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4. Grapho-Analytical Optimization of Key-Joints.

Author

Szabó, Ferenc J.

Subjects
FINITE element method, AIRCRAFT industry, THREE-dimensional modeling
Abstract

Key-joints and splined shafts are used in many drives and rotating elements in engineering practice. Nowadays it is increasingly important to decrease the dead-weight of structures (in the vehicle industry, aircraft industry, etc). This paper shows an optimization process for the minimum weight design of key-joints. For the solution of the optimization problem a 3D grapho-analytical optimization process is used, based on the Kuhn-Tucker optimality criterion. During the graphic part of the process, three-dimensional diagrams show the behavior of the objective function and of the design constraints, which makes easy to read the optimum solution from the diagram. The final optimum solution is also given numerically in a table. For better demonstration, the finite element analysis of the three-dimensional CAD model of the optimal joint is also shown. As a further application, the grapho-analytical optimization of parallel key splined shafts is shown, too. [ABSTRACT FROM AUTHOR]

Published
2023
Full Text
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6. GARFIELD-AF: risk profiles, treatment patterns and 2-year outcomes in patients with atrial fibrillation in Germany, Austria and Switzerland (DACH) compared to 32 countries in other regions worldwide

Author

Haas, S., Camm, J.A., Harald, D., Steffel, J., Virdone, S., Pieper, K., Brodmann, M., Schellong, S., Misselwitz, F., Kayani, G., Kakkar, A.K., Jean-Pierre, B., John Camm, A., Fitzmaurice, D.A., Fox, K.A.A., Gersh, B.J., Goldhaber, S.Z., Shinya, G., Sylvia, H., Werner, H., Mantovani, L.G., Frank, M., Pieper, K.S., Turpie, A.G.G., Martin van Eickels, Verheugt, F.W.A., Fox Bernard, K.A.A., Gersh, J., Hector, L., Luciardi Harry Gibbs, Marianne, B., Frank, C., Antonio Carlos Pereira Barretto, Connolly, S.J., John, E., Ramon, C., Zhi-Cheng, J., Petr, J., Jørn Dalsgaard Nielsen, Hany, R., Pekka, R., Jean-Yves Le Heuzey, Matyas, K., Jitendra Pal Singh Sawhney, Giancarlo, A., Giuseppe, A., Yukihiro, K., Carlos Jerjes Sánchez Díaz, Hugo Ten Cate, Dan, A., Janina, S., Elizaveta, P., Toon Wei Lim, Barry, J., Seil, O., Xavier, V., Marten, R., Jan, S., Pantep, A., Ali, O., Alex, P., Wael Al Mahmeed, David, F., Samuel, Z.G., Dayi Hu Kangning Chen, Yusheng, Z., Huaiqin, Z., Jiyan, C., Shiping, C., Daowen, W., Yuejin, Y., Weihua, L., Hui, L., Yuehui, Y., Guizhou, T., Ping, Y., Yingmin, C., Shenghu, H., Yong, W., Guosheng, F., Xin, L., Tongguo, W., Xiaoshu, C., Xiaowei, Y., Ruiping, Z., Moshui, C., Longgen, X., Ping, C., Yang, J., Ying, G., Xue, L., Zhiming, Y., Praveen Jadhavm Raghava Sarma, Govind, K., Prakash, C., Rasesh Atulbhai Pothiwala, Mohanan Padinhare Purayil, Kamaldeep, C., Veerappa Annasaheb Kothiwale, Bagirath, R., Vinod Madan Vijan, Jitendra, S., Ganapathi, B., Aziz, K., Ramdhan, M., Manojkumar, C., Sunitha, A., Vikas, B., Govindan, V., Debabrata, R., Rajashekhar, D., G Ravi Shankar, A., Sunil, K., Dinesh, J., Kartikeya, B., Vinay, K., Udigala Madappa Nagamalesh, Rajeeve Kumar Rajput, Yukihiro Koretsune Seishu Kanamori, Kenichi, Y., Koichiro, K., Yosuke, K., Keiki, Y., Fumitoshi, T., Yuji, M., Ikuo, M., Hiroo, N., Shinichi, A., Tetsuro, S., Masahiro, M., Hiroyuki, O., Susumu, A., Kei, C., Hiroaki, N., Makoto, T., Takeshi, K., Kunihiko, Y., Hiroshi, A., Takayuki, H., Megumi, O., Shiro, A., Shinichiro, K., Kenshi, K., Takashi, M., Jun, M., Yurika, O., Ryuji, S., Kazuo, G., Kotaro, M., Yoshikuni, H., Hisakazu, S., Hiroo, M., Hitoshi, K., Tsugihiro, N., Tadashi, N., Hidekazu, N., Ryuji, Z., Yoshihisa, F., Akira, Y., Hiroyuki, N., Jun, O., Yasuyuki, K., Kinshiro, M., Yutaka, W., Masanori, Y., Hiromitsu, M., Sumihisa, A., Hajime, K., Satoru, T., Katsumi, S., Hiroki, T., Ichiro, O., Takashi, K., Satoshi, H., Masamichi, G., Takuma, E., Hidetoshi, C., Kazuaki, F., Yuhei, S., Hirokuni, S., Toshihisa, N., Yoshihiko, A., Toshiro, N., Kazuhisa, S., Fumihiro, H., Naoto, Y., Masahiro, K., Toshifumi, T., Munesumi, I., Yoshitake, F., Daisuke, I., Taku, S., Tetsu, I., Norio, I., Koichi, O., Keizo, T., Yutaka, H., Motoshi, T., Hiroto, T., Shinjiro, N., Masaaki, I., Yuichiro, N., Naomasa, M., Ashida, K., Jun, A., Seishiro, M., Osamu, A., Shuji, F., Hirofumi, M., Kazuya, M., Yoshiki, H., Ichiro, S., Kotaro, O., Ichiro, T., Mitsuyuki, A., Toshihide, U., Yoshinori, G., Makoto, I., Shoji, M., Shigeru, M., Hideo, D., Mitsuru, T., Takaaki, K., Shigeo, K., Chiga, O., Masaki, S., Masami, N., Yutaka, K., Yoichi, N., Hiroshi, O., Rikimaru, O., Masato, A., Teruaki, M., Kazuhiko, N., Takafumi, M., Junichi, M., Mitsunori, A., Masako, F., Makoto, O., Tsuneo, F., Toshiya, T., Tenei, K., Hiroshi, K., Mizuho, I., Masahiro, A., Takashi, U., Hironori, O., Masahiko, I., Yoshiki, K., Atsuyuki, N., Shinobu, T., Mitsuhiro, S., Masayuki, N., Kenichiro, I., Motoyuki, I., Taro, M., Masamichi, W., Hiroaki, M., Masato, M., Fumio, O., Teruaki, K., Kuniaki, T., Masaaki, T., Morio, I., Hiroshi, W., Toshihiko, S., Shinya, H., Hiroaki, H., Mitsumoto, H., Michitaka, H., Koichi, M., Hideki, H., Nobuyoshi, S., Yukio, S., Akira, S., Kazuo, N., Tetsuro, Y., Kunio, A., Sen, A., Chiei, T., Saori, M., Hirofumi, K., Masanori, K., Shiro, N., Atsushi, T., Shuta, T., Kazuyuki, S., Akiko, M., Hiroki, S., Jin, N., Taketo, H., Takash, I., Kazuki, S., Kazuya, K., Tomobumi, K., Tsuyoshi, T., Hirosumi, S., Kiyoshi, N., Kenichi, I., Kazuo, M., Tomohiro, S., Takeshi, I., Koichi, K., Hiromichi, K., Tsutomu, T., Mamoru, H., Jisho, K., Akitoshi, S., Yoshihiro, T., Tetsuo, B., Koji, H., Masaaki, H., Koichi, H., Takao, B., Kazuaki, M., Toshihiko, K., Kunihiko, H., Toshihide, K., Akira, N., Eiji, O., Takashi, S., Hiroyoshi, H., Chikako, S., Takashi, Y., Ichiro, M., Kazunori, S., Isamu, N., Ken, T., Osamu, I., Koichi, T., Samu, U., Hirokazu, K., Takuya, O., Seizo, O., Junya, K., Toshihiko, N., Itaru, M., Yoshifusa, M., Yasuyuki, M., Kazuo, T., Hajime, H., Tetsutaro, K., Koji, M., Masaichi, N., Takashi, W., Tomoki, Y., Masato, S., Hidekazu, A., Hisanori, S., Hiroyuki, T., Nobufusa, F., Akira, O., Kentaro, Y., Kenji, A., Taku, Y., Takeaki, K., Shunji, S., Shu, S., Nitaro, S., Masayuki, W., Yosuke, N., Toru, A., Masaki, O., Tetsushi, W., Tomoko, K., Yasuo, S., Takeshi, T., Yoshihito, H., Shinichi, H., Yukihiko, A., Yoshihiro, S., Hirohide, U., Hiroshi, T., Shuichi, T., Naoto, H., Seiichi, M., Hisashi, S., Takuma, A., Yasunobu, S., Yawara, N., Osamu, M., Hideko, I., Katsumasa, N., Masatsugu, N., Kazuo, S., Toshiyuki, F., Nobuhisa, I., Shunichi, N., Kiyoharu, S., Yujin, S., Naoko, O., Teruhiko, K., Hideaki, O., Masato, E., Tsutomu, G., Makoto, H., Emiko, N., Noriyuki, N., Toshizumi, M., Shuichi, S., Katsuhiro, O., Yoko, E., Tsuyoshi, F., Haruhiko, D., Shuichi, K., Sho, N., Yuya, U., Tetsuro, F., Mitsuru, I., Takuo, O., Shunsuke, T., Hideo, I., Norihiko, S., Kiyomitsu, I., Nobuo, W., Masatake, A., Junji, D., Tetsuya, K., Masato, T., Naoya, M., Yasuaki, F., Wataru, F., Susumu, S., Akinori, F., Ryosai, N., Hiroyasu, K., Rei, F., Keijiro, N., Yoji, K., Junya, A., Kiyoshi, Y., Toshio, A., Yasuhiro, S., Tatsuo, H., Yuichiro, K., Yasuhide, S., Yukihiro, S., Shingo, M., Kojuro, M., Yasuko, S., Toyoshi, S., Fumiko, I., Toshiyuki, K., Jaeyoung, K., Hiroshi, Y., Yoichi, T., Yoko Onuki Pearce, Yasuyuki, S., Takayuki, F., Toru, N., Hideaki, K., Yoshiyuki, K., Tetsuji, I., Hironori, M., Yasufumi, M., Masahito, S., Shimato, O., Yutaka, O., Satoshi, U., Kojiro, K., Tatsuo, O., Naoki, M., Koichi, I., Atsushi, I., Tomohiro, Y., Toshihiro, G., Tsukasa, K., Atsushi, S., Etsuo, M., Toshio, T., Hiroshi, S., Shunichi, F., Tomohiro, K., Yoshiyuki, F., Hiroshi, H., Jun, N., Kiichiro, Y., Takuya, I., Takafumi, A., Chi Keong Ching Toon Wei Lim, Kelvin, W., Tan, Y., Seil Oh Hui Nam Park, Woo-Shik, K., Hyeyoung, L., Sung-Won, J., Dae Hyeok Kim, Jun, K., Dongryeol, R., Jaemin, S., Dae-Kyeong, K., Dong Ju Choi, Yong Seog Oh, Myeong-Chan, C., Hack-Lyoung, K., Hui-Kyung, J., Dong-Gu, S., Sang Weon Park, Hoon Ki Park, Sang-Jin, H., Jung Hoon Sung, Hyung-Wook, P., Gi-Byoung, N., Young Keun On, Hong Euy Lim, Jaejin, K., Tae-Joon, C., Taek Jong Hong, Seong Hoon Park, Jung Han Yoon, Nam-Ho, K., Kee-Sik, K., Byung Chun Jung, Gyo-Seung, H., Chong-Jin, K., Sakda Rungaramsin Peerapat Katekangplu, Porames, K., Thanita, B., Wanwarang, W., Pinij, K., Khanchai, S., Waraporn, T., Supalerk, P., Khanchit, L., Doungrat, C., Warangkana, B., Sirichai, C., Songkwan, S., Pisit, H., Seksan, C., Pairoj, C., Boonsert, C., Yingsak, S., Khompiya, K., Piya, M., Sasivimon, J., Ongkarn, K., Armagan Altun Ali Aydinlar, Ramazan, T., Zeki, O., Sadik, A., Durmus Yildiray Sahin, Ozcan, Y., Mehmet Birhan Yilmaz, Hasan, P., Mesut, D., Murat, S., Levent, S., Murat, E., Ertugrul, O., Dursun, A., Florencia Rolandi Adrian Cesar Ingaramo, Gustavo Alberto Sambadaro, Vanina Fernandez Caputi, Sofia Graciela Berman, Pablo, D., Andres Javier Kleiban, Nestor, C., Rodolfo Andres Ahuad Guerrero, Leonel Adalberto Di Paola, Ricardo Dario Dran, Javier, E., Matias Jose Fosco, Victor Alfredo Sinisi, Luis Rodolfo Cartasegna, Oscar Gomez Vilamajo, Jose Luis Ramos, Sonia, S., Gerardo, Z., Diego, C., Guillermo, G., Alberto Alfredo Fernandez, Mario Alberto Berli, Fabian, F., Dário Celestino Sobral Filho Jefferson Jaber, Luciana Vidal Armaganijan, Costantino Roberto Frack Costantini, André, S., Weimar Kunz Sebba Barroso de Souzaem, João David de Souza Neto, José Márcio Ribeiro, Marcelo Silveira Teixeira, Paulo, R., Leonardo, P., Daniel, M., José Carlos Moura Jorge, Adalberto Menezes Lorga Filho, Luiz, B., Marcelo Westerlund Montera, Carlos Henrique Del Carlo, Jamil Abdalla Saad, Fernando Augusto Alves da Costa, Renato, L., Gilson Roberto de Araújo, Euler Roberto Manenti, Jose Francisco Kerr Saraiva, João Carlos Ferreira Braga, Alexandre, N., Carlos, M., Dalton, P., Fernando, R., Gilmar, R., Roberto Álvaro Ramos Filho, Estêvão Lanna Figueiredo, Roberto Vieira Botelho, Cláudio Munhoz da Fontoura Tavares, Helius Carlos Finimundi, Adriano, K., César Cássio Broilo França, Fábio, A., Guido Bernardo Aranha Rosito, João Batista de Moura Xavier Moraes Junior, Rogério Tadeu Tumelero, Lilia, M., Roberto Simões de Almeida, Ney Carter do Carmo Borges, Luís Gustavo Gomes Ferreira, Ramón Corbalán Benjamin Aleck Joseh Stockins Fernandez, Humberto, M., Fernando, L., Martín Larico Gómez, Carlos, A., Carlos, C., Patricio Marin Cuevas, Alejandro, F., Claudio Bugueño Gutiérrez, Juan, A., Sergio Potthoff Cardenas, German, E., Cesar, H., Carlos, R., Germán, A., Gustavo Charme Vilches, Carlos Jerjes Sanchez Diaz Jesus Jaime Illescas Diaz, Raul Leal Cantu, Maria Guadalupe Ramos Zavala, Ricardo Cabrera Jardines, Nilda Espinola Zavaleta, Enrique Lopez Rosas, Guillermo Antonio Llamas Esperón, Gerardo, P., Ernesto Cardona Muñoz, Norberto Matadamas Hernandez, Adolfo Leyva Rendon, Norberto