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1. Transverse momentum correlations in hadronic Z decays

Author: Paul Hanke, A. Jacholkowska, C. N. Booth, A. Blondel, J. Jousset, Michael Schmitt, P.G. Bright-Thomas, M. Verderi, Jm Yamartino, Mc Lemaire, J.H. Dann, H. Dietl, D. J. Candlin, T. J. Sloan, F. Ranjard, Alain Bonissent, Emmerich Kneringer, S. L. Cartwright, I. Videau, A. M. Lutz, Ap Betteridge, Dirk Zerwas, Rp Johnson, A. Trabelsi, M. Thulasidas, Gerardo Ganis, Jiali Lin, A. Moutoussi, J. Steinberger, M. Jacquet, G. B. Taylor, P. Tempesta, M. Wunsch, C. Vannini, P. Henrard, Hg Moser, H. Wachsmuth, J. Lefrançois, Ja Perlas, W. Orejudos, Pa Mcnamara, T. Fearnley, C. Gotzhein, C. Boyer, Hg Sander, L. M. Mir, Eric Lancon, R. Xu, P. Colas, Pj Dornan, R. Boswell, Jm Nachtman, Mp Casado, Ciulli, Donato Creanza, John T Harvey, Franco Ligabue, Ig Knowles, B. Pietrzyk, Y. Saadi, Lorenzo Foà, P. Maley, G. Sanguinetti, M. Martinez, Ramon Miquel, E. B. Martin, Mg Green, Oj Hayes, L. Garrido, R. Fantechi, Claus Grupen, De Jaffe, G. Bujosa, Hasko Stenzel, E. Fernandez, Ao Bazarko, L. Passalacqua, Dominique Pallin, G. Parrini, Alessandro Giassi, Sj Dorris, Marco Cattaneo, I. Siotis, B. Jost, Giuseppe Iaselli, Rw Forty, Jie Zhang, Alberto Messineo, G. Hansper, Fabrizio Palla, F. Combley, S. Gonzalez, J. J. Veillet, K. Tittel, Georg Zobernig, G. Bencivenni, P. Mato, G. Lutters, O'Shea, G. Lutz, Ck Bowdery, P. Payre, Lei Zhang, M-N Minard, A. Koksal, B. Renk, Laurent Duflot, Roberto Dell'Orso, A. Wagner, Dm Binnie, Giovanna Selvaggi, F. Sanchez, Paolo Azzurri, S. Xue, Christian Bauer, Wm Newton, G. Lütjens, Imma Riu, J. Sommer, D. Decamp, Karl Jakobs, I. Giehl, Giuseppe Raso, G. Rudolph, G. Rizzo, S. Bettarini, D. Kuhn, Hansen, Giorgio Maggi, J. Schwindling, Mossadek Talby, Nancy Marinelli, K. Trabelsi, A. Ranieri, Andrea Sciabà, Dw Kim, Alberto Lusiani, A.E. Wright, W. Zhao, L. Curtis, Günther Dissertori, M. Fernandez-Bosman, Konrad Kleinknecht, T. Oest, Z. Y. Feng, J. Minguet-Rodriguez, F. Rivera, Buscher, S. Orteu, H.Y. Kim, A. Sadouki, P. Perret, A. Valassi, M. Davier, J. Boucrot, Patrick Janot, F. Foster, Jg Lynch, B. Marx, Robert Richter, B. Gobbo, A. Galla, R. Alemany, Jf Pusztaszeri, Bs Nilsson, Joseph Rothberg, F. Thomson, A. Höcker, Hubert Kroha, Aw Halley, Jm Rossignol, W. Männer, Am Litke, Jh Vonwimmerspergtoeller, Maria Agnese Ciocci, W. Tejessy, P. Teixeira-Dias, Philippe Odier, A. Pacheco, Jt Chambers, L. Smolik, M. Zheng, S. L. Wu, Jf Renardy, D.P.S. Ferguson, Pablo Rodriguez Perez, Duccio Abbaneo, A. Rougé, Elizabeth Locci, Fabio Cerutti, Alessia Tricomi, M. Rumpf, C. Goy, Ic Park, Maria Girone, L. Rolandi, Ilias Efthymiopoulos, C. Raine, D. Schlatter, Jordan Nash, J-C. Brient, Yang Gao, J.Y. Nief, G. Mannocchi, C. Guicheney, F Lediberder, Am Stacey, M.G. Schmidt, Christian Zeitnitz, L. Moneta, Pierluigi Campana, S. Monteil, A. Vayaki, A. Cordier, Joseph Proriol, F. Teubert, Ziad Ajaltouni, P. Comas, Caj Brew, Stefan Simion, G. Bonvicini, Pg Verdini, G. Giannini, C. Geweniger, M. Letho, H. Drevermann, G. R. Bonneaud, Manuel Delfino, R. Hagelberg, R Dellamarina, Armstrong, Kevin M. Smith, Guido Tonelli, M. Chmeissani, F. Stephan, Philippe Rosnet, F. Murtas, J. P. Lees, Lucia Silvestris, A. Roussarie, U. Becker, Chiarella, G. Bologna, Young-Il Choi, Ja Strong, P. Ghez, I. Ferrante, K. Zachariadou, R. Berlich, Ps Marrocchesi, Am Greene, H. Hu, Jm Scarr, P. Saraiva, A. Barres, H. Videau, Ma Giorgi, C. Markou, R. Beuselinck, C. Benchouk, Giuseppe Zito, M. Apollonio, P. Girtler, Rw Clifft, Peter Elmer, Ir Tomalin, P. Bourdon, F. Forti, Pr Norton, Jb Hansen, D. Rousseau, Alain Falvard, Ph Heusse, Jj Aubert, Arnaud Lucotte, S. Schael, A. Böhrer, Ettore Focardi, Jm Crespo, John Rander, M. Pepe-Altarelli, G. Calderini, Hepp, J.D. Hansen, C. Hoffmann, Salvatore Nuzzo, G. Batignani, Rm Turnbull, A. J. Finch, Jk Sedgbeer, J. Carr, G. Felici, Marie Helene Schune, F. Ruggieri, E. Rohne, Gp Murtas, M Depalma, Q. Ouyang, Tc Greening, G. Musolino, Francesco Ragusa, Roberto Tenchini, Stephen Haywood, S.N. Black, P. Colrain, T. R. Edgecock, G. Hughes, J-C. Montret, B. Rensch, A. Wäänänen, O. Schneider, Aristotelis Kyriakis, G. Graefe, C. Georgiopoulos, L. F. Thompson, X. Huang, As Thompson, Mi Williams, J. Grahl, Ma Mcneil, L. Bosisio, Paolo Laurelli, S. Wasserbaech, T. Medcalf, J. J. Walsh, S. Werner, Mi Parsons, Williams, M. Carpinelli, Nikolaos Konstantinidis, P. Rensing, J. Reeve, I.J. Scott, A. Pascual, F. Dydak, Yuehong Xie, W. Cameron, Hj Park, P. Perrodo, Giuseppe Bagliesi, Y. S. Gao, B. Vallage, B. Michel, Ga Blair, W. Kozanecki, R Stdenis, W. Blum, Am Walsh, Gy. Wolf, G. A. Cowan, G. Capon, A. Juste, Gunter Quast, M. Aleppo, Xin Wu, I Debonis, A. Gregorio, A. Minten, A. Rosado-Schlosser, Mario Maggi, G. Crawford, P. H. Hansen, D. Casper, B. Bloch-Devaux, P. Coyle, G. Gelao, S. Brandt, R. Settles, F. Etienne, Am Bencheikh, H. Seywerd, J. Knobloch, Anna Colaleo, P vanGemmeren, Andrea Venturi, F. Bossi, A. Putzer, I. Lehraus, Markus Frank, M. Corden, I. Nikolic, F. Podlyski, D. Buskulic, Jp Schuller, A. Antonelli, S. Emery, Cristinel Diaconu, Yb Pan, Paolo Spagnolo, Lm Bryant, C. Padilla, Werner Wiedenmann, O. Callot, E. Simopoulou, David Calvet, S. Thorn, P. Reeves, M. Schmelling, Botterill, C. Bozzi, Jc Thompson, Ting Wang, J-F Grivaz, E-E Kluge, Laboratoire d'Annecy de Physique des Particules (LAPP), Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry])-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Physique Corpusculaire - Clermont-Ferrand (LPC), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Leprince-Ringuet (LLR), Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-École polytechnique (X)-Centre National de la Recherche Scientifique (CNRS), Centre de Physique des Particules de Marseille (CPPM), Aix Marseille Université (AMU)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de l'Accélérateur Linéaire (LAL), Université Paris-Sud - Paris 11 (UP11)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), ALEPH, Centre National de la Recherche Scientifique (CNRS)-École