Xammar Oro, J., Donnamaria, M. C., Neagu, Monica, Neagu, Adrian, Janežič, Dušanka, Praprotnik, Matej, Nilsson, Lennart, Mark, Pekka, Fata, La L., Dardenne, Laurent E., Werneck, Araken S., Neto, Marçal de O., Kannan, N., Vishveshwara, S., Veluraja, K., Opitz, David, Balasubramanian, Krishnan, Gute, Brian D., Mills, Denise, Lungeanu, Diana, Mihalas, G. I., Macovievici, G., Gruia, Raluca, Dalcin, B., Cortez-Maghelly, C., Passos, E. P., Ljubisavljevic, M., Blesic, S., Milosevic, S., Stratimirovic, D. J., Bachhawat, Nandita, Mande, Shekhar C., Nandy, A., Nishigaki, Koichi, Saito, Ayumu, Naimuddin, Mohammed, Takaesu, Hirotomo, Ono, Mitsuo, Hirokawa, Takatsugu, Eissa, A. M., Ahmed, Abdalla S., El Gohary, M. I., Nakashima, Hiroshi, Raghava, G. P. S., Kurgalvuk, N., Goryn, O., Gerstman, Bernard S., Kratasyuk, V. A., Esimbekova, E. N., Gritsenko, E. V., Remmel, N. N., Maznyak, O. M., German, A., Tikhonov, A., Tchitchkan, D., Koulchitsky, S., Pashkevich, S., Pletnev, S., Kulchitsky, V., Pesotskaya, Y., Shapiro, Erik M., Borthakur, Arijitt, Dimitrov, Ivan, Leigh, John S., Rizi, Rahim, Reddy, Ravinder, Charagundla, Sridhar, Duvvuri, Umamaheswar, Degaonkar, M., Khubchandani, M., Kumar, Mahesh, Jagannathan, N R., Raghunathan, P., Jayasundar, Rama, Coshic, O., Rath, O. K., Julka, P. K., Iliescu, Karina Roxana, Sajin, Maria, Petcu, Ileana, Moisoi, Nicolcta, Kuzmenko, A. I., Donchenko, G. V., Nikolenko, I. A., Morozova, R. P., Rahman, M. K., Ahmed, M. M., Watanabe, Takehiro, Uretzky, G., Ammar, R., Sharony, R., Rubin, Y., Gilboa, H., Mallick, H. N., Kumar, Mohan V., Begum, Gulnaz M., Degaonkar, Mahaveer N., Govindasamy, S., Kumosani, T. A., Lupusoru, C., Titescu, G., Haulica, I., Stefanescu, I., Iliescu, R., Nastasa, V., Bild, W., Khetawat, Gopal, Nealen, M., Faraday, N., Bray, P. F., Noga, S., Lycholat, E. A., Ananieva, T. V., Kosevich, M V., Stepanyan, S. G., Antonyuk, S. V., Khachatryan, A., Kumar, A., Arakelian, H., Khachatryan, R., Agadjanyan, S., Ayrapetyan, S., Mkheyan, V., Rajan, S. S., Kabaleeswaran, V., Gopalakrishnan, Geetha, Govindachari, T. R., Ramrakhiani, Meera, Cullen, David C., Lowe, Phillip, Badley, Andrew, Hermel, H., Möhwald, H., Schmahl, W., Singh, Anil K., Das, Joydip, Majumdar, Nirmalya, Dér, András, Oroszi, László, Kelemen, Loránd, Ormos, Pál, Hámori, András, Ramsden, Jeremy J., Mitra, Chanchal K., Savitri, D., Yanagida, Toshio, Esaki, Seiji, Sowa, Yosiyuki, Nishida, Tomoyuki, Kimura, Yuji, Radu, M., Laukhina, E. E., Kasumova, L. A., Koltover, V. K., Bubnov, V. P., Estrin, Ya. I., Dotta, Rajiv, Zahradník, Ivan, Marko, Milan, Novák, Pavel, Miyata, Hidetake, Hirata, Hiroaki, Sengupta, P., Maiti, S., Balaji, J., Banerjee, S., Barker, A. L., Winlove, C. P., OʼHare, D., Macpherson, J. V., Gonsalves, M., Unwin, P. R., Phillip, R., Kumar, Ravindra G., Murata, K., Nagayaka, K., Danev, R., Sugitani, S., Gősch, Michael, Thyberg, P., Földes-Papp, Z., Björk, G., Blom, H., Holm, J., Heino, T., Inagaki, Fuyuhiko, Yokochi, Masashi, Kusunoki, Masami, Matthews, E. K., Pines, J., Chukova, Yu. P., Koltover, Vitaly K., Kang, B. P. S., Bansal, Geetanjali, Bansal, M. P., Singh, U., Singh, Uma, Nakata, Kotoko, Nakano, Tastuya, Kaminuma, Tsuguchika, Kirn, Bonn, Potocnik, Neja, Stare, Vito, Shukla, Latal, Sastry, M. D., Natarajan, V., Devasagayam, T. P. A., Kesavan, P. C., Sayfutdinov, R., Degermendzhy, A. G., Adamovich, V. V., Rogozin, Yu. D., Khetrapal, C. L., Gowda, G. A. Nagana, Ghimire, Kedar Nath, Masaru, Ishida, Fujita, H., Ishiwata, S., Suzuki, M., Kawahara, S., Kirino, Y., Kishimoto, Y., Mori, H., Mishina, M., Ohshima, H., Dukhin, A. S., Goetz, P. J., Shilov, V. N., and Mishra, R. K.