Garcia Hernandez, Manuel de Los Rios Ibarra, Luis Ramon Virgen Carrillo, David Lopez Villezca, Carlos Hernandez Herrera, Juan Jose Lopez Prieto, Rodolfo Gaona Rodriguez, Efrain Villeda Espinosa, David Flores Martinez, Jose Velasco Barcena, Omar Fierro Fierro, Ignacio Rodriguez Briones, Jose Luis Leiva Pons, Humberto Alvarez Lopez, Rafael Olvera Ruiz, Carlos Gerardo Cantu Brito, Eduardo Julian Jose Roberto Chuquiure Valenzuela, Roxana Reyes Sanchez, Alberto Esteban Bazzoni Ruiz, Oscar Martin Lopez Ruiz, Roberto Arriaga Nava, Jesus David Morales Cerda, Pedro Fajardo Campos, Mario Benavides Gonzalez, Marianne Brodmann Kurt Lenz, Claus, H., Johannes, F., Heinz, D., Kurt, H., Andrea, P., Michael, W., Bruno, S., Alfons, G., Wilfried, L., Sabine, E., Peter, K., Josef, S., Heribert, R., Bernhard, S., Luc Capiau Geert Vervoort, Bart, W., Geert, H., Jan, V., Dirk, F., Yohan, B., Marc, D., Olivier, X., Harry, S., John, T., Georges, M., Wim, A., Ivan, B., Michel, B., Stefan, V., Peter, V., Philippe, P., Pascal, G., Tim, B., Philippe, D., Alex, H., Joeri, V., Axel De Wolf Eva Zidkova Petr Jansky, Rudolf, S., Vilma, M., Ondrej, L., Josef, O., Lubos, K., Blazej, R., Richard, F., Jan, H., Ilja, K., Zdenek, M., Hana, B., Ondrej, J., Jana, P., Iveta, P., Vratislav, D., Michaela, H., Petr, P., Petr, R., Jindrich, S., Miroslav, N., Vaclav, D., Katarina, P., Jiri, L., Jørn Nielsen Steen Husted, Helena, D., Ulrik, H., Søren, R., Næstved, S., Arne, B., John, M., Jan, B., Jorgen, S., Ebbe, E., Thomas, L., Michael, B., Jacob, M., Morten, S., Michael, O., Pekka Raatikainen Carmela Viitanen, Franck Paganelli Joël Ohayon, Frédéric, C., Michel, G., Yannick, G., Philippe, L., Jean-Joseph, M., Mohamed Bassel Koujan, André, M., Sylvain, D., Olivier, P., Nicolas, D., Jean-Pierre, C., Maxime, G., Dominique, G., G Lokesh, A., Mathieu, Z., Pierre, A., Emmanuel, E., James, K., Pierre-Yves, F., Jean-Pierre, H., Nestor, L., Gilles, R., Igor, S., Jean-Philippe, N., Marie Hélène Mahagne, Antoine, M., Marc, B., Jean-Baptiste, C., Vincent, N., Frederic, S., Gilles, M., Jean-Paul, B., Bernard, D., Michel, M., Désiré, O., Bernard, C., Joseph, M., Etienne, B., Jean Philippe Brugnaux, Alain, F., Pierre, N., Jean-Baptiste, B., Sebastien Schellong Harald Darius, Georg, K., Andreas, K., Uwe, G., Bernd-Thomas, K., Thomas, S., Jan, P., Enno, E., Heinz-Dieter, Z., Peter, R., Christoph, A., Gerd-Ulrich, H., Holger, M., Andreas, P., Stefan, Z., Wolfgang, E., Guenter, R., Dirk, G., Norbert, L., Petra, S., Henning, W., Cosmas, W., Steffen, S., Toralf, S., Adyeri, B., Maximilian, K., Hans-Hermann, Z., Friedhelm, K., Andreas, C., Sabine, O., Torsten, L., Hermann-Josef, H., Gunter, L., Hans-Walter, B., Gunter, H., Dietrich, R., Joachim, H., Praxis Dres Werner Erdle, Wilfried, D., Janna, D., Karl-Albrecht, R., Reinhold, V., Thomas, M., Peter, M., Uwe, H., Volker, E., Heinz, H., Heinz, L., Volker, L., Heiner, M., Christian, S., Herrmann, L., Thomas, B., Gunter, B., Susanne, K., Karsten, M., Sylvia, B., Muwafeg, A., Hans-Holger, E., Carsten, S., Peter, B., Laszlo, K., Britta, S., Wilhelm, H., Jens-Uwe, R., Andras Vertes Gabor Szantai, Andras, M., Nikosz, K., Zoltan, B., Erno, K., Balazs, G., Ferenc, J., Gizella, J., Sandor, K., Zoltan, L., Zsolt, M., Bela, M., Ebrahim, N., Tamas, H., Peter, P., Gabriella, S., Sandor, V., Andras, N., Gabriella, E., Judit, F., Mihaly, E., Giuliana Martini Leone Maria Cristina, Eros, T., Rita, S., Sophie, T., Giovanni Di Minno, Marco, M., Teresa Maria Caimi, Maria, T., Roberto, C., Daniela, P., Roberto, Q., Franco, C., Raffaele, F., Vincenzo, O., Raffaele, R., Roberto, S., Raimondo De Cristofaro, Giuliana, G., Angelo De Blasio, Jorge Salerno Uriate, Flavia, L., Enrico Maria Pogliani, Grzegorz, B., Michele, A., Antonio, M., Mauro, F., Arturo, R., Luciano, F., Andrea, M., Fabrizio, G., Luca, T., Maria, S., Sergio, N., Paolo, R., Antonio, A., Claudio, B., Filippo, T., Massimo, V., Maria, D., Maria Grazia Bongiorni, Silva, S., Alessandro, C., Corrado, L., Enrico, S., Gaetano, S., Tondo, C., Paolo, G., Carmine, M., Saverio, I., Hugo Ten Cate J, H.R., Andreas, L., Henk, A., Maarten, B., Mathijs, P., Coen van Guldener, Johannes, H., S H K P, R.N., Pieter, H., Walter, H., E Groenemeijer, B., Terpstra, W., Cees, B., L V, A.B., Eivind Berge Per Anton Sirnes, Erik, G., Torstein, H., Knut, E., Arne, H., Gunnar, S., Anders, Ø., Beraki, G., Arne, S., Peter, C., Torbjørn, Ø., Svein Høegh Henrichsen, Jan Erik Otterstad, Janina Stepinska Andrzej Gieroba, Malgorzata, B., Michal, O., Beata, W., Krystyna, L., Jaroslaw, Wieslaw, S., Jerzy, K., Roman, Z., Jaroslaw, H., Lucyna, S., Lech, K., Marcin, G., Piotr, M., Maciej, O., Grzegorz, K., Malgorzata, K., Zbigniew, L., Bozenna, O., Jerzy, L., Elzbieta, Z., Agnieszka, K., Malgorzata, C., Iwona, W., Grzegorz, O., Marek, B., Marcin, O., Grazyna, G., Piotr, R., Grzegorz, S., Ryszard, S., Boguslaw, O., Piotr, K., Krzysztof, G., Krzysztof, C., Jaroslaw, J., Pawel, M., Waldemar, M., Stanislaw, M., Roman, L., Jacek, B., Teresa, R., Grzegorz, R., Ewa, D., Jadwiga, N., Jozef, L., Vera Eltishcheva Roman Libis, Gadel, K., Dmitry, B., Liudmila, E., Alexander, K., Eduard, Y., Dmitry, Z., Olga, B., Olga, M., Evgeniy, M., Konstantin, Z., Tatyana, N., Yulia, M., Elena, P., Konstantin, S., Maria, R., Yulia, S., Alla, K., Konstantin, N., Oksana, Z., Anna, Z., Victor, K., Sergey, P., Maria, P., Anton, E., Elena Aleksandrova Oksana Drapkina, Alexander, V., Oleg, N., Petr, C., Svetlana, R., Mikhail, S., Borys, K., Alexey, U., Xavier