polytechnique (X)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3), Centre National de la Recherche Scientifique (CNRS)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Université Paris-Sud - Paris 11 (UP11), Buskulic, D, Debonis, I, Decamp, D, Ghez, P, Goy, C, Lees, J, Lucotte, A, Minard, M, Nief, J, Odier, P, Pietrzyk, B, Casado, M, Chmeissani, M, Crespo, J, Delfino, M, Efthymiopoulos, I, Fernandez, E, Fernandezbosman, M, Garrido, L, Juste, A, Martinez, M, Orteu, S, Padilla, C, Park, I, Pascual, A, Perlas, J, Riu, I, Sanchez, F, Teubert, F, Colaleo, A, Creanza, D, Depalma, M, Gelao, G, Girone, M, Iaselli, G, Maggi, G, Maggi, M, Marinelli, N, Nuzzo, S, Ranieri, A, Raso, G, Ruggieri, F, Selvaggi, G, Silvestris, L, Tempesta, P, Tricomi, A, Zito, G, Huang, X, Lin, J, Ouyang, Q, Wang, T, Xie, Y, Xu, R, Xue, S, Zhang, J, Zhang, L, Zhao, W, Alemany, R, Bazarko, A, Bonvicini, G, Brightthomas, P, Cattaneo, M, Comas, P, Coyle, P, Drevermann, H, Forty, R, Frank, M, Hagelberg, R, Harvey, J, Janot, P, Jost, B, Kneringer, E, Knobloch, J, Lehraus, I, Lutters, G, Martin, E, Mato, P, Minten, A, Miquel, R, Mir, L, Moneta, L, Oest, T, Pacheco, A, Pusztaszeri, J, Ranjard, F, Rensing, P, Rizzo, G, Rolandi, L, Schlatter, D, Schmelling, M, Schmitt, M, Schneider, O, Tejessy, W, Tomalin, I, Venturi, A, Wachsmuth, H, Wagner, A, Ajaltouni, Z, Barres, A, Boyer, C, Falvard, A, Gay, P, Guicheney, C, Henrard, P, Jousset, J, Michel, B, Monteil, S, Montret, J, Pallin, D, Perret, P, Podlyski, F, Proriol, J, Rosnet, P, Rossignol, J, Fearnley, T, Hansen, J, Hansen, P, Nilsson, B, Rensch, B, Waananen, A, Kyriakis, A, Markou, C, Simopoulou, E, Siotis, I, Vayaki, A, Zachariadou, K, Blondel, A, Bonneaud, G, Brient, J, Bourdon, P, Rouge, A, Rumpf, M, Valassi, A, Verderi, M, Videau, H, Candlin, D, Parsons, M, Focardi, E, Parrini, G, Corden, M, Georgiopoulos, C, Jaffe, D, Antonelli, A, Bencivenni, G, Bologna, G, Bossi, F, Campana, P, Capon, G, Casper, D, Chiarella, V, Felici, G, Laurelli, P, Mannocchi, G, Murtas, F, Murtas, G, Passalacqua, L, Pepealtarelli, M, Curtis, L, Dorris, S, Halley, A, Knowles, I, Lynch, J, Oshea, V, Raine, C, Reeves, P, Scarr, J, Smith, K, Teixeiradias, P, Thompson, A, Thomson, F, Thorn, S, Turnbull, R, Becker, U, Geweniger, C, Graefe, G, Hanke, P, Hansper, G, Hepp, V, Kluge, E, Putzer, A, Schmidt, M, Sommer, J, Stenzel, H, Tittel, K, Werner, S, Wunsch, M, Abbaneo, D, Beuselinck, R, Binnie, D, Cameron, W, Dornan, P, Moutoussi, A, Nash, J, Sedgbeer, J, Stacey, A, Williams, M, Dissertori, G, Girtler, P, Kuhn, D, Rudolph, G, Betteridge, A, Bowdery, C, Colrain, P, Crawford, G, Finch, A, Foster, F, Hughes, G, Sloan, T, Galla, A, Giehl, I, Greene, A, Hoffmann, C, Jakobs, K, Kleinknecht, K, Quast, G, Renk, B, Rohne, E, Sander, H, Vangemmeren, P, Zeitnitz, C, Aubert, J, Bencheikh, A, Benchouk, C, Bonissent, A, Bujosa, G, Calvet, D, Carr, J, Diaconu, C, Etienne, F, Konstantinidis, N, Payre, P, Rousseau, D, Talby, M, Sadouki, A, Thulasidas, M, Trabelsi, K, Aleppo, M, Ragusa, F, Bauer, C, Berlich, R, Blum, W, Buscher, V, Dietl, H, Dydak, F, Ganis, G, Gotzhein, C, Kroha, H, Lutjens, G, Lutz, G, Manner, W, Moser, H, Richter, R, Rosadoschlosser, A, Schael, S, Settles, R, Seywerd, H, Stdenis, R, Wiedenmann, W, Wolf, G, Boucrot, J, Callot, O, Choi, Y, Cordier, A, Davier, M, Duflot, L, Grivaz, J, Heusse, P, Hocker, A, Jacholkowska, A, Jacquet, M, Kim, D, Lediberder, F, Lefrancois, J, Lutz, A, Nikolic, I, Park, H, Schune, M, Simion, S, Veillet, J, Videau, I, Zerwas, D, Azzurri, P, Bagliesi, G, Batignani, G, Bettarini, S, Bozzi, C, Calderini, G, Carpinelli, M, Ciocci, M, Ciulli, V, Dellorso, R, Fantechi, R, Ferrante, I, Foa, L, Forti, F, Giassi, A, Giorgi, M, Gregorio, A, Ligabue, F, Lusiani, A, Marrocchesi, P, Messineo, A, Palla, F, Sanguinetti, G, Sciaba, A, Spagnolo, P, Steinberger, J, Tenchini, R, Tonelli, G, Vannini, C, Verdini, P, Walsh, J, Blair, G, Bryant, L, Cerutti, F, Chambers, J, Gao, Y, Green, M, Medcalf, T, Perrodo, P, Strong, J, Vonwimmerspergtoeller, J, Botterill, D, Clifft, R, Edgecock, T, Haywood, S, Maley, P, Norton, P, Thompson, J, Wright, A, Blochdevaux, B, Colas, P, Emery, S, Kozanecki, W, Lancon, E, Lemaire, M, Locci, E, Marx, B, Perez, P, Rander, J, Renardy, J, Roussarie, A, Schuller, J, Schwindling, J, Trabelsi, A, Vallage, B, Black, S, Dann, J, Johnson, R, Kim, H, Litke, A, Mcneil, M, Taylor, G, Booth, C, Boswell, R, Brew, C, Cartwright, S, Combley, F, Koksal, A, Letho, M, Newton, W, Reeve, J, Thompson, L, Bohrer, A, Brandt, S, Cowan, G, Grupen, C, Minguetrodriguez, J, Rivera, F, Saraiva, P, Smolik, L, Stephan, F, Apollonio, M, Bosisio, L, Dellamarina, R, Giannini, G, Gobbo, B, Musolino, G, Rothberg, J, Wasserbaech, S, Armstrong, S, Elmer, P, Feng, Z, Ferguson, D, Gonzalez, S, Grahl, J, Greening, T, Hayes, O, Hu, H, Mcnamara, P, Nachtman, J, Orejudos, W, Pan, Y, Saadi, Y, Scott, I, Walsh, A, Wu, S, Wu, X, Yamartino, J, Zheng, M, Zobernig, G, Lees, Jp, Minard, Mn, Nief, Jy, Casado, Mp, Crespo, Jm, Park, Ic, Perlas, Ja, Bazarko, Ao, Forty, Rw, Martin, Eb, Mir, Lm, Pusztaszeri, Jf, Rolandi, Luigi, Tomalin, Ir, Montret, Jc, Rossignol, Jm, Hansen, Jb, Hansen, Jd, Hansen, Jr, Hansen, Ph, Brient, Jc, Candlin, Dj, Parsons, Mi, Jaffe, De, Murtas, Gp, Dorris, Sj, Halley, Aw, Knowles, Ig, Lynch, Jg, Scarr, Jm, Turnbull, Rm, Kluge, Ee, Binnie, Dm, Dornan, Pj, Sedgbeer, Jk, Stacey, Am, Williams, Md, Betteridge, Ap, Bowdery, Ck, Finch, Aj, Williams, Mi, Greene, Am, Sander, Hg, Aubert, Jj, Bencheikh, Am, Moser, Hg, Grivaz, Jf, Kim, Dw, Lutz, Am, Park, Hj, Schune, Mh, Veillet, Jj, Ciocci, Ma, Giorgi, Ma, Ligabue, Franco, Lusiani, Alberto, Verdini, Pg, Blair, Ga, Bryant, Lm, Chambers, Jt, Green, Mg, Strong, Ja, Vonwimmerspergtoeller, Jh, Botterill, Dr, Clifft, Rw, Edgecock, Tr, Norton, Pr, Thompson, Jc, Wright, Ae, Lemaire, Mc, Renardy, Jf, Schuller, Jp, Black, Sn, Dann, Jh, Johnson, Rp, Kim, Hy, Litke, Am, Mcneil, Ma, Booth, Cn, Brew, Caj, Newton, Wm, Thompson, Lf, Armstrong, Sr, Ferguson, Dp, Greening, Tc, Hayes, Oj, Mcnamara, Pa, Nachtman, Jm, Pan, Yb, Scott, Ij, Walsh, Am, Wu, Sl, Yamartino, Jm, and Zobernig, G.