- Published
- 1999
- Full Text
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6. Protein diffusion, stability and activity in crowded media
- Author
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Loredana Antonella Randazzo, Santangelo, M. G., Noto, R., Vassalli, M., Manno, M., Martorana, V., Randazzo, L, Santangelo, MG, Noto, R, Vassalli, M, Manno, M, and Martorana, V
- Subjects
crowding, ovalbumin, diffusion ,Settore FIS/07 - Fisica Applicata(Beni Culturali, Ambientali, Biol.e Medicin) - Published
- 2015
7. Solvent-Induced Free Energy Landscape and Solute-Solvent Dynamic Coupling in a Multielement Solute
- Author
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San Biagio, P.L., Martorana, V., Bulone, D., Palma-Vittorelli, M.B., and Palma, M.U.
- Published
- 1999
- Full Text
- View/download PDF
8. Functional and dysfunctional isoforms of human neuroserpin
- Author
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Noto, R, SANTANGELO, Maria Grazia, LEVANTINO, Matteo, CUPANE, Antonio, Mangione, MR, Parisi, D, Ricagno, S, Bolognesi, M, Manno, M, Martorana, V., Noto, R, Santangelo, MG, Levantino, M, Cupane A, Mangione, MR, Parisi, D, Ricagno, S, Bolognesi, M, Manno, M, and Martorana, V
- Subjects
human neuroserpin ,Settore FIS/07 - Fisica Applicata(Beni Culturali, Ambientali, Biol.e Medicin) - Abstract
Neuroserpin (NS) is a serine protease inhibitor (SERPIN) involved in different neurological pathologies, including the Familial Encephalopathy with Neuroserpin Inclusion Bodies (FENIB), related to the aberrant polymerization of NS mutants. Here we present an in vitro and in silico characterization of native NS and its dysfunctional conformation isoforms: the proteolytically cleaved conformer, the inactive latent conformer, and the polymeric conformer. Using circular dichroism and fluorescence spectroscopy, we present an experimental validation of the latent model and highlight the main structural features of the different conformers. In par- ticular, emission spectra of aromatic residues yield a distinct conformational fingerprint, that provides a novel and simple spectroscopic tool for selecting serpin conformers in vitro. Based on the analogy between cleaved and latent serpins, we propose a structural model for latent neuroserpin, for which an experimental crystallographic structure is lacking. Molecular Dynamics simulations suggest that NS conformational stability and flexibility arise from the spatial pattern of intramolecular salt-bridges and hydrogen bonds.