Vinolas Pere Alvarez Garcia, Maria Fernanda Lopez Fernandez, Luis Tercedor Sanchez, Salvador Tranche Iparraguirre, Pere Toran Monserrat, Emilio Marquez Contreras, Jordi Isart Rafecas, Juan Motero Carrasco, Pablo Garcia Pavia, Casimiro Gomez Pajuelo, Luis Miguel Rincon Diaz, Luis Fernando Iglesias Alonso, Angel Grande Ruiz, Jordi Merce Klein, Jose Ramon Gonzalez Juanatey, Ines Monte Collado, Herminia Palacin Piquero, Carles Brotons Cuixart, Esther Fernandez Escobar, Joan Bayo, I.L., Cecilia Corros Vicente, Manuel Vida Gutierrez, Francisco Epelde Gonzalo, Carlos Alexandre Almeida Fernandez, Encarnacion Martinez Navarro, Juan Jose Montero Alia, Maria Barreda Gonzalez, Maria Angels Moleiro Oliva, Jose Iglesias Sanmartin, Mercedes Jimenez Gonzalez, Maria Del Mar Rodriguez Alvarez, Juan Herreros Melenchon, Tomas Ripoll Vera, Manuel Jimenez Navarro, Maria Vazquez Caamano, Maria Fe Arcocha Torres, Gonzalo Marcos Gomez, Andres Iniguez Romo, Miguel Angel Prieto Diaz, Mårten Rosenqvist Alexander Wirdby, Centrumkliniken, Jan, L., Kerstin, H., Micael, E., Arnor, E., Ulf, B., Liu, B., Anders, L., Lars-Bertil, O., Mikael, G., Lars, A., Lars, B., Claes, B., Ali, H., Björn, M., Marianne, E., Åke, O., Håkan, L., Peter, S., Katarina, T., Hans, H., Pyotr, P., Fredrik, B., Ingar, T., Milita, C., Jan-Erik, K., Agneta, A., Lennart, M., Johan, E., Jörgen, T., Aida, H., Steen, J., Per, S., Jan Steffel Johann Debrunner, Juerg, H.B., Dipen, S., Iurii Rudyk Vira Tseluyko, Oleksandr, K., Svitlana, Z., Igor, K., Oleksandr, P., Iryna, K., Nestor, S., Yuriy, M., Oleksiy, U., Olena, K., Yevgeniya, S., Oleg, S., Mykola, S., Andriy, Y., Susanna, T., Ivan, F., Will Murdoch Naresh Chauhan, Daryl, G., Louise, L., Ramila, P., Philip, S., Bennett, W., Alex, C., Niranjan, P., Jhittay, P., Andrew, R., S Kainth, M., Karim, L., Kevin, D., Gill, P., Joanna, M., Laura, H., Trevor, G., Helga, W., Cumberlidge, Colin, B., Catherine, B., Kevin, J., Shoeb, S., Richard, C., Bhupinder, S., Willcock, W., Sircar, S., John, C., Gilliand, A., Roman, B., Strieder, E., Peter, H., Anne, W., Michael, S., Graham, K., Bhaskhar, V., Nigel, B., Paul, E., Clark, M., John, B., Jennifer, L., Fisher, E., Tim, F., Richard, K., Neil, P., Elizabeth, A., Michael, A., Ramesh, C., Pete, W., Simon, F., Sue, F., Julian, T., Hasan, C., Gary, T., Dawn, T., Matt, P., Claire, S., Carolyn, P., Mark, R., Angus, J., Helen, S., Hywel, J., Claire, G., Matthew, B., Philip, W., Jehad, A., Simon, W., William, L., Phil, E., Frances, S., Neil, M., Stephen, R., Yvette, S., Richard, W., Philip, P., Paul, W., Preeti, P., Andrew, G., Railton, T., Emyr, D., Jonathan, M., Marc, J., Claire, H., Thompson, R., Bijoy, S., Keith, B., Susan, B., Helen, L., David, R., Ulka, C., Ikram, H., Paul, A., Claire, J., Phil, W., Jane, E., Lisa, G., Janet, G., Alison, M., Poland, K., Conor, M., Warke, A., Paul, C., Burns, D., Smith, R., Kamath, R., Jonathan, W., Ian, H., Stephen, V., Paul, R., Hilary, P., Jayesh, P., Amar, A., Nigel, H., Richard, D., Nigel, D., Catherine, N., Mark, D., Purnima, S., Sophia, G., Charlotte, H., Raife, O., Martin, A., Mira, P., Gordon, I., Shahid, A., Catherine, R., Fiaz, C., Sabrina, K., Stephanie, S., Sharon, P., Warwick, C., Neil, R., Amy Butler Steven Coates, Ben, W., Daniel, J., Steve, W., Diane, S., Toh, W., Mark, B., Melanie, D., David, C., Sarah, D., Ben, F., Nick, H., Henry, C., Jon, S., Tim, M., Salah, E., Diane, G., Justin, W., Richard, V., Karen, F., Rob, H., Kashif, Z., Catherine, L., Rebecca, W., Paul, M., Andre, B., Philip, C., Mike, W., Mark, P., Chaminda, D., Greg, R., James, B., Polly, J., Rajesh, M., Matthew, A., Robin, F., Nicolas, T., Simon, C., Rory, R., Simon, R., Christine, A., Ann, F., Andrew, H., Simon, D., Minnal, N., Iain, M., Jane, G., Phil, S., John, S., Emma, B., Adam Blenkhorn Bhuwanendu Singh, Penny, A., William van Gaal, Walter, A., Philip, T., Ron, L., Jens, K., Andrei, C., Hosen, K., David, E., John, F., Bronte, A., Thanh, P., James, R., David, O., Sang Cheol Bae, Harry, G., Patrick, C., Greg, S., Margaret, A., Maurits, B., Astin, L., John Eikelboom Robert Luton, Milan, G., Amritanshu Shekhar Pandey, Stephen, C., Rolland, L., Philippe, B., Félix, A., Joseph, B., John, H., Germain, P., Miranda du Preez, Bradley, S., Reginald, N., Ripple, D., Tomasz, H., Andrea, L., Ratika, P., James, C., Benoit, C., Brian, R., Jorge, B., Saul, V., Sameh, F., Ahmed Mowafy Azza Katta, Mazen, T., Moustafa, N., Mohamed, S., Seif Kamal Abou Seif, Tarek, K., Ahmed Abd El-Aziz, Nasser, T., Ashraf, R., Atef, E., Mohamed Gamal El Din, Magdi, E., Adel, E., David Kettles Junaid Bayat, Heidi, S., Adrian, H., Ynez, K., Riaz, G., Thayabran, P., Michele, G., Louis van Zyl, Hendrik, T., Andrew, M., Rikus, L., Deon, G., Pindile, M., Siddique, I., Fayzal, A., Johannes, E., Shambu, M., Wessel, O., Rehana, L., Veronica, U., Wael AlAl Mahmeed AbdullahNaeemi, Ghazi, Y., Nooshin, B., Munther, A., Rajan, M., Rupesh, S., Ahmed, N., Mohamed, I., Amrish, A., Mukesh, N., Ehab, M.E., Adel, W., Rajeev, G., Michael Cox Scott Beach, Peter, D., Stephen, F., Kevin, F., Miguel, F., W Michael Kutayli, Annette, Q., Niraj, S., Vance, W., Stephen, M., Mark, A., Edwin, B., Roddy, C., Ted, G., Rodney, I., Jorge, G., Howard, N., Pamela, R., Rajneesh, R., Marcus, W., Daniel, N., Keith, F., Ihsan, H., Robert, M., Sridevi, P., Daniel, T., Charles, T., Moustafa, M., Cas, C., Walter, P., Alisha, O., George, P., Jaspal, G., James, W., and Firas, K.