Subjects: Physics, Aleph, Particle physics, Physics and Astronomy (miscellaneous), 010308 nuclear & particles physics, Electron–positron annihilation, Detector, Monte Carlo method, Hadron, Parton, 01 natural sciences, Nuclear physics, 0103 physical sciences, [PHYS.HEXP]Physics [physics]/High Energy Physics - Experiment [hep-ex], High Energy Physics::Experiment, Nuclear Experiment, 010306 general physics, Parton shower, Particle Physics - Experiment, Event reconstruction
Abstract: Using data obtained with the ALEPH detector at the Z resonance, a measure based on transverse momentum is shown to exhibit a correlation between the two halves of a hadronic event which cannot be explained by energy-momentum conservation, flavour conservation, the imposition of an event axis or imperfect event reconstruction. Two possible interpretations based on existing Monte Carlo models are examined: a) ARIADNE, with the correlation forming early in the parton shower and with the transition from partons to hadrons playing only a minor part; b) JETSET, with the correlation forming at the fragmentation stage. A correlation technique based on a jet cluster analysis is used to make a comparison of the models with the data. It is concluded that both non-perturbative and perturbative effects make important contributions to the observed correlation. RI ANTONELLI, ANTONELLA/C-6238-2011; Passalacqua, Luca/F-5127-2011; Murtas, Fabrizio/B-5729-2012; St.Denis, Richard/C-8997-2012; Sanchez, Federico/F-5809-2012; Forti, Francesco/H-3035-2011; Ferrante, Isidoro/F-1017-2012
Published: 1997
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2. The topology dependence of charged particle multiplicities in three-jet events

Author: W Tejessy, P. Tempesta, L Duflot, Guido Tonelli, C Diaconu, A Kyriakis, Mp Casado, G Bologna, G Rizzo, Ps Marrocchesi, Hepp, Dm Binnie, U Becker, G. Batignani, Patrick Janot, A. Galla, J Knobloch, E Fernandez, C Vannini, G. Daskalakis, M. Fernandez-Bosman, J Reeve, M Corden, B. Bloch-Devaux, A. Valassi, S Ganzalez, J Proriol, D. J. Candlin, Hg Moser, C Raine, G Ganis, H Wachsmuth, Donato Creanza, A Falvard, M Talby, J.Y. Nief, P. Spagnolo, S Simion, Am Lutz, R Dellamarina, D Buskulic, P Azzurri, Jm Crespo, S Brandt, J Boucrot, M Rumpf, Si Chen, Ja Perlas, Q Ouyang, S Monteil, A Bonissent, G. Rudolph, G Quast, P. Laurelli, P Perret, Lorenzo Foà, D Kuhn, K Zachariadou, R Xu, A Minten, J. Grahl, G Bujosa, K Tittel, T Fearnley, F. Sanchez, A. Rosado-Schlosser, Jk Sedgbeer, M Cattaneo, M Depalma, S Haywood, Giovanna Selvaggi, G Calderini, G Crawford, Young-Il Choi, S. Emery, J-F Grivaz, E-E Kluge, Yb Pan, A Rouge, Ga Blair, F. Ruggieri, S Werner, A Sadouki, Ao Bazarko, S.N. Black, R Richter, L. Passalacqua, J-C. Montret, J Carr, P Colrain, E Locci, G. Bencivenni, P vanGemmeren, O Leroy, G Gelao, B Gobbo, J Lin, P Saraiva, P. Bright-Thomas, P Girtler, Pg Verdini, W Manner, P Colas, A. Tricomi, Claudine Boyer, S. Goodsir, Ciulli, R Miquel, Ck Bowdery, B Michel, L Curtis, G. Hansper, P. Campana, B. Rensch, P. H. Hansen, W Zhao, F. Murtas, H Seywerd, K. Trabelsi, R. Berlich, F Stephan, David Calvet, F. Bossi, H Hu, A Ranieri, O'Shea, G Parrini, P. Teixeira-Dias, G Graefe, R Settles, M. Aleppo, P. Rensing, W. Kozanecki, Lm Bryant, J Harvey, I. Giehl, M. Schmelling, P Maley, L Smolik, W Orejudos, P Rosnet, C Padilla, Am Greene, O. Callot, A Gregorio, P Heusse, J Zhang, S Nuzzo, R Beuselinck, G Taylor, Wm Newton, K Kleinknecht, Y Saadi, Evelyn Thomson, D Zerwas, P. Comas, Mg Green, Kelly, D. Casper, M Thulasidas, M Frank, J Rothberg, F. Etienne, D Rousseau, A. Blondel, Botterill, L. F. Thompson, F. Forti, E Focardi, A.E. Wright, S. L. Wu, A Pascual, R Tenchini, G Hughes, Mi Williams, C. N. Booth, S Xue, A. Antonelli, D Schlatter, Dps Ferguson, Jh Vonwimmerspergtoeller, A. Trabelsi, Eb Martin, I Videau, M. Pepe-Altarelli, De Jaffe, M Martinez, Mi Parsons, Y. S. Gao, A. Wagner, C Goy, R Hagelberg, D Decamp, O. Buchmüller, Philippe Odier, C. Bozzi, G Dissertori, G. Zobernig, F. Ligabue, C Georgiopoulos, A. Jacholkowska, J Steinberger, R Alemany, E. Lancon, R Stdenis, B. Vallage, P Ghez, Hj Park, L Moneta, Ig Knowles, A. Lusiani, S Bettarini, Jj Veillet, A Putzer, J.D. Hansen, M. Carpinelli, Buscher, S. L. Cartwright, C Gotzhein, J Sommer, S. Orteu, Z. Y. Feng, M Girone, Oj Hayes, A Giassi, F Foster, H Videau, Rm Turnbull, Jg Lynch, Rp Johnson, L Zhang, A Roussarie, Mc Lemaire, J.H. Dann, J. P. Lees, F Cerutti, H Kroha, Chiarella, J Lefrancois, Jc Thompson, F Lediberder, Sj Dorris, C. Grupen, Mario Maggi, N Konstantinidis, Arnaud Lucotte, O Schneider, M Delfino, G. Felici, G. Zito, L Garrido, Rw Forty, R. Barate, T Sloan, D. Pallin, Yang Gao, P Perrodo, C Zeitnitz, Gp Murtas, L. M. Mir, K Smith, Am Litke, R Fantechi, G Wolf, Ic Park, X Huang, L Bosisio, T Medcalf, B Renk, Jm Rossignol, C. Guicheney, Hg Sander, I Nikolic, C. Ferdi, A Moutoussi, Maria Agnese Ciocci, C Geweniger, Jp Schuller, Aw Halley, A Messineo, B Jost, Pj Dornan, I. Siotis, E Kneringer, P Coyle, M.G. Schmidt, Giuseppe Iaselli, M. N. Minard, X Wu, L. Rolandi, W Cameron, A. Böhrer, I Riu, Jf Pusztaszeri, Bs Nilsson, S Schael, T. R. Edgecock, Jm Nachtman, Ap Betteridge, I.J. Scott, Jt Chambers, E Rohne, J Jousset, M. Zheng, Am Stacey, G Lutjens, I Lehraus, H. Y. Kim, A Sciaba, G Musolino, M. H. Schune, A Colaleo, A. J. Finch, Armstrong, A. Vayaki, J. J. Aubert, M. Chmeissani, F Palla, M. Verderi, Jm Yamartino, Jf Renardy, M. Apollonio, P Hanke, C. Hoffmann, J Rander, C. Markou, G. Mannocchi, J-C. Brient, Pa Mcnamara, J. Schwindling, G Giannini, Rw Clifft, Ir Tomalin, Tc Greening, P. Bourdon, H Stenzel, Ziad Ajaltouni, G Bagliesi, F. Thomson, G Cowan, I Ferrante, P