- Published
- 2015
9. Protein diffusion in ovo
- Author
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Randazzo, L, Vassalli, M, Manno, M, Martorana, V., SANTANGELO, Maria Grazia, Randazzo, L, Santangelo, MG, Vassalli, M, Manno, M, and Martorana, V
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diffusion, ovalbumin - Published
- 2014
10. Naïve Hsp60, similarly to GroEL, oligomerizes to build heptameric and tetradecameric structures
- Author
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MARINO GAMMAZZA, Antonella, CAMPANELLA, Claudia, BURGIO, Giosalba, ZUMMO, Giovanni, CAPPELLO, Francesco, Vilasi, S, Carrotta, R, Mangione,MR, Librizzi, F, Martorana,V, Ortore,MG, Vilasi,A, Corona,D, Bulone,D, Conway de Macario,E, Macario, AJL, San Biagio, PL, Marino Gammazza,A, Vilasi, S, Carrotta, R, Mangione,MR, Campanella,C, Librizzi, F, Martorana,V, Ortore,MG, Vilasi,A, Burgio, G, Corona,D, Zummo,G, Bulone,D, Conway de Macario,E, Macario, AJL, San Biagio, PL, and Cappello F
- Subjects
Hsp60, structure, Groel - Published
- 2013
11. On the molecular structure of human neuroserpin polymers. Coagulation, fragmentation and latentization control serpin aggregation
- Author
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SANTANGELO, Maria Grazia, LEVANTINO, Matteo, CUPANE, Antonio, Noto, R, Ricagno, S, Pezzullo, M, Bolognesi, M, Mangione, MR, Martorana, V, Manno, M., Santangelo, MG, Noto, R, Levantino, M, Cupane, A, Ricagno, S, Pezzullo, M, Bolognesi, M, Mangione, MR, Martorana, V, and Manno, M
- Subjects
FTIR ,Settore FIS/07 - Fisica Applicata(Beni Culturali, Ambientali, Biol.e Medicin) ,Polymerization - Abstract
The polymerization of serpins is at the root of a large class of diseases; the molecular structure of serpin polymers has been recently debated. In this work, we study the polymerization kinetics of human neuroserpin by Fourier Transform Infra Red spectroscopy and by time-lapse Size Exclusion Chromatography. First, we show that two distinct neuroserpin polymers, formed at 45 and 85 °C, display the same isosbestic points in the Amide I band, and therefore share common secondary structure features. We also find a concentration independent polymerization rate at 45 °C suggesting that the polymerization rate limiting step is the formation of an activated monomeric species. The polymer structures are consistent with a model that predicts the bare insertion of portions of the reactive center loop into the A b-sheet of neighboring serpin molecule, although with different extents at 45 and 85 °C. Further studies are currently addressing the structure of monomeric neuroserpin conformers.
- Published
- 2012
12. Influence of exogenous and endogenous ions on the properties of BSA
- Author
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Giacomazza, G, Mangione, MR, Bulone, D, Martorana, V, San Biagio, PL, NAVARRA, Giovanna, Alekseev, RJ, Rebane, AL, Giacomazza, G, Mangione, MR, Bulone, D, Martorana, V, Navarra, G, and San Biagio, PL
- Subjects
conformational change ,Bovin serum albumin ,aggregation ,metal ion ,Settore FIS/07 - Fisica Applicata(Beni Culturali, Ambientali, Biol.e Medicin) - Published
- 2012
13. Role of electrostatic interactions in the fibrillogenesis of lysozyme
- Author
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RACCOSTA, Samuele, Martorana, V, Manno, M., Raccosta, S, Martorana, V, and Manno, M
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fibrillogenesis, lysozyme, oligomers, electrostatic interaction ,Settore FIS/07 - Fisica Applicata(Beni Culturali, Ambientali, Biol.e Medicin) - Published
- 2011
14. Role of repulsive interaction on the fibrillogenesis of hen egg-white lysozyme
- Author
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RACCOSTA, Samuele, Martorana, V, Manno, M., Raccosta, S, Martorana, V, and Manno, M
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fibrillogenesis, lysozyme, oligomer, electrostatic interaction - Published
- 2010
15. Inactivation and polymerization of human neuroserpin
- Author
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Manno, A, Mangione, MR, Ricagno, S, Pezzullo, M, Bolognesi, M, Martorana, V, Noto, R., SANTANGELO, Maria Grazia, LEVANTINO, Matteo, Manno, A, Santangelo, MG, Mangione, MR, Levantino, M, Ricagno, S, Pezzullo, M, Bolognesi, M, Martorana, V, and Noto, R
- Subjects
human neuroserpin, polymerization, conformational changes ,Settore FIS/07 - Fisica Applicata(Beni Culturali, Ambientali, Biol.e Medicin) - Abstract
Neuroserpin is an inhibitory enzyme, belonging to the family of serpins and involved in several pathologies, such as ischemia, Alzheimer disease, and FENIB (Familial Encephalopathy with Neuroserpin Inclusion Body). Here, we study the mechanism of neuroserpin inactivation and polymerization by different experimental techniques (static and dynamic light scattering, liquid chromatography, Fourier transform infrared spectroscopy, emission spectroscopy). Our results show that at intermediate temperatures (45-55 °C) neuroserpin forms flexible polymers with a size from a few tens to a few hundreds of nanometers. At high temperatures, above 80 °C, our results reveal a different polymeric form, reached through an analogous loop-sheet mechanism, with considerably larger size and higher chemical stability. Our observations highlight the role of the different processes involved in serpin self-assembly, namely inactivating conformational changes, oligomer formation, polymer elongation and fragmentation.