Subjects
Vitamin K antagonists, Atrial fibrillation, GARFIELD-AF, Non-vitamin K antagonist oral anticoagulants, Oral anticoagulation, Phenprocoumon, Settore MED/11 - Malattie dell'Apparato Cardiovascolare
Abstract

The Global Anticoagulant Registry in the FIELD-Atrial Fibrillation (GARFIELD-AF) is a worldwide non-interventional study of stroke prevention in patients with non-valvular AF.52,080 patients with newly diagnosed AF were prospectively enrolled from 2010 to 2016. 4121 (7.9%) of these patients were recruited in DACH [Germany (n = 3567), Austria (n = 465) and Switzerland (n = 89) combined], and 47,959 patients were from 32 countries in other regions worldwide (ORW). Hypertension was most prevalent in DACH and ORW (85.3% and 75.6%, respectively). Diabetes, hypercholesterolaemia, carotid occlusive disease and vascular disease were more prevalent in DACH patients vs ORW (27.6%, 49.4%, 5.8% and 29.0% vs 21.7%, 40.9%, 2.8% and 24.5%). The use of non-vitamin K antagonist oral anticoagulants (NOACs) increased more in DACH over time. Management of vitamin K antagonists was suboptimal in DACH and ORW (time in therapeutic range of INR ≥ 65% in 44.6% and 44.4% of patients or ≥ 70% in 36.9% and 36.0% of patients, respectively). Adjusted rates of cardiovascular mortality and MI/ACS were higher in DACH while non-haemorrhagic stroke/systemic embolism was lower after 2-year follow-up.Similarities and dissimilarities in AF management and clinical outcomes are seen in DACH and ORW. The increased use of NOAC was associated with a mismatch of risk-adapted anticoagulation (over-and-undertreatment) in DACH. Suboptimal control of INR requires educational activities in both regional groups. Higher rates of cardiovascular death in DACH may reflect the higher risk profile of these patients and lower rates of non-haemorrhagic stroke could be associated with increased NOAC use.

Published
2022

12. Exploiting the Molecular Template of Angiotensinogen in the Discovery and Design of Peptidyl, Pseudopeptidyl and Peptidemimetic Inhibitors of Human Renin: A Structure-Activity Perspective

Author

Sawyer, Tomi K., Hester, Jackson B., Schostarez, Heinrich J., Thaisrivongs, S., Bundy, Gordon L., Liu, Li, Bradford, V. Susan, De Vaux, Anne E., Staples, Douglas J., Maggiora, Linda L., TenBrink, Ruth E., Kinner, John H., Smith, Clark W., Pals, Donald T., Couch, Sally J., Hinzmann, Jessica S., Poorman, Roger A., Einspahr, Howard M., Finzel, Barry C., Watenpaugh, Keith D., Mao, Boryeu, Epps, Dennis E., Kezdy, Ferenc J., Heinrikson, Robert L., and Dunn, Ben M., editor

Published
1991
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26. Evidence for transbilayer, tail-to-tail cholesterol dimers in dipalmitoylglycerophosphocholine liposomes

Author

Harris, Jessica S., Epps, Dennis E., Davio, Stephen R., and Kezdy, Ferenc J.

Subjects
Lecithin -- Research, Liposomes -- Research, Cholesterol -- Research, Biological sciences, Chemistry
Abstract

Differential scanning calorimetric analysis of multilamellar liposomes of 2,3-dipalmitoyl-sn-glycero-1-phosphocholine (DPPC) suggests that cholesterol exists as interlamellar tail-to-tail dimer in the DPPC bilayers. In the fully extended state, solid cholesterol is interspersed with solid-ordered domains. Cholesterol enhances the stability of the bilayer and the dissolution of lipids in the phospholipid bilayer.

Published
1995

27. Kinetic studies with the non-nucleoside HIV-1 reverse transcriptase inhibitor U-88204E

Author

Althaus, Irene W., Chou, James J., Gonzales, Andrea J., Deibel, Martin R., Kuo-Chen Chou, Kezdy, Ferenc J., Romero, Donna L., and Palmer, John R.

Subjects
HIV (Viruses) -- Inactivation, Reverse transcriptase -- Research, Biological sciences, Chemistry
Abstract

The inhibitory activity of Bis (heteroaryl) piperazine U-88204 E on HIV-1 reverse transcriptase (RT) is analogous to that of AZT, ddI, ddC is useful in the treatment of AIDS patients. Thus, there is a great need for research involving RT inhibitors. U-88204E exhibits antiviral activity at nontoxic doses in the HIV-1 populated lymphocytes in cultured tissues.

Published
1993

28. Improvement of magnetocaloric properties of Gd-Ge-Si alloys by alloying with iron

Author

Erenc-Sędziak T., Cieślak G., Kowalczyk M., Ferenc J., and Kulik T.

Subjects
Physics, QC1-999
Abstract

The influence of annealing of Gd5Ge2Si2Fex alloys at 1200°C and of alloying with various amount of iron on structure as well as thermal and magnetocaloric properties is investigated. It was found that annealing for 1 to 10 hours improves the entropy change, but reduces the temperature of maximum magnetocaloric effect by up to 50 K. Prolonged annealing of the Gd5Ge2Si2 alloy results in the decrease of entropy change due to the reduction of Gd5Ge2Si2 phase content. Addition of iron to the ternary alloy enhances the magnetocaloric effect, if x = 0.4 – 0.6, especially if alloying is combined with annealing at 1200°C: the peak value of the isothermal entropy change from 0 to 2 T increases from 3.5 to 11 J/kgK. Simultaneously, the temperature of maximum magnetocaloric effect drops to 250 K. The changes in magnetocaloric properties are related to the change in phase transformation from the second order for arc molten ternary alloy to first order in the case of annealed and/or alloyed with iron. The results of this study indicate that the minor addition of iron and heat treatment to Gd-Ge-Si alloys may be useful in improving the materials’ magnetocaloric properties..

Published
2013
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29. Mechanical Testing of Iron based Bulk Metallic Glasses and Their Suitability for Force Sensors

Author

Erenc-Sędziak T., Kowalczyk M., Ferenc J., Cieślak G., and Kulik T.

Subjects
Physics, QC1-999
Abstract

Thermal, mechanical and magnetic properties of (Fe-Co)-(Zr/Si)-Nb-B alloys in the form of rapidly quenched rods of 1.2 mm in diameter were studied. The as-cast alloys with Zr were crystalline, and the alloys with Si were amorphous. Microhardness measured at 50 g load is from 500 to 2000 HV (the less cobalt, the higher), and the compressive strength reaches nearly 4000 MPa for Si doped alloys and 2000 MPa for Zr doped ones. This substantial difference may be attributed to partial crystallinity of the latter alloys. The magnetic hysteresis loops of fully amorphous rods measured under compression, exhibited a clear dependence of permeability vs. stress, proving that iron-based bulk metallic glasses may be promising materials for magnetoelastic force sensors.

Published
2013
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34. Magnetically soft nanomaterials for high-temperature applications

Author

Kulik, T., Wlazlowska, A., Ferenc, J., and Latuch, J.

Subjects
Magnetic alloys -- Analysis, Magnetism -- Measurement, Business, Electronics, Electronics and electrical industries
Abstract

FeCo-based soft magnetic alloys of compositions [Fe.sub.45][Co.sub.43][Cu.sub.1][B.sub.3.6][Zr.sub.7.4-x]A[M.sub.x], where x = 3.7 at.% and 7.4 at.%, and the alloying metals (AM) are Nb and Hf and were prepared in the form of amorphous ribbons by melt-spinning technique. A two-phase microstructure, consisting of [alpha]-FeCo nanocrystais and amorphous matrix, was created by partial devitrification of the amorphous alloys during annealing for 1 h at temperatures 500 [degrees]C-600 [degrees]C. The crystallization process of the amorphous alloys was studied using differential scanning calorimetry, X-ray diffractometry, and transmission electron microscopy. The quasi-static hysteresis loop was measured using an inductive method. Partial replacement of zirconium by hafnium improved thermal stability of amorphous structure and magnetic properties of the alloys studied. The effect of niobium is opposite. The best magnetic properties were found in the alloy [Fe.sub.45][Co.sub.43][Cu.sub.1][B.sub.3.7][Zr.sub.3.7][Hf.sub.3.7]. It was found that nanocrystallization temperature strongly influences the thermal stability of the magnetic properties of the alloys studied. Index Terms--FeCo alloys, HITPERM, nanocrystalline materials, soft magnetic alloys.

Published
2002

35. Correlation between microstructure and temperature dependence of magnetic properties in Fe60Co18(Nb,Zr)6B15Cu1 alloy series.

Author

Blázquez, J. S., Franco, V., Conde, C. F., Conde, A., Ferenc, J., Kulik, T., and Kiss, L. F.

Subjects
MICROSTRUCTURE, TEMPERATURE, MAGNETIC properties, NANOCRYSTALS, ALLOYS, TRANSMISSION electron microscopy, CURIE temperature, MAGNETIZATION
Abstract

Temperature dependence of magnetic properties of nanocrystalline Fe60Co18Cu1B15Nb6-xZrx (x=0, 3, 6) alloys has been studied at different stages of devitrification. Transmission electron microscopy shows nanocrystals of the size ∼5 nm, which remains almost constant along the nanocrystallization process. Curie temperature of the residual amorphous phase decreases as nanocrystallization progresses for all the studied alloys. Thermal dependence of the exchange stiffness constant is obtained from the measurement of specific magnetization and coercivity as a function of crystalline fraction and temperature for the three studied alloys. [ABSTRACT FROM AUTHOR]

Published
2009
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39. Correlation between microstructure and temperature dependence of magnetic properties in [Fe.sub.60][Co.sub.18][(Nb,Zr).sub.6][B.sub.15][Cu.sub.1] alloy series

Author

Blazquez, J.S., Franco, V., Conde, C.F., Conde, A., Ferenc, J., Kulik, T., and Kiss, L.F.

Subjects
Cobalt -- Magnetic properties, Cobalt -- Electric properties, Iron alloys -- Magnetic properties, Iron alloys -- Thermal properties, Iron alloys -- Electric properties, Magnetization -- Analysis, Niobium -- Electric properties, Niobium -- Magnetic properties, Zirconium -- Magnetic properties, Zirconium -- Electric properties, Physics
Abstract

The temperature dependence of magnetic properties of nanocrystalline [Fe.sub.60][Co.sub.18][Cu.sub.1][B.sub.15][Nb.sub.6-x][Zr.sub.x] (x=0, 3, 6) alloys is studied at different stages of devitrification. Thermal dependence of the exchange stiffness constant is obtained from the measurement of specific magnetization and coercivity as a function of crystalline fraction and temperature for the three studied alloys.

Published
2009

40. The Substrate Specificity of Phospholipase A2: The Reaction of the Enzyme with 3-Octanoyloxy-4-Nitrobenzoic Acid

Author

Michael A. Markowitz, Ferenc J. Kezdy, and John T. Seykora

Subjects
chemistry.chemical_classification, Chromatography, food.ingredient, biology, Chemistry, chemistry.chemical_element, General Chemistry, Calcium, Lecithin, Hydrolysis, Enzyme, food, Reaction rate constant, Phospholipase A2, Enzymatic hydrolysis, biology.protein, Enzyme kinetics
Abstract

3-Octanoyloxy-4-nitrobenzoic acid is hydrolyzed by the phospholipase A2 (D-49) from the venom of Agkistrodon piscivorus. The hydrolytic reaction is truly catalytic, requiring the presence of calcium ion (Kd=3.3 ± 0.7mM). At pH=7.0 the value of the enzymatic rate constant is (Kcat/Km)max=175 ± 14 M−1 sec−1, comparable to that of the enzymatic hydrolysis of 3-sn-dibutyryl lecithin.

Published
2010

41. Inflow stenoses in dysfunctional hemodialysis access fistulae and grafts

Author

Rob H.H. van der Rijt, Harrie C. M. van den Bosch, Ferenc J. Nobrega, Alexander V. Tielbeek, Lucien E. M. Duijm, Petra Douwes-Draaijer, Ylian S. Liem, Philippe W.M. Cuypers, and Epidemiology

Subjects
Adult, Male, medicine.medical_specialty, medicine.medical_treatment, Subclavian Artery, Constriction, Pathologic, Magnetic resonance angiography, Arteriovenous Shunt, Surgical, Catheters, Indwelling, Renal Dialysis, medicine.artery, Angioplasty, medicine, Humans, Prospective Studies, cardiovascular diseases, Subclavian artery, Aged, Aged, 80 and over, medicine.diagnostic_test, business.industry, Incidence, Angiography, Digital Subtraction, Digital subtraction angiography, Middle Aged, medicine.disease, Surgery, Stenosis, Regional Blood Flow, Nephrology, Angiography, cardiovascular system, Female, business, Subclavian vein, Vascular Stenosis, Magnetic Resonance Angiography
Abstract

Background: The aim of the study is to prospectively determine the incidence of inflow stenoses in dysfunctional hemodialysis access arteriovenous fistulae (AVFs) and grafts (AVGs). Methods: Contrast-enhanced magnetic resonance angiography (CE-MRA) was performed of 66 dysfunctional AVFs and 35 AVGs in 56 men and 45 women (mean age, 62 years; age range, 31 to 86 years). Complete inflow (from the subclavian artery), shunt region, and complete outflow (including subclavian vein) were shown at CE-MRA. In addition to standard digital subtraction angiography (DSA) of the shunt region and outflow, DSA of the complete inflow was obtained through access catheterization of all cases in which CE-MRA showed an inflow stenosis. Vascular stenosis is defined as greater than 50% decrease in luminal diameter compared with an uninvolved vascular segment located adjacent to the stenosis. Endovascular intervention of stenoses was performed in connection with DSA. Results: CE-MRA showed 19 arterial stenoses in 14 patients (14%). DSA confirmed 18 of these lesions in 13 patients and showed no additional inflow lesions. Of the 13 patients, 7 patients had arterial stenoses only and 6 patients had accompanying stenoses in the shunt region and/or outflow. Referral criteria for the 13 patients to undergo access evaluation had been decreased flow rates (9 patients), steal symptoms (2 patients), and insufficient access maturation (2 patients). Access flow of the 9 patients with a low-flow access improved from 477 ± 74 mL/min to 825 ± 199 mL/min after angioplasty. One patient with steal symptoms became symptom free after angioplasty. Endovascular intervention in 3 patients proved to be unsuccessful. Conclusion: Inflow stenoses are not uncommon in dysfunctional hemodialysis access shunts. We suggest that radiological evaluation comprise assessment of the complete arterial inflow.

Published
2006

42. The Lectin Domain of UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase 1 Is Involved in O-Glycosylation of a Polypeptide with Multiple Acceptor Sites

Author

Mari Tenno, Ferenc J. Kezdy, Åke P. Elhammer, Akira Kurosaka, and Aki Saeki

Subjects
Glycosylation, Amino Acid Motifs, Blotting, Western, Polypeptide N-acetylgalactosaminyltransferase, Ricin, Biology, Biochemistry, Substrate Specificity, Serine, chemistry.chemical_compound, Tandem repeat, C-type lectin, Lectins, parasitic diseases, Animals, Point Mutation, Cysteine, Disulfides, Amines, Threonine, Molecular Biology, Binding Sites, Dose-Response Relationship, Drug, Sepharose, CD69, C-terminus, Monosaccharides, Cell Biology, Molecular biology, Recombinant Proteins, Protein Structure, Tertiary, Rats, carbohydrates (lipids), Kinetics, Models, Chemical, chemistry, COS Cells, Mutation, Mutagenesis, Site-Directed, N-Acetylgalactosaminyltransferases, lipids (amino acids, peptides, and proteins), Gene Deletion, Protein Binding
Abstract

Mucin type O-glycosylation begins with the transfer of GalNAc to serine and threonine residues on proteins by a family of UDP-GalNAc:polypeptide N-acetylgalactosaminlytransferases. These enzymes all contain a lectin-like (QXW)(3) repeat sequence at the C terminus that consists of three tandem repeats (alpha, beta, and gamma). The putative lectin domain of one of the most ubiquitous isozymes, GalNAc-T1, is reportedly not functional. In this report, we have reevaluated the role of the GalNAc-T1 lectin domain. Deletion of the lectin domain resulted in a complete loss of enzymatic activity. We also found that GalNAc-T1 has two activities distinguished by their sensitivities to inhibition with free GalNAc; one activity is sensitive, and the other is resistant. In our experiments, the former activity is represented by the O-glycosylation of apomucin, an acceptor that contains multiple glycosylation sites, and the latter is represented by synthetic peptides that contain a single glycosylation site. Site-directed mutagenesis of the lectin domain selectively reduced the former activity and identified Asp(444) in the alpha repeat as the most important site for GalNAc recognition. A further reduction of the GalNAc-inhibitable activity was observed when both Asp(444) and the corresponding aspartate residues in the beta and the gamma repeats were mutated. This suggests a cooperative involvement of each repeat unit in the glycosylation of polypeptides with multiple acceptor sites.

Published
2002

43. Identification of two cysteine residues involved in the binding of UDP-GalNAc to UDP-GalNAc:polypeptideN-acetylgalactosaminyltransferase 1 (GalNAc-T1)

Author

Mari Tenno, Shinya Toba, Akira Kurosaka, Ferenc J. Kezdy, and Åke P. Elhammer

Subjects
Alanine, Polypeptide N-acetylgalactosaminyltransferase, Biochemistry, Isozyme, carbohydrates (lipids), Serine, chemistry.chemical_compound, Biosynthesis, chemistry, parasitic diseases, medicine, Diisopropyl fluorophosphate, Metallothionein, lipids (amino acids, peptides, and proteins), Cysteine, medicine.drug
Abstract

Biosynthesis of mucin-type O-glycans is initiated by a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases, which contain several conserved cysteine residues among the isozymes. We found that a cysteine-specific reagent, p-chloromercuriphenylsulfonic acid (PCMPS), irreversibly inhibited one of the isozymes (GalNAc-T1). Presence of either UDP-GalNAc or UDP during PCMPS treatment protected GalNAc-T1 from inactivation, to the same extent. This suggests that GalNAc-T1 contains free cysteine residues interacting with the UDP moiety of the sugar donor. For the functional analysis of the cysteine residues, several conserved cysteine residues in GalNAc-T1 were mutated individually to alanine. All of the mutations except one resulted in complete inactivation or a drastic decrease in the activity, of the enzyme. We identified only Cys212 and Cys214, among the conserved cysteine residues in GalNAc-T1, as free cysteine residues, by cysteine-specific labeling of GalNAc-T1. To investigate the role of these two cysteine residues, we generated cysteine to serine mutants (C212S and C214S). The serine mutants were more active than the corresponding alanine mutants (C212A and C214A). Kinetic analysis demonstrated that the affinity of the serine-mutants for UDP-GalNAc was decreased, as compared to the wild type enzyme. The affinity for the acceptor apomucin, on the other hand, was essentially unaffected. The functional importance of the introduced serine residues was further demonstrated by the inhibition of all serine mutant enzymes with diisopropyl fluorophosphate. In addition, the serine mutants were more resistant to modification by PCMPS. Our results indicate that Cys212 and Cys214 are sites of PCMPS modification, and that these cysteine residues are involved in the interaction with the UDP moiety of UDP-GalNAc.

Published
2002

44. Types of Lipid Clustering in Phospholipid Membranes as Classified by Nearest-Neighbor Recognition Analysis

Author

and Ferenc J. Kézdy, Yasuhito Miyake, Steven L. Regen, and Takehisa Dewa

Subjects
Chromatography, Apparent Equilibrium Constant, Phospholipid, Surfaces and Interfaces, Composition (combinatorics), Condensed Matter Physics, k-nearest neighbors algorithm, chemistry.chemical_compound, Crystallography, Membrane, chemistry, Electrochemistry, General Materials Science, Fluid phase, Cluster analysis, Spectroscopy
Abstract

The nearest-neighbor recognition method is applied to the problem of phospholipid clustering in bilayers composed of di[1,2-dimyristoyl-sn-glycero-3-phosphoethanol(3‘-thio)propionamide] (I), di[1,2-distearoyl-sn-glycero-3-phosphoethanol(3‘-thio)propionamide] (II), and 1,2-dimyristoyl-sn-glycero-3-phosphoethanol(3‘-thio)propionamide−1,2-distearoyl-sn-glycero-3-phosphoethanol(3‘-thio)propionamide (III). The value and the composition dependency of the apparent equilibrium constant, K, defined by the equilibrium concentrations of homodimers (I and II) and the corresponding heterodimer (III), allow one to distinguish among three fundamentally different classes of clustering: (i) random clustering, (ii) cooperative clustering, and (iii) nonrandom−noncooperative clustering. Experimental results indicate that random clustering of these phospholipids is pervasive in fluid bilayers, whereas cooperative clustering exists in the gel−fluid coexistence region. In the physiologically relevant fluid phase, these same li...

Published
2000

45. [Untitled]

Author

Akira Kurosaka, Ake P. Elhammer, and Ferenc J. Kezdy

Subjects
chemistry.chemical_classification, Glycosylation, biology, Chemistry, Stereochemistry, Protein primary structure, Polypeptide N-acetylgalactosaminyltransferase, Active site, Peptide, Cell Biology, Biochemistry, Acceptor, Serine, chemistry.chemical_compound, biology.protein, Threonine, Molecular Biology
Abstract

The in vitro and in vivo specificity of the family of peptide:N-acetylgalactosaminyltransferases (GalNAcT) is analyzed on the basis of the reactivity and/or inhibitory activity of peptides and protein segments. The transferases appear to be multi-substrate enzymes with extended active sites containing a least nine subsites that interact cooperatively with a linear segment of at least nine amino acid residues on the acceptor polypeptide. Functional acceptor sites are located on the surface of the protein and extended conformations (β-strand conformation) are preferred. The acceptor specificity of GalNAc-T can be predicted from the primary structure of the acceptor peptide with an accuracy of 70 to 80%. The same GalNAc-T enzymes catalyze the glycosylation of both serine and threonine residues. The higher in vitro catalytic efficiency toward threonine versus serine is the result of enhanced binding as well as increased reaction velocity, both effects being the result of steric interactions between the active site of the enzyme and the methyl group of threonine. Results from substrate binding studies suggest that GalNAc-T catalyzed transfer proceeds via an ordered sequential mechanism.

Published
1999

49. Novenamines as inhibitors of two independent enzymes during DNA replication in a toluenized Escherichia coli cell system

Author

Fritz Reusser, Irene W. Althaus, Charles H. Spilman, Ferenc J. Kezdy, and T. Peterson

Subjects
Pharmacology, Dose-Response Relationship, Drug, DNA synthesis, biology, Circular bacterial chromosome, Topoisomerase, DNA replication, DNA, Biochemistry, DNA gyrase, chemistry.chemical_compound, chemistry, Escherichia coli, biology.protein, medicine, Enzyme Inhibitors, RNase H, Novobiocin, medicine.drug
Abstract

The amphiphilic novenamines described in this report have been shown previously to be specific inhibitors of human immunodeficiency virus type 1 reverse transcriptase-associated ribonuclease, which they inhibit when they are in the micellar state but not when they are monomeric. These compounds also inhibit the bacterial enzyme DNA gyrase, which is essential for DNA replication. Hence, the present studies were initiated to determine whether the molecular species inhibiting the gyrase reaction was the monomeric or the micellar form. For this purpose, the rate of DNA replication was measured in a toluenized Escherichia coli cell system in the presence of increasing concentrations of novenamines. The resulting concentration-response curves proved anomalous, suggesting the involvement of micelles or some other, noncovalently aggregated forms of the inhibitors. The results were analyzed in terms of a variety of kinetic schemes and were found to be most consistent with the model where novenamines inhibit replicative DNA synthesis predominantly as cooperative dimers and, to a lesser extent, as monomers, but not as highly aggregated micelles. Based on this analysis and the knowledge that novobiocin and all novenamine-containing analogs are powerful gyrase inhibitors, we conclude that the target of the cooperative, dimeric inhibition is the gyrase, whereas the monomers of the novenamines inhibit another enzyme species involved in the bacterial DNA replication process.

Published
1996

50. The benzylthio-pyrimidine U-31,355, a potent inhibitor of HIV-1 reverse transcriptase

Author

Mariano Busso, Kuo-Chen Chou, W. Gary Tarpley, Kathleen M. Downey, Donna L. Romero, Paul A. Aristoff, Kellie M. Franks, Fritz Reusser, Richelle J. Lemay, Lionel Resnick, Ferenc J. Kezdy, Martin R. Deibel, Irene W. Althaus, Antero G. So, and Richard C. Thomas

Subjects
DNA polymerase, Ribonuclease H, HIV Infections, Antiviral Agents, Biochemistry, Mice, Viral Proteins, Non-competitive inhibition, Animals, Humans, Lymphocytes, Enzyme Inhibitors, Binding site, Mathematical Computing, Polymerase, Pharmacology, biology, RNA-Directed DNA Polymerase, HIV Reverse Transcriptase, Reverse transcriptase, Kinetics, Pyrimidines, Retroviridae, Enzyme inhibitor, HIV-1, biology.protein, Reverse Transcriptase Inhibitors, Primer (molecular biology)
Abstract

U-31,355, or 4-amino-2-(benzylthio)-6-chloropyrimidine is an inhibitor of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) and possesses anti-HIV activity in HIV-1-infected lymphocytes grown in tissue culture. The compound acts as a specific inhibitor of the RNA-directed DNA polymerase function of HIV-1 RT and does not impair the functions of the DNA-catalyzed DNA polymerase or the RNase H of the enzyme. Kinetic studies were carried out to elucidate the mechanism of RT inhibition by U-31,355. The data were analyzed using Briggs-Haldane kinetics, assuming that the reaction is ordered in that the template:primer binds to the enzyme first, followed by the addition of dNTP, and that the polymerase is a processive enzyme. Based on these assumptions, a velocity equation was derived that allows the calculation of all the essential forward and backward rate constants for the reactions occurring between the enzyme, its substrates, and the inhibitor. The results obtained indicate that U-31,355 acts as a mixed inhibitor with respect to the templatetprimer and dNTP binding sites associated with the RNA-directed DNA polymerase domain of the enzyme. The inhibitor possessed a significantly higher binding affinity for the enzyme-substrate complexes than for the free enzyme and consequently did not directly affect the functions of the substrate binding sites. Therefore, U-31,355 appears to impair an event occurring after the formation of the enzyme-substrate complexes, which involves either inhibition of the phosphoester bond formation or translocation of the enzyme relative to its template:primer following the formation of the ester bond. Moreover, the potency of U-31,355 depends on the base composition of the template:primer in that the inhibitor showed a much higher binding affinity for the enzyme-poly (rC):(dG) 10 complexes than for the poly (rA):(dT) 10 complexes.

Published
1996

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