Perez, Caj Brew, A Barres, H Dietl, K Jakobs, G. Capon, H Drevermann, As Thompson, M Jacquet, Ma Mcneil, T Wang, Hansen, P Payre, Giorgio Maggi, Lucia Silvestris, Williams, E Simopoulou, M Davier, Jm Scarr, F Ranjard, G Lutz, Dw Kim, M Schmitt, F. Dydak, Ja Strong, R DellOrso, B Pietrzyk, P Mato, F Teubert, R Boswell, A Cordier, Ma Giorgi, W Blum, J Walsh, A Venturi, A Hocker, F Combley, A. Wäänänen, A Pacheco, G. Raso, S Wasserbaech, G Sanguinetti, N. Marinelli, Pr Norton, Jb Hansen, Y Xie, M Wunsch, F Ragusa, G. R. Bonneaud, M H. Lehto, A Juste, C Benchouk, G Lutters, F Podlyski, P Elmer, W Wiedenmann, D Abbaneo, Jordan Nash, P Henrard, Barate, R, Buskulic, D, Decamp, D, Ghez, P, Goy, C, Lees, Jp, Lucotte, A, Minard, Mn, Nief, Jy, Odier, P, Pietrzyk, B, Casado, Mp, Chmeissani, M, Comas, P, Crespo, Jm, Delfino, M, Fernandez, E, Fernandezbosman, M, Garrido, L, Juste, A, Martinez, M, Miquel, R, Mir, Lm, Orteu, S, Padilla, C, Park, Ic, Pascual, A, Perlas, Ja, Riu, I, Sanchez, F, Teubert, F, Colaleo, A, Creanza, D, Depalma, M, Gelao, G, Iaselli, G, Maggi, G, Maggi, M, Marinelli, N, Nuzzo, S, Ranieri, A, Raso, G, Ruggieri, F, Selvaggi, G, Silvestris, L, Tempesta, P, Tricomi, A, Zito, G, Huang, X, Lin, J, Ouyang, Q, Wang, T, Xie, Y, Xu, R, Xue, S, Zhang, J, Zhang, L, Zhao, W, Abbaneo, D, Alemany, R, Bazarko, Ao, Brightthomas, P, Cattaneo, M, Cerutti, F, Drevermann, H, Forty, Rw, Frank, M, Hagelberg, R, Harvey, J, Janot, P, Jost, B, Kneringer, E, Knobloch, J, Lehraus, I, Lutters, G, Mato, P, Minten, A, Moneta, L, Pacheco, A, Pusztaszeri, Jf, Ranjard, F, Rensing, P, Rizzo, G, Rolandi, Luigi, Schlatter, D, Schmelling, M, Schmitt, M, Schneider, O, Tejessy, W, Tomalin, Ir, Wachsmuth, H, Wagner, A, Ajaltouni, Z, Barres, A, Boyer, C, Falvard, A, Ferdi, C, Gay, P, Guicheney, C, Henrard, P, Jousset, J, Michel, B, Monteil, S, Montret, Jc, Pallin, D, Perret, P, Podlyski, F, Proriol, J, Rosnet, P, Rossignol, Jm, Fearnley, T, Hansen, Jb, Hansen, Jd, Hansen, Jr, Hansen, Ph, Nilsson, B, Rensch, B, Waananen, A, Daskalakis, G, Kyriakis, A, Markou, C, Simopoulou, E, Siotis, I, Vayaki, A, Zachariadou, K, Blondel, A, Bonneaud, G, Brient, Jc, Bourdon, P, Rouge, A, Rumpf, M, Valassi, A, Verderi, M, Videau, H, Candlin, Dj, Parsons, Mi, Focardi, E, Parrini, G, Corden, M, Georgiopoulos, C, Jaffe, De, Antonelli, A, Bencivenni, G, Bologna, G, Bossi, F, Campana, P, Capon, G, Casper, D, Chiarella, V, Felici, G, Laurelli, P, Mannocchi, G, Murtas, F, Murtas, Gp, Passalacqua, L, Pepealtarelli, M, Curtis, L, Dorris, Sj, Halley, Aw, Knowles, Ig, Lynch, Jg, Oshea, V, Raine, C, Scarr, Jm, Smith, K, Teixeiradias, P, Thompson, A, Thomson, E, Thomson, F, Turnbull, Rm, Becker, U, Buchmuller, O, Geweniger, C, Graefe, G, Hanke, P, Hansper, G, Hepp, V, Kluge, Ee, Putzer, A, Schmidt, M, Sommer, J, Stenzel, H, Tittel, K, Werner, S, Wunsch, M, Beuselinck, R, Binnie, Dm, Cameron, W, Dornan, Pj, Girone, M, Goodsir, S, Martin, Eb, Moutoussi, A, Nash, J, Sedgbeer, Jk, Stacey, Am, Williams, Md, Dissertori, G, Girtler, P, Kuhn, D, Rudolph, G, Betteridge, Ap, Bowdery, Ck, Colrain, P, Crawford, G, Finch, Aj, Foster, F, Hughes, G, Sloan, T, Williams, Mi, Galla, A, Giehl, I, Greene, Am, Hoffmann, C, Jakobs, K, Kleinknecht, K, Quast, G, Renk, B, Rohne, E, Sander, Hg, Vangemmeren, P, Zeitnitz, C, Aubert, Jj, Benchouk, C, Bonissent, A, Bujosa, G, Calvet, D, Carr, J, Coyle, P, Diaconu, C, Etienne, F, Konstantinidis, N, Leroy, O, Payre, P, Rousseau, D, Talby, M, Sadouki, A, Thulasidas, M, Trabelsi, K, Aleppo, M, Ragusa, F, Berlich, R, Blum, W, Buscher, V, Dietl, H, Dydak, F, Ganis, G, Gotzhein, C, Kroha, H, Lutjens, G, Lutz, G, Manner, W, Moser, Hg, Richter, R, Rosadoschlosser, A, Schael, S, Settles, R, Seywerd, H, Stdenis, R, Wiedenmann, W, Wolf, G, Boucrot, J, Callot, O, Chen, S, Choi, Y, Cordier, A, Davier, M, Duflot, L, Grivaz, Jf, Heusse, P, Hocker, A, Jacholkowska, A, Jacquet, M, Kim, Dw, Lediberder, F, Lefrancois, J, Lutz, Am, Nikolic, I, Park, Hj, Schune, Mh, Simion, S, Veillet, Jj, Videau, I, Zerwas, D, Azzurri, P, Bagliesi, G, Batignani, G, Bettarini, S, Bozzi, C, Calderini, G, Carpinelli, M, Ciocci, Ma, Ciulli, V, Dellorso, R, Fantechi, R, Ferrante, I, Foa, L, Forti, F, Giassi, A, Giorgi, Ma, Gregorio, A, Ligabue, Franco, Lusiani, Alberto, Marrocchesi, P, Messineo, A, Palla, F, Sanguinetti, G, Sciaba, A, Spagnolo, P, Steinberger, J, Tenchini, R, Tonelli, G, Vannini, C, Venturi, A, Verdini, Pg, Blair, Ga, Bryant, Lm, Chambers, Jt, Gao, Y, Green, Mg, Medcalf, T, Perrodo, P, Strong, Ja, Vonwimmerspergtoeller, Jh, Botterill, Dr, Clifft, Rw, Edgecock, Tr, Haywood, S, Maley, P, Norton, Pr, Thompson, Jc, Wright, Ae, Blochdevaux, B, Colas, P, Emery, S, Kozanecki, W, Lancon, E, Lemaire, Mc, Locci, E, Perez, P, Rander, J, Renardy, Jf, Roussarie, A, Schuller, Jp, Schwindling, J, Trabelsi, A, Vallage, B, Black, Sn, Dann, Jh, Johnson, Rp, Kim, Hy, Litke, Am, Mcneil, Ma, Taylor, G, Booth, Cn, Boswell, R, Brew, Caj, Cartwright, S, Combley, F, Kelly, M, Lehto, M, Newton, Wm, Reeve, J, Thompson, Lf, Bohrer, A, Brandt, S, Cowan, G, Grupen, C, Saraiva, P, Smolik, L, Stephan, F, Apollonio, M, Bosisio, L, Dellamarina, R, Giannini, G, Gobbo, B, Musolino, G, Rothberg, J, Wasserbaech, S, Armstrong, Sr, Elmer, P, Feng, Z, Ferguson, Dp, Ganzalez, S, Grahl, J, Greening, Tc, Hayes, Oj, Hu, H, Mcnamara, Pa, Nachtman, Jm, Orejudos, W, Pan, Yb, Saadi, Y, Scott, Ij, Walsh, J, Wu, Sl, Wu, X, Yamartino, Jm, Zheng, M, Zobernig, G., Laboratoire d'Annecy de Physique des Particules (LAPP), Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry])-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Physique Corpusculaire - Clermont-Ferrand (LPC), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Leprince-Ringuet (LLR), Centre National de la Recherche Scientifique (CNRS)-École polytechnique (X)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3), Centre de Physique des Particules de Marseille (CPPM), Aix Marseille Université (AMU)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de l'Accélérateur Linéaire (LAL), Centre National de la Recherche Scientifique (CNRS)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Université Paris-Sud - Paris 11 (UP11), ALEPH, Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-École polytechnique (X)-Centre National de la Recherche Scientifique (CNRS), Université Paris-Sud - Paris 11 (UP11)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Lees, J, Minard, M, Nief, J, Casado, M, Crespo, J, Mir, L, Park, I, Perlas, J, Bazarko, A, Forty, R, Pusztaszeri, J, Rolandi, L, Tomalin, I, Montret, J, Rossignol, J, Hansen, J, Hansen, P, Brient, J, Candlin, D, Parsons, M, Jaffe, D, Murtas, G, Dorris, S, Halley, A, Knowles, I, Lynch, J, Scarr, J, Turnbull, R, Kluge, E, Binnie, D, Dornan, P, Martin, E, Sedgbeer, J, Stacey, A, Williams, M, Betteridge, A, Bowdery, C, Finch, A, Greene, A, Sander, H, Aubert, J, Moser, H, Grivaz, J, Kim, D, Lutz, A, Park, H, Schune, M, Veillet, J, Ciocci, M, Giorgi, M, Ligabue, F, Lusiani, A, Verdini, P, Blair, G, Bryant, L, Chambers, J, Green, M, Strong, J, Vonwimmerspergtoeller, J, Botterill, D, Clifft, R, Edgecock, T, Norton, P, Thompson, J, Wright, A, Lemaire, M, Renardy, J, Schuller, J, Black, S, Dann, J, Johnson, R, Kim, H, Litke, A, Mcneil, M, Booth, C, Brew, C, Newton, W, Thompson, L, Armstrong, S, Ferguson, D, Greening, T, Hayes, O, Mcnamara, P, Nachtman, J, Pan, Y, Scott, I, Wu, S, Yamartino, J, and Zobernig, G
Subjects: Physics, Jet (fluid), Physics and Astronomy (miscellaneous), 010308 nuclear & particles physics, Astrophysics::High Energy Astrophysical Phenomena, Electron–positron annihilation, 01 natural sciences, Charged particle, Nuclear physics, 0103 physical sciences, Transverse momentum, [PHYS.HEXP]Physics [physics]/High Energy Physics - Experiment [hep-ex], High Energy Physics::Experiment, 010306 general physics, Particle Physics - Experiment, Topology (chemistry)
Abstract: A study of individual jet and whole-event charged particle multiplicities in three-jet events measured in e(+)e(-) annihilation at the Z reveals a significant topology dependence. Mean jet multiplicities are inadequately described by jet energies; interjet angles must also be specified. Quantitative tests suggest that it is necessary to use transverse-momentum-like scales to describe the data. RI ANTONELLI, ANTONELLA/C-6238-2011; Passalacqua, Luca/F-5127-2011; Murtas, Fabrizio/B-5729-2012; St.Denis, Richard/C-8997-2012; Sanchez, Federico/F-5809-2012; Forti, Francesco/H-3035-2011; Ferrante, Isidoro/F-1017-2012

3. Inclusive production of neutral pions in hadronic Z decays

Author: A. Ranieri, H. Hu, D. Schlatter, A. Rougé, P. Colas, C. Geweniger, J-C. Brient, S. Schael, G. Sanguinetti, M. Martinez, Ramon Miquel, G. Bujosa, Rm Turnbull, R Dellamarina, Ziad Ajaltouni, G. Felici, Philippe Rosnet, Gp Murtas, J. Reeve, I.J. Scott, Lei Zhang, S. J. Chen, A. Pascual, M-N Minard, B. Renk, O. Callot, H. Seywerd, Roberto Dell'Orso, Stefan Simion, Alain Falvard, J.Y. Nief, Manuel Delfino, E. Simopoulou, David Calvet, M. Schmelling, R. Hagelberg, P. Henrard, Olivier Leroy, Botterill, G. Lütjens, Imma Riu, G. Capon, Kevin M. Smith, Guido Tonelli, F. Stephan, Aw Halley, Paul Hanke, Ao Brightthomas, X. Huang, J. Sommer, J. Boucrot, Pablo Rodriguez Perez, F. Bossi, J. Knobloch, G. Mannocchi, Lucia Silvestris, U. Becker, D. Decamp, Jm Scarr, P. Saraiva, A. Putzer, Dm Binnie, Anna Colaleo, J.D. Hansen, G. R. Bonneaud, Paolo Laurelli, D. Rousseau, A. Jacholkowska, C. N. Booth, R. Xu, A. Roussarie, P. Ghez, Alessia Tricomi, Ja Strong, Ting Wang, F Lediberder, Maria Girone, S. Wasserbaech, S. Werner, J-F Grivaz, E-E Kluge, Q. Ouyang, W. Kozanecki, Giovanna Selvaggi, Jf Pusztaszeri, Bs Nilsson, Am Stacey, D.P.S. Ferguson, O. Schneider, C. Bozzi, Franco Ligabue, Hj Park, J. Jousset, Michael Schmitt, Young-Il Choi, F. Podlyski, D. Buskulic, S. Emery, Christian Zeitnitz, Cristinel Diaconu, Yb Pan, Ph. Heusse, T. R. Edgecock, F. Combley, E. Fernandez, Eric Lancon, Am Lutz, P. Girtler, B. Michel, Ga Blair, M. Apollonio, Mg Green, Kelly, A. Sciabà, A. Juste, Jc Thompson, D. Kuhn, Gunter Quast, L. Bosisio, Patrick Janot, A. Galla, Peter Elmer, Ic Park, De Jaffe, A. Vayaki, S. Bettarini, Giuseppe Zito, Marco Cattaneo, I. Videau, J. Schwindling, Mc Lemaire, J.H. Dann, B. Bloch-Devaux, F. Ruggieri, Ettore Focardi, Jm Crespo, John Rander, Gy. Wolf, Wm Newton, Pr Norton, M. Thulasidas, E. Rohne, G. A. Cowan, Ciulli, Jk Sedgbeer, G. Musolino, Ma Giorgi, C. Markou, Joseph Rothberg, Jb Hansen, S. Brandt, H. Drevermann, R. Settles, P. Perret, Xin Wu, O'Shea, M Depalma, F. Thomson, A. Hocker, T. J. Sloan, J-J. Aubert, C. Raine, A. Valassi, F. Etienne, Francesco Ragusa, Roberto Tenchini, Georg Zobernig, S. Monteil, J. P. Lees, Chiarella, W. Männer, Am Litke, C. Goy, Gerardo Ganis, A. Barres, I. Nikolic, G. Lutz, B. Rensch, F. Sanchez, C. Hoffmann, Karl Jakobs, B. Pietrzyk, Hubert Kroha, F. Cerutti, I. Giehl, Jg Lynch, Ps Marrocchesi, S.N. Black, A.E. Wright, Yang Gao, G. Graefe, C. Georgiopoulos, A. Blondel, W. Zhao, G. Bologna, M. Davier, L. F. Thompson, M. Rumpf, K. Zachariadou, R. Beuselinck, G. B. Taylor, P. Tempesta, Claus Grupen, M. Pepe-Altarelli, Hepp, J-C. Montret, M. Verderi, A. Trabelsi, Mi Williams, R. Barate, A. Böhrer, C. Guicheney, Caj Brew, Hg Moser, H. Wachsmuth, J. J. Walsh, Jm Yamartino, J. Carr, Ma Mcneil, R. Berlich, Mi Parsons, T. Medcalf, M. Aleppo, H