- Published
- 2010
16. Fibrillogenesis of Hen Egg-White Lysozyme at acid pH
- Author
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RACCOSTA, Samuele, Martorana, V, Manno, M., Raccosta, S, Martorana, V, and Manno, M.
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fibrillogenesis, lysozyme, electrostatic interactions - Published
- 2009
17. The necessary chances of a thermodynamically metastable protein: inactivation and polymeritzation of human neuroserpin
- Author
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SANTANGELO, Maria Grazia, CUPANE, Antonio, D'AMICO, Michele, LEVANTINO, Matteo, Bolognesi M, Mangione M. R, Martorana V, Noto R, Pezzullo M, Ricagno S, Manno M., Santangelo M G, Bolognesi M, Cupane A, D’Amico M, Levantino M, Mangione M R, Martorana V, Noto R, Pezzullo M, Ricagno S, and Manno M
- Subjects
Settore FIS/07 - Fisica Applicata(Beni Culturali, Ambientali, Biol.e Medicin) ,Human neuroserpin, polymerization - Abstract
Serpins are a wide class of proteins with high structural similarity, characterized by a unique substrate-like inhibitory mechanism that resembles a "molecular mousetrap". The active serpin is characterized by a main 5-stranded β-sheet and an exposed Reactive Centre Loop, which acts as a bait for the target protease. The cleavage of the loop by the protease triggers the insertion of the loop into the β-sheet as a strand and the disruptive translocation of the protease. This peculiar conformational mobility is achievable since serpins fold into a metastable native conformation. This feature gives a selective advantage to the serpin family to develop inhibitory activities, but leaves these proteins labile to misfolding and dysfunctional mutations, which cause a class of diseases known as serpinopathies. Indeed, the thermodynamically stable non-functional conformation can be reached without cleavage by intramolecular loop insertion (latent state) or by intermolecular insertion, leading to polymerization. Neuroserpin is a an inhibitor of tissue-type plasminogen activator that has a role in many pathologies, such as ischemia, Alzheimer disease, and FENIB (Familial Encephalopathy with Neuroserpin Inclusion Body). It is particularly suited to study the molecular basis of serpin inactivation and polymerization, since it may form latent conformers and polymers by thermal activation even in the wild type form. Here, we study the mechanism of neuroserpin unfolding and polymerization by different experimental techniques (static and dynamic light scattering, liquid chromatography, Fourier transform infrared spectroscopy) and by the support of Molecular Dynamics simulations. Our results show that at intermediate temperatures (45-55 °C) neuroserpin forms flexible polymers with a size from a few tens to a few hundreds of nanometers. At high temperatures, above 80 °C, our results reveal a different polymeric form, reached through an analogous loop-sheet mechanism, with considerably larger size and higher chemical stability. These observations highlight the fact that serpin polymerization is context-dependent, and that polymers accumulated in serpinopathies under physiological conditions may be different for different serpin and even for different pathological mutants of the same serpin.
- Published
- 2009
18. Preferential solvatation of TFE in lysozyme: a luminescence study
- Author
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D'AMICO, Michele, CANNAS, Marco, RACCOSTA, Samuele, Martorana, V, Manno, M., D’Amico, M, Cannas, M, Martorana, V, Raccosta, S, and Manno, M
- Subjects
Lysozyme, TFE, aggregation, solvatation - Published
- 2009
19. Influence of TFE on the proteins interactions of a lysozyme solution: a small angle X-ray scattering study
- Author
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Giordano, F, Longo, A, Manno, M, Martorana, V., D'AMICO, Michele, RACCOSTA, Samuele, Giordano, F, Longo, A, Manno, M, D’Amico, M, Raccosta, S, and Martorana, V
- Subjects
TFE, Lysozyme, saxs - Published
- 2009
20. SEVERE OSTEOPOROSIS AND MULTIPLE FRACTURES A CASE REPORT
- Author
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Martorana, D, Martorana, V, Brancato, D, CANNIZZARO, Emanuele, Martorana, D, Martorana, V, Brancato, D, and Cannizzaro, E
- Subjects
osteoporosi, fratture multiple - Abstract
The authors present a clinical case of severe osteoporosis with periprothesic femoral fracture and numerous vertebral fractures in a 87 years old patient. Treatment had consist in reposition of prosthesis, fracture reduction with internal fixation plate. Teriparatide drug was administer as usual protocol. Clinical and X-rays controls after 3, 6 and 12 months showed a good result of therapy, with a healing fracture, a orthostatism and normal deambulation, with improvement of densimetry values and a less dorsolombar pain, as well as a significant improvement of patient’s quality of life
- Published
- 2008
21. AMYLOID AGGREGATION IN CONCANAVALIN A AT HIGH PH STUDIED BY LIGHT SCATTERING, FLUORESCENCE AND CIRCULAR DICHROISM SPECTROSCOPY
- Author
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CARROTTA, Rita, VETRI, Valeria, MILITELLO, Valeria, LEONE, Maurizio, Librizzi F, Martorana V, and Carrotta R, Vetri V, Librizzi F, Martorana V, Militello V, Leone M
- Subjects
DLS, Circular Dichroism, thioflavin T - Published
- 2008
22. Kinetics of different processes in human insulin amyloid formation
- Author
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Manno M., Craparo E.F., Podestà A., Bulone D., Carrotta R., Martorana V., Milani P., Tiana G., San Biagio P.L., MANNO M, CRAPARO EF, PODESTA' A, BULONE D, CARROTTA R, MARTORANA V, TIANA G, and SAN BIAGIO PL
- Subjects
Amyloid ,medicine.medical_treatment ,Kinetics ,Microscopy, Atomic Force ,Fibril ,Models, Biological ,Fluorescence ,chemistry.chemical_compound ,light-scattering ,Structural Biology ,amyloid fibril ,Microscopy ,medicine ,Humans ,Insulin ,Scattering, Radiation ,Microscopy, Phase-Contrast ,Benzothiazoles ,Particle Size ,Molecular Biology ,Fluorescent Dyes ,atomic force microscopy ,aggregation ,Temperature ,Hydrogen-Ion Concentration ,Thiazoles ,Crystallography ,Monomer ,chemistry ,Biophysics ,Thioflavin ,Elongation - Abstract
Human insulin has long been known to form amyloid fibrils under given conditions. The molecular basis of insulin aggregation is relevant for modeling the amyloidogenesis process, which is involved in many pathologies, as well as for improving delivery systems, used for diabetes treatments. Insulin aggregation displays a wide variety of morphologies, from small oligomeric filaments to huge floccules, and therefore different specific processes are likely to be intertwined in the overall aggregation. In the present work, we studied the aggregation kinetics of human insulin at low pH and different temperatures and concentrations. The structure and the morphogenesis of aggregates on a wide range of length scales (from monomeric proteins to elongated fibrils and larger aggregates networks) have been monitored by using different experimental techniques: time-lapse atomic force microscopy (AFM), quasi-elastic light-scattering (QLS), small and large angle static light-scattering, thioflavin T fluorescence, and optical microscopy. Our experiments, along with the analysis of scattered intensity distribution, show that fibrillar aggregates grow following a thermally activated heterogeneous coagulation mechanism, which includes both tip-to-tip elongation and lateral thickening. Also, the association of fibrils into bundles and larger clusters (up to tens of microns) occurs simultaneously and is responsible for an effective lag-time.
- Published
- 2007
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23. Embelin binds to human neuroserpin and impairs its polymerisation
- Author
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Saga, G, Sessa, F, Barbiroli, A, Santambrogio, C, Russo, R, Sala, M, Raccosta, S, Martorana, V, Caccia, S, Noto, R, Moriconi, C, Miranda, E, Grandori, R, Manno, M, Bolognesi, M, Ricagno, S, SANTAMBROGIO, CARLO, GRANDORI, RITA, Ricagno, S., Saga, G, Sessa, F, Barbiroli, A, Santambrogio, C, Russo, R, Sala, M, Raccosta, S, Martorana, V, Caccia, S, Noto, R, Moriconi, C, Miranda, E, Grandori, R, Manno, M, Bolognesi, M, Ricagno, S, SANTAMBROGIO, CARLO, GRANDORI, RITA, and Ricagno, S.
- Abstract
Neuroserpin (NS) is a serpin inhibitor of tissue plasminogen activator (tPA) in the brain. The polymerisation of NS pathologic mutants is responsible for a genetic dementia known as familial encephalopathy with neuroserpin inclusion bodies (FENIB). So far, a pharmacological treatment of FENIB, i.e. an inhibitor of NS polymerisation, remains an unmet challenge. Here, we present a biophysical characterisation of the effects caused by embelin (EMB a small natural compound) on NS conformers and NS polymerisation. EMB destabilises all known NS conformers, specifically binding to NS molecules with a 1:1 NS:EMB molar ratio without unfolding the NS fold. In particular, NS polymers disaggregate in the presence of EMB, and their formation is prevented. The NS/EMB complex does not inhibit tPA proteolytic activity. Both effects are pharmacologically relevant: firstly by inhibiting the NS polymerisation associated to FENIB, and secondly by potentially antagonizing metastatic processes facilitated by NS activity in the brain.
- Published
- 2016
24. Oligomerizing ability of newly made human Hsp60 with its mitochondrial import signal
- Author
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Vilasi, S., Carrotta, R., Mangione, M.R., Campanella, C., Palumbo Piccionello, A., Librizzi, F., Martorana, V., Ortore, M.G., Marino Gammazza, A., Vilasi, A., Burgio, G., Corona, D., Zummo, G., Bulone, D., Conway De Macario, E., Macario, A.J.L., San Biagio, P.L., and Cappello, F.
- Subjects
animal structures ,fungi ,chemical and pharmacologic phenomena ,complex mixtures - Abstract
It is currently accepted that the human Hsp60 resides and works not only in the mitochondria, the canonical residence, but also outside it. It is also known that Hsp60 although coded by a nuclear gene is synthesized in the cytosol and includes an N-terminal mitochondrial import signal (MIS), which directs the polypeptide toward the inside of the organelle where the MIS is removed. Therefore, there are at least two functional types of Hsp60, with and without MIS, the former in the cytosol the latter inside the mitochondria. A key question is: how do these two forms of Hsp60 differ beyond the fact that while one has MIS the other lacks it? How presence or absence of MIS affects the ability of Hsp60 to form oligomers, which are considered important for chaperoning peptides and assist them to reach a native state? We report here our initial observations on this issue. Typically, in the mitochondria, Hsp60 forms ring-shaped heptamers, two of which associate to build a barrel-shaped tetradecamer, the functional chaperoning complex. It is not known if the cytosolic Hsp60 with its MIS, also forms hepta- and tetradecamers. A clarification of this issue will most likely shed light on the physiological functions of extramitochondrial Hsp60, and also on its pathogenic role in Hsp60 chaperonopathies. Consequently, we compared recombinant Hsp60 bearing the MIS with the prokaryotic ortholog GroEL, which under normal conditions forms functional double-ring tetradecamers. Characteristic hydrodynamic sizes of the oligomeric complex for both systems were investigated by small angle X-ray (SAXS) and static and dynamic light scattering (SLS and DLS) in solution under similar physicochemical conditions. High Performance Liquid Chromatography (HPLC) and blue native polyacrylamide-gel electrophoresis were used to further clarify the equilibrium between the different oligomeric species of the two proteins over a wide range of concentrations. Hsp60 with MIS formed hepta- and tetradecamers similarly to GroEL. Oligomerization was dependent on concentration for GroEL and Hsp60, but for the latter, formation of larger oligomers, e.g., tetradecamers, required higher concentrations than the former., Italian Journal of Anatomy and Embryology, Vol 118, No 2 (Supplement) 2013
- Published
- 2014
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25. Preservation of the smooth muscular internal (vesical) sphincter and of the proximal urethra during retropubic radical prostatectomy: A technical modification to improve the early recovery of continence
- Author
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Brunocilla, and Schiavina, E., And, R., Borghesi, M., And, Pultrone, and Cevenini, C., and Vagnoni, M., and and Martorana, V.
- Published
- 2014
26. Influence of Exogenous and Endogenous Ions on the Gelation of BSA
- Author
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Giacomazza D, Mangione MR, Bulone D, Martorana V, Navarra G, and San Biagio PL
- Published
- 2012
27. Sucrose Pectin Interaction from Solution to Gels
- Author
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Bulone D., Giacomazza D., Manno M., Martorana V., and San Biagio P.L.
- Abstract
Pectin is a very important polysaccharide in food technology, due to its ability to thicken or gel in aqueous solution under specific condition. One of the most common uses of pectin is in making jellies or jams, which requires the addition of a large amount of sucrose to acidic solutions. The role of sucrose in promoting pectin gelation has been ascribed to the strengthening of hydrophobic interaction consistently with its well-known stabilizing effect on protein structure. On the other hand, more specific effects on dimension and stiffness of pectin chains have been suggested by computational work. Here we present measurements of rheology, static and dynamic light scattering on samples of pectin containing different amounts of sucrose, ranging from few percent up to close the solubility limit of sucrose. This corresponds to spanning from low viscous liquid samples to strong gels. Results show that below the threshold value of 55% w/w, sucrose acts a critical parameter for the sol/gel transition by increasing the strength of excluded volume and hydrodynamic interaction between polymer chains. A further increase of sucrose above the critical concentration yields gels with a higher viscoelastic component corresponding to a higher amount of frozen structural inhomogeneities.
- Published
- 2010
28. Aggregation of a multidomain protein: A coagulation mechanism governs aggregation of a model IgG1 antibody under weak thermal stress
- Author
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Andersen C. B., Manno M., Rischel C., Thórólfsson M., and Martorana V.
- Abstract
Using an IgG1 antibody as a model system, we have studied the mechanisms by which multidomain proteins aggregate at physiological pH when incubated at temperatures just below their lowest thermal transition. In this temperature interval, only minor changes to the protein conformation are observed. Light scattering consistently showed two coupled phases: an initial fast phase followed by several hours of exponential growth of the scattered intensity. This is the exact opposite of the lag-time behavior typically observed in protein fibrillation. Dynamic light scattering showed the rapid formation of an aggregate species with a hydrodynamic radius of about 25 nm, which then increased in size throughout the experiment. Theoretical analysis of our light scattering data showed that the aggregate number density goes through a maximum in time providing compelling evidence for a coagulation mechanism in which aggregates fuse together. Both the analysis as well as size-exclusion chromatography of incubated samples showed the actual increase in aggregate mass to be linear and reach saturation long before all molecules had been converted to aggregates. The CH2 domain is the only domain partly unfolded in the temperature interval studied, suggesting a pivotal role of this least stable domain in the aggregation process. Our results show that for multidomain proteins at temperatures below their thermal denaturation, transient unfolding of a single domain can prime the molecule for aggregation, and that the formation of large aggregates is driven by coagulation.
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- 2010
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29. Applications of optical sensors to the detection of light scattered from gelling systems
- Author
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Bulone D., Manno M., San Biagio P.L., and Martorana V.
- Abstract
Visible light, scattered within an angle of few degrees, (Small Angle Light Scattering, SALS) yields information on the spatial correlations and dynamical properties on the scale of the micrometers. In this way a quick and non-invasive characterization of a variety of samples is feasible. Lately the SALS instruments have been built around multielement optical sensors (CCD, CMOS), allowing the simultaneous measurement of the complete structure factor even during fast kinetics. An assessment of some sensor matrices of different technology will be presented. The macromolecular assemblies produced by polysaccharides or proteins can be functional or dysfunctional, their properties being either desirable or detrimental. Anyhow, their morphology often depends, in a very delicate way, on the presence of cosolutes, on the thermal history, on the biopolymer concentration etc. We present some applications of low angle dynamic and static light scattering to the study of gelling systems (agarose, pectin, insulin).
- Published
- 2009
30. Attivatori del trasporto ionico della CFTR: identificazione e modellazione molecolare dei siti leganti
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Moran, O, Martorana, V, Pincin, C, Ferrera, L, Guida, P, Noto, R, and Zegarra-Moran, O
- Published
- 2005
31. Metastable liquid-liquid phase separation in supersaturated lysozyme solutions
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Manno M., Xiao C., Bulone D., Martorana V., and San Biagio P. L.
- Published
- 2003
32. Attivatori del trasporto ionico mediato dalla CFTR: identificazione e modellistica dei siti di legame
- Author
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Moran O., Pincin C., Martorana V., and Zegarra O.
- Published
- 2003
33. A sweet way to jamming: Structural arrest in sugar-pectin systems
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Bulone D., Giacomazza D., Manno M., Martorana V., and San Biagio P.L.
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- 2003
34. Thermodynamic instability in supersaturated Lysozyme solutions: Effect of salt and role of concentration fluctuations
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Manno M., Bulone D., Martorana V., and San_Biagio P.L.
- Published
- 2003
35. Interaction of Explicit Solvent with Hydrophobic/Philic/Charged Residues of a Protein-Residue Character Vs. Conformational Context
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Martorana, V., Corongiu, Giorgina, and Palma, M. U.
- Published
- 1998
36. Inorganic anions in goat and ovine milk from Calabria (Italy) by suppressed ion chromatography
- Author
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Licata, P., primary, Naccari, F., additional, Di Bella, G., additional, Lo Turco, V., additional, Martorana, V., additional, and mo Dugo, G., additional
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- 2013
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37. Amyloid Fibrils Formation of Concanavalin A at Basic pH
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Carrotta, R., primary, Vetri, V., additional, Librizzi, F., additional, Martorana, V., additional, Militello, V., additional, and Leone, M., additional
- Published
- 2011
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38. Quantification of Underivatized Fatty Acids From Vegetable Oils by HPLC with UV Detection
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Guarrasi, V., primary, Mangione, M. R., additional, Sanfratello, V., additional, Martorana, V., additional, and Bulone, D., additional
- Published
- 2010
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39. Role of Charges and Solvent on the Conformational Properties of Poly(galacturonic acid) Chains: A Molecular Dynamics Study
- Author
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Noto, R., primary, Martorana, V., additional, Bulone, D., additional, and San Biagio, P. L., additional
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- 2005
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40. K+ and Na+ effects on the gelation properties of κ-Carrageenan
- Author
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Mangione, M.R., primary, Giacomazza, D., additional, Bulone, D., additional, Martorana, V., additional, Cavallaro, G., additional, and San Biagio, P.L., additional
- Published
- 2005
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41. Thermodynamic instability and off-critical slowing down in supersaturated lysozyme solutions
- Author
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Manno, M, primary, Bulone, D, additional, Martorana, V, additional, and Biagio, P L San, additional
- Published
- 2004
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42. Ergodic to non-ergodic transition monitored by scattered light intensity statistics
- Author
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Manno, M., primary, Bulone, D., additional, Martorana, V., additional, and San Biagio, P.L., additional
- Published
- 2004
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43. Interaction of processes on different length scales in a bioelastomer capable of performing energy conversion
- Author
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Manno, M., primary, Emanuele, A., additional, Martorana, V., additional, San Biagio, P. L., additional, Bulone, D., additional, Palma-Vittorelli, M. B., additional, McPherson, D. T., additional, Xu, J., additional, Parker, T. M., additional, and Urry, D. W., additional
- Published
- 2001
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44. Micro- and mesoscopic process interactions in protein coagulation.
- Author
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San Biagio, P. L., Martorana, V., Emanuele, A., Vaiana, S. M., Manno, M., Bulone, D., Palma-Vittorelli, M. B., and Palma, M. U.
- Subjects
- *
DENATURATION of proteins , *PROTEIN binding - Abstract
It has recently been recognized that pathological protein coagulation is responsible for lethal pathologies as diverse as amyloidosis, Alzheimer and TSE. Understanding the coagulation mechanisms is therefore stirring great interest. In previous studies we have shown that on profoundly different systems coagulation is the result of a strong interaction between two processes on different length scales (mesoscopic and microscopic). Here we report experiments on bovine serum albumin (BSA) showing that the overall mechanism is the result of at least 3 distinct and strongly intertwined processes, on both length scales: molecular conformational changes, solution demixing and intermolecular crosslinking. This mechanism involves the statistical mechanics of protein-solvent interaction, its relation to the protein’s landscape of configurational free energy and to the solution’s thermodynamic stability, and its relation to the topological problem of crosslink-percolation, responsible for coagulation. © 2000 American Institute of Physics. [ABSTRACT FROM AUTHOR]
- Published
- 2000
45. Interacting processes in protein coagulation
- Author
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San Biagio, P.L., primary, Martorana, V., additional, Emanuele, A., additional, Vaiana, S.M., additional, Manno, M., additional, Bulone, D., additional, Palma-Vittorelli, M.B., additional, and Palma, M.U., additional
- Published
- 1999
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46. Multiple interactions between molecular and supramolecular ordering
- Author
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Manno, M., primary, Emanuele, A., additional, Martorana, V., additional, Bulone, D., additional, San Biagio, P. L., additional, Palma-Vittorelli, M. B., additional, and Palma, M. U., additional
- Published
- 1999
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47. Interaction of explicit solvent with hydrophobic/philic/charged residues of a protein: Residue character vs. conformational context
- Author
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Martorana, V., primary, Corongiu, G., additional, and Palma, M.U., additional
- Published
- 1998
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48. Effects of electric charges on hydrophobic forces
- Author
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Bulone, D., primary, Martorana, V., additional, San Biagio, P. L., additional, and Palma-Vittorelli, M. B., additional
- Published
- 1997
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49. Collective properties of hydration: long range and specificity of hydrophobic interactions
- Author
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Martorana, V., primary, Bulone, D., additional, San Biagio, P.L., additional, Palma-Vittorelli, M.B., additional, and Palma, M.U., additional
- Published
- 1997
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50. Correlated solvent-induced forces on a protein at single residue resolution: relation to conformation, stability, dynamics and function
- Author
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Martorana, V., primary, Corongiu, G., additional, and Palma, M.U., additional
- Published
- 1996
- Full Text
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