Schune, F. Ranjard, J. Steinberger, F. Dydak, Pj Dornan, C. Vannini, Jie Zhang, Tc Greening, Emmerich Kneringer, W. Cameron, Williams, G. Calderini, G. Giannini, M. Letho, Aristotelis Kyriakis, Hansen, C. Padilla, Y. Saadi, Jordan Nash, P. Mato, G. Lutters, T. Fearnley, H. Videau, As Thompson, G. Hansper, Ja Perlas, W. Orejudos, Eb Martin, A. Moutoussi, Donato Creanza, L. Moneta, M. Jacquet, John T Harvey, Werner Wiedenmann, J. Lefrançois, M. Carpinelli, A. Gregorio, S. Gonzalez, A. Lusiani, K. Tittel, Konrad Kleinknecht, S. Xue, Alessandro Giassi, Stephen Haywood, A. Wäänänen, Paolo Azzurri, D. Casper, H. Dietl, A. Rosado-Schlosser, Günther Dissertori, Mario Maggi, Hg Sander, Mossadek Talby, Giuseppe Raso, R. Boswell, L. Curtis, P. Comas, F. Foster, G. Rudolph, C. Benchouk, G. Maggi, Alain Bonissent, M. Fernandez-Bosman, Buscher, S. L. Cartwright, S. Orteu, Jm Rossignol, A. Sadouki, S. L. Wu, A. Pacheco, Jt Chambers, I. Ferrante, T. Oest, Z. Y. Feng, Salvatore Nuzzo, G. Batignani, L. Smolik, M. Zheng, P. Coyle, B. Vallage, J. Minguet-Rodriguez, Dirk Zerwas, R. Alemany, Arnaud Lucotte, Dw Kim, Nancy Marinelli, K. Trabelsi, P. Colrain, F. Rivera, Rp Johnson, G. Hughes, W. Tejessy, L. Rolandi, Jm Nachtman, G. Gelao, Jiali Lin, M.G. Schmidt, Joseph Proriol, F. Teubert, N Kontantinidis, C. Gotzhein, C. Boyer, M. Wunsch, A. Minten, L. M. Mir, G. Rizzo, A. J. Finch, I. Siotis, Lorenzo Foà, P. Maley, G. Crawford, P. H. Hansen, Giuseppe Iaselli, Maria Agnese Ciocci, L. Garrido, R. Fantechi, P. Teixeira-Dias, Ao Bazarko, L. Passalacqua, P. Rensing, Dominique Pallin, B. Jost, Pa Mcnamara, Jf Renardy, Ck Bowdery, Alberto Messineo, Evelyn Thomson, Y. S. Gao, R Stdenis, A. Wagner, H.Y. Kim, W. Blum, Jh Vonwimmerspergtoeller, Philippe Odier, Pierluigi Campana, Pg Verdini, F. Murtas, Am Greene, F. Forti, Robert Richter, B. Gobbo, Duccio Abbaneo, Elizabeth Locci, D. J. Candlin, Ig Knowles, Fabrizio Palla, Oj Hayes, Hasko Stenzel, G. Parrini, Sj Dorris, Rw Forty, P. Payre, L. Duflot, Paolo Spagnolo, Lm Bryant, A. Cordier, Ap Betteridge, I. Lehraus, Jj Veillet, Markus Frank, M. Corden, Jp Schuller, A. Antonelli, P vanGemmeren, Andrea Venturi, Mp Casado, G. Bencivenni, J. Grahl, Yuehong Xie, P. Perrodo, Giuseppe Bagliesi, Armstrong, M. Chmeissani, Georgios Daskalakis, Rw Clifft, Ir Tomalin, P. Bourdon, Laboratoire d'Annecy de Physique des Particules (LAPP), Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry])-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Physique Corpusculaire - Clermont-Ferrand (LPC), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Leprince-Ringuet (LLR), Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-École polytechnique (X)-Centre National de la Recherche Scientifique (CNRS), Centre de Physique des Particules de Marseille (CPPM), Aix Marseille Université (AMU)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de l'Accélérateur Linéaire (LAL), Université Paris-Sud - Paris 11 (UP11)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), ALEPH, Kerec, Hélène, Centre National de la Recherche Scientifique (CNRS)-École polytechnique (X)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3), Centre National de la Recherche Scientifique (CNRS)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Université Paris-Sud - Paris 11 (UP11), Barate, R, Buskulic, D, Decamp, D, Ghez, P, Goy, C, Lees, J, Lucotte, A, Minard, M, Nief, J, Odier, P, Pietrzyk, B, Casado, M, Chmeissani, M, Comas, P, Crespo, J, Delfino, M, Fernandez, E, Fernandezbosman, M, Garrido, L, Juste, A, Martinez, M, Orteu, S, Padilla, C, Park, I, Pascual, A, Perlas, J, Riu, I, Sanchez, F, Teubert, F, Colaleo, A, Creanza, D, Depalma, M, Gelao, G, Girone, M, Iaselli, G, Maggi, G, Maggi, M, Marinelli, N, Nuzzo, S, Ranieri, A, Raso, G, Ruggieri, F, Selvaggi, G, Silvestris, L, Tempesta, P, Tricomi, A, Zito, G, Huang, X, Lin, J, Ouyang, Q, Wang, T, Xie, Y, Xu, R, Xue, S, Zhang, J, Zhang, L, Zhao, W, Abbaneo, D, Alemany, R, Bazarko, A, Brightthomas, A, Cattaneo, M, Cerutti, F, Coyle, P, Drevermann, H, Forty, R, Frank, M, Hagelberg, R, Harvey, J, Janot, P, Jost, B, Kneringer, E, Knobloch, J, Lehraus, I, Lutters, G, Mato, P, Minten, A, Miquel, R, Mir, L, Moneta, L, Oest, T, Pacheco, A, Pusztaszeri, J, Ranjard, F, Rensing, P, Rizzo, G, Rolandi, L, Schlatter, D, Schmelling, M, Schmitt, M, Schneider, O, Tejessy, W, Tomalin, I, Venturi, A, Wachsmuth, H, Wagner, A, Ajaltouni, Z, Barres, A, Boyer, C, Falvard, A, Gay, P, Guicheney, C, Henrard, P, Jousset, J, Michel, B, Monteil, S, Montret, J, Pallin, D, Perret, P, Podlyski, F, Proriol, J, Rosnet, P, Rossignol, J, Fearnley, T, Hansen, J, Hansen, P, Nilsson, B, Rensch, B, Waananen, A, Daskalakis, G, Kyriakis, A, Markou, C, Simopoulou, E, Siotis, I, Vayaki, A, Zachariadou, K, Blondel, A, Bonneaud, G, Brient, J, Bourdon, P, Rouge, A, Rumpf, M, Valassi, A, Verderi, M, Videau, H, Candlin, D, Parsons, M, Focardi, E, Parrini, G, Corden, M, Georgiopoulos, C, Jaffe, D, Antonelli, A, Bencivenni, G, Bologna, G, Bossi, F, Campana, P, Capon, G, Casper, D, Chiarella, V, Felici, G, Laurelli, P, Mannocchi, G, Murtas, F, Murtas, G, Passalacqua, L, Pepealtarelli, M, Curtis, L, Dorris, S, Halley, A, Knowles, I, Lynch, J, Oshea, V, Raine, C, Scarr, J, Smith, K, Teixeiradias, P, Thompson, A, Thomson, E, Thomson, F, Turnbull, R, Becker, U, Geweniger, C, Graefe, G, Hanke, P, Hansper, G, Hepp, V, Kluge, E, Putzer, A, Schmidt, M, Sommer, J, Stenzel, H, Tittel, K, Werner, S, Wunsch, M, Beuselinck, R, Binnie, D, Cameron, W, Dornan, P, Martin, E, Moutoussi, A, Nash, J, Sedgbeer, J, Stacey, A, Williams, M, Dissertori, G, Girtler, P, Kuhn, D, Rudolph, G, Betteridge, A, Bowdery, C, Colrain, P, Crawford, G, Finch, A, Foster, F, Hughes, G, Sloan, T, Galla, A, Giehl, I, Greene, A, Hoffmann, C, Jakobs, K, Kleinknecht, K, Quast, G, Renk, B, Rohne, E, Sander, H, Vangemmeren, P, Zeitnitz, C, Aubert, J, Benchouk, C, Bonissent, A, Bujosa, G, Calvet, D, Carr, J, Diaconu, C, Etienne, F, Kontantinidis, N, Leroy, O, Payre, P, Rousseau, D, Talby, M, Sadouki, A, Thulasidas, M, Trabelsi, K, Aleppo, M, Ragusa, F, Berlich, R, Blum, W, Buscher, V, Dietl, H, Dydak, F, Ganis, G, Gotzhein, C, Kroha, H, Lutjens, G, Lutz, G, Manner, W, Moser, H, Richter, R, Rosadoschlosser, A, Schael, S, Settles, R, Seywerd, H, Stdenis, R, Wiedenmann, W, Wolf, G, Boucrot, J, Callot, O, Chen, S, Choi, Y, Cordier, A, Davier, M, Duflot, L, Grivaz, J, Heusse, P, Hocker, A, Jacholkowska, A, Jacquet, M, Kim, D, Lediberder, F, Lefrancois, J, Lutz, A, Nikolic, I, Park, H, Schune, H, Simion, S, Veillet, J, Videau, I, Zerwas, D, Azzurri, P, Bagliesi, G, Batignani, G, Bettarini, S, Bozzi, C, Calderini, G, Carpinelli, M, Ciocci, M, Ciulli, V, Dellorso, R, Fantechi, R, Ferrante, I, Foa, L, Forti, F, Giassi, A, Giorgi, M, Gregorio, A, Ligabue, F, Lusiani, A, Marrocchesi, P, Messineo, A, Palla, F, Sanguinetti, G, Sciaba, A, Spagnolo, P, Steinberger, J, Tenchini, R, Tonelli, G, Vannini, C, Verdini, P, Blair, G, Bryant, L, Chambers, J, Gao, Y, Green, M, Medcalf, T, Perrodo, P, Strong, J, Vonwimmerspergtoeller, J, Botterill, D, Clifft, R, Edgecock, T, Haywood, S, Maley, P, Norton, P, Thompson, J, Wright, A, Blochdevaux, B, Colas, P, Emery, S, Kozanecki, W, Lancon, E, Lemaire, M, Locci, E, Perez, P, Rander, J, Renardy, J, Roussarie, A, Schuller, J, Schwindling, J, Trabelsi, A, Vallage, B, Black, S, Dann, J, Johnson, R, Kim, H, Litke, A, Mcneil, M, Taylor, G, Booth, C, Boswell, R, Brew, C, Cartwright, S, Combley, F, Kelly, M, Letho, M, Newton, W, Reeve, J, Thompson, L, Bohrer, A, Brandt, S, Cowan, G, Grupen, C, Minguetrodriguez, J, Rivera, F, Saraiva, P, Smolik, L, Stephan, F, Apollonio, M, Bosisio, L, Dellamarina, R, Giannini, G, Gobbo, B, Musolino, G, Rothberg, J, Wasserbaech, S, Armstrong, S, Elmer, P, Feng, Z, Ferguson, D, Gonzalez, S, Grahl, J, Greening, T, Hayes, O, Hu, H, Mcnamara, P, Nachtman, J, Orejudos, W, Pan, Y, Saadi, Y, Scott, I, Walsh, J, Wu, S, Wu, X, Yamartino, J, Zheng, M, Zobernig, G, Lees, Jp, Minard, Mn, Nief, Jy, Casado, Mp, Crespo, Jm, Garrido, Li, Park, Ic, Perlas, Ja, Bazarko, Ao, Brightthomas, Ao, Forty, Rw, Mir, Lm, Pusztaszeri, Jf, Tomalin, Ir, Montret, Jc, Rossignol, Jm, Hansen, Jb, Hansen, Jd, Hansen, Jr, Hansen, Ph, Brient, Jc, Candlin, Dj, Parsons, Mi, Jaffe, De, Murtas, Gp, Dorris, Sj, Halley, Aw, Knowles, Ig, Lynch, Jg, Scarr, Jm, Turnbull, Rm, Kluge, Ee, Binnie, Dm, Dornan, Pj, Martin, Eb, Sedgbeer, Jk, Stacey, Am, Williams, Md, Betteridge, Ap, Bowdery, Ck, Finch, Aj, Williams, Mi, Greene, Am, Sander, Hg, Aubert, Jj, Moser, Hg, Grivaz, Jf, Kim, Dw, Lutz, Am, Park, Hj, Veillet, Jj, Ciocci, Ma, Giorgi, Ma, Ligabue, Franco, Lusiani, Alberto, Verdini, Pg, Blair, Ga, Bryant, Lm, Chambers, Jt, Green, Mg, Strong, Ja, Vonwimmerspergtoeller, Jh, Botterill, Dr, Clifft, Rw, Edgecock, Tr, Norton, Pr, Thompson, Jc, Wright, Ae, Lemaire, Mc, Renardy, Jf, Schuller, Jp, Black, Sn, Dann, Jh, Johnson, Rp, Kim, Hy, Litke, Am, Mcneil, Ma, Booth, Cn, Brew, Caj, Newton, Wm, Thompson, Lf, Armstrong, Sr, Ferguson, Dp, Greening, Tc, Hayes, Oj, Mcnamara, Pa, Nachtman, Jm, Pan, Yb, Scott, Ij, Wu, Sl, Yamartino, Jm, and Zobernig, G.
Subjects: Physics, Particle physics, Range (particle radiation), Photon, [PHYS.HEXP] Physics [physics]/High Energy Physics - Experiment [hep-ex], Physics and Astronomy (miscellaneous), Meson, 010308 nuclear & particles physics, Electron–positron annihilation, Monte Carlo method, Hadron, 01 natural sciences, Nuclear physics, Momentum, Pion, 0103 physical sciences, [PHYS.HEXP]Physics [physics]/High Energy Physics - Experiment [hep-ex], High Energy Physics::Experiment, Nuclear Experiment, 010306 general physics, Particle Physics - Experiment
Abstract: A measurement of the inclusive production of pi(0) mesons in hadronic Z decays is presented and compared to Monte Carlo model predictions. The analysis is based on approximately 2 million hadronic events recorded with the ALEPH detector at LEP at a centre-of-mass energy of root s = 91.2 GeV. Neutral pions are reconstructed using photons measured in the electromagnetic calorimeter and photons from conversion pairs. The inclusive pi(0) momentum spectrum is measured in the range 0.025 < x(p) = p/p(beam) < 1. In this range the number of pi(0) per hadronic Z is found to be 4.80 +/- 0.07(stat) +/- 0.31(sys). The differential inclusive pi(0) cross section is also measured as a function of transverse momentum with respect to the event plane (p(T)(in) and p(T)(out)). RI ANTONELLI, ANTONELLA/C-6238-2011; Passalacqua, Luca/F-5127-2011; Murtas, Fabrizio/B-5729-2012; St.Denis, Richard/C-8997-2012; Forti, Francesco/H-3035-2011; Ferrante, Isidoro/F-1017-2012

4. A measurement of the QCD colour factors and a limit on the light gluino

Author: Armstrong, S Schael, G Lutjens, M. Chmeissani, G. R. Bonneaud, M H. Lehto, A Juste, M Thulasidas, H Dietl, K Jakobs, C Benchouk, G Lutters, J Sommer, Am Litke, X Wu, L. Rolandi, E. Lancon, G Giannini, Hansen, Rw Clifft, Ir Tomalin, P Saraiva, P Payre, Giorgio Maggi, Lucia Silvestris, P. Bourdon, S Haywood, A. Blondel, C Padilla, O. Callot, Jordan Nash, P Henrard, Tc Greening, H Stenzel, Pa Mcnamara, A. Trabelsi, D Zerwas, As Thompson, Ja Strong, Arnaud Lucotte, B Pietrzyk, L Moneta, G Gelao, P Perrodo, B Jost, M Frank, I. Siotis, Ga Blair, G. Capon, O'Shea, Jj Veillet, Hg Sander, E Simopoulou, E Fernandez, A Putzer, F Ranjard, L. F. Thompson, Ao Bazarko, L. Passalacqua, R. Barate, Giuseppe Iaselli, A Moutoussi, S Xue, Dps Ferguson, Claudine Boyer, T Fearnley, G Lutz, Mi Williams, C. Grupen, W Tejessy, R. Denis, Dw Kim, D Rousseau, J. Grahl, G Bujosa, P. Tempesta, A.E. Wright, S Bettarini, F. Sanchez, P Coyle, R Settles, C. N. Booth, Ck Bowdery, P Heusse, Pj Dornan, G. Hansper, Mg Green, Kelly, L Duflot, S. Gonzalez, A. Antonelli, L Garrido, M. Pepe-Altarelli, K Tittel, Jm Nachtman, C Goy, Ig Knowles, Chiarella, De Jaffe, S Nuzzo, D. Pallin, Mi Parsons, P Colas, A. Tricomi, A. Jacholkowska, M. Verderi, Oj Hayes, Jm Rossignol, Jm Yamartino, A Kyriakis, Mc Lemaire, J.H. Dann, Jp Schuller, Eb Martin, L Zhang, A Roussarie, A Messineo, D. J. Candlin, P. Comas, G. Bencivenni, M. Aleppo, Q Ouyang, S Monteil, A Bonissent, F. Ligabue, C Georgiopoulos, D. Casper, R Boswell, G Dissertori, G. Zobernig, P vanGemmeren, R Alemany, G. Mannocchi, A Minten, Sj Dorris, Jf Renardy, A Hocker, Lorenzo Foà, A Rouge, A. Wäänänen, Ic Park, Z. Y. Feng, S. L. Wu, P. Bright-Thomas, G Rizzo, Ps Marrocchesi, A Pascual, Jh Vonwimmerspergtoeller, Rw Forty, Philippe Odier, A Cordier, Hepp, G. Batignani, D Schlatter, T Sloan, J.Y. Nief, G Bagliesi, M. N. Minard, Ma Giorgi, P. Laurelli, P Ghez, M Corden, A. Böhrer, F Palla, X Huang, M Talby, F Podlyski, Giovanna Selvaggi, L Bosisio, Hg Moser, R Beuselinck, M. Carpinelli, M Girone, I Lehraus, H. Y. Kim, Maria Agnese Ciocci, A. Vayaki, J. P. Lees, S Brandt, A Sadouki, G Cowan, Caj Brew, Guido Tonelli, W Zhao, M Rumpf, P Elmer, Rm Turnbull, W Blum, Am Lutz, C Raine, G Ganis, H Wachsmuth, Si Chen, Ja Perlas, F Cerutti, H Kroha, G. Zito, P Maley, J Steinberger, R Tenchini, G Wolf, G Hughes, L Smolik, W Orejudos, P Rosnet, A Gregorio, C Zeitnitz, I Ferrante, S. L. Cartwright, Gp Murtas, Evelyn Thomson, R Maggi, W Wiedenmann, D Abbaneo, Donato Creanza, A Falvard, J Walsh, I Nikolic, J Boucrot, C Diaconu, Mp Casado, A. Rosado-Schlosser, Y Xie, A Giassi, Rp Johnson, A Venturi, P Azzurri, Jm Crespo, F. Ruggieri, E Kneringer, Jf Pusztaszeri, R Fantechi, Bs Nilsson, T Medcalf, Aw Halley, Young-Il Choi, P Colrain, Buscher, C Gotzhein, S. Orteu, W Cameron, C Vannini, P Perret, R Xu, Jk Sedgbeer, M Cattaneo, I.J. Scott, J-C. Brient, J Carr, M Wunsch, Ap Betteridge, O Leroy, J Lin, Ziad Ajaltouni, C. Hoffmann, E Rohne, Wm Newton, J Jousset, I Videau, A. Wagner, P Girtler, Pg Verdini, M Delfino, B Gobbo, B Renk, A Sciaba, G. Daskalakis, J. J. Aubert, M Depalma, P. H. Hansen, G Parrini, G Calderini, G. Rudolph, M. Fernandez-Bosman, J Reeve, I Riu, P Perez, A Barres, S.N. Black, R Richter, F. Murtas, P. Rensing, Y Saadi, P. Campana, B. Rensch, F Ragusa, M. H. Schune, L. M. Mir, Am Stacey, G Quast, A Colaleo, D Kuhn, M.G. Schmidt, A. Valassi, P Hanke, J-C. Montret, H Seywerd, K. Trabelsi, Am Greene, G Musolino, M Davier, F Combley, J. Schwindling, Jg Lynch, K Zachariadou, B Michel, M Schmitt, F. Dydak, A. J. Finch, N Konstantinidis, J Zhang, Yang Gao, P Mato, F Teubert, A Pacheco, H Hu, A Ranieri, W. Kozanecki, F. Forti, M Martinez, Y. S. Gao, C. Guicheney, C. Ferdi, H Drevermann, G. Raso, Lm Bryant, J Harvey, C. Markou, D Decamp, Dm Binnie, E Locci, S Wasserbaech, G Sanguinetti, N. Marinelli, I. Giehl, Pr Norton, Jb Hansen, C Geweniger, M. Apollonio, U Becker, F. Thomson, G. Felici, Patrick Janot, A. Galla, J Knobloch, Jm Scarr, Jt Chambers, M. Zheng, J Rothberg, R. Berlich, M Jacquet, Ma Mcneil, T Wang, Williams, R DellOrso, R Hagelberg, A. Lusiani, H Videau, S. Goodsir, Ciulli, K Smith, R Miquel, B. Bloch-Devaux, E Focardi, J Proriol, P. Spagnolo, J.D. Hansen, J Lefrancois, F Lediberder, S. Emery, Yb Pan, W Manner, L Curtis, T. R. Edgecock, F. Bossi, P. Teixeira-Dias, G Graefe, J Rander, S Simion, R Dellamarina, D Buskulic, K Kleinknecht, G Bologna, S Werner, F. Etienne, G Crawford, J-F Grivaz, E-E Kluge, F Stephan, David Calvet, M. Schmelling, G Taylor, Botterill, C. Bozzi, B. Vallage, Hj Park, F Foster, Jc Thompson, O Schneider, Barate, R, Buskulic, D, Decamp, D, Ghez, P, Goy, C, Lees, Jp, Lucotte, A, Minard, Mn, Nief, Jy, Odier, P, Pietrzyk, B, Casado, Mp, Chmeissani, M, Comas, P, Crespo, Jm, Delfino, M, Fernandez, E, Fernandezbosman, M, Garrido, L, Juste, A, Martinez, M, Miquel, R, Mir, Lm, Orteu, S, Padilla, C, Park, Ic, Pascual, A, Perlas, Ja, Riu, I, Sanchez, F, Teubert, F, Colaleo, A, Creanza, D, Depalma, M, Gelao, G, Iaselli, G, Maggi, G, Maggi, R, Marinelli, N, Nuzzo, S, Ranieri, A, Raso, G, Ruggieri, F, Selvaggi, G, Silvestris, L, Tempesta, P, Tricomi, A, Zito, G, Huang, X, Lin, J, Ouyang, Q, Wang, T, Xie, Y, Xu, R, Xue, S, Zhang, J, Zhang, L, Zhao, W, Abbaneo, D, Alemany, R, Bazarko, Ao, Brightthomas, P, Cattaneo, M, Cerutti, F, Drevermann, H, Forty, Rw, Frank, M, Hagelberg, R, Harvey, J, Janot, P, Jost, B, Kneringer, E, Knobloch, J, Lehraus, I, Lutters, G, Mato, P, Minten, A, Moneta, L, Pacheco, A, Pusztaszeri, Jf, Ranjard, F, Rensing, P, Rizzo, G, Rolandi, Luigi, Schlatter, D, Schmelling, M, Schmitt, M, Schneider, O, Tejessy, W, Tomalin, Ir, Wachsmuth, H, Wagner, A, Ajaltouni, Z, Barres, A, Boyer, C, Falvard, A, Ferdi, C, Gay, P, Guicheney, C, Henrard, P, Jousset, J, Michel, B, Monteil, S, Montret, Jc, Pallin, D, Perret, P, Podlyski, F, Proriol, J, Rosnet, P, Rossignol, Jm, Fearnley, T, Hansen, Jb, Hansen, Jd, Hansen, Jr, Hansen, Ph, Nilsson, B, Rensch, B, Waananen, A, Daskalakis, G, Kyriakis, A, Markou, C, Simopoulou, E, Siotis, I, Vayaki, A, Zachariadou, K, Blondel, A, Bonneaud, G, Brient, Jc, Bourdon, P, Rouge, A, Rumpf, M, Valassi, A, Verderi, M, Videau, H, Candlin, Dj, Parsons, Mi, Focardi, E, Parrini, G, Corden, M, Georgiopoulos, C, Jaffe, De, Antonelli, A, Bencivenni, G, Bologna, G, Bossi, F, Campana, P, Capon, G, Casper, D, Chiarella, V, Felici, G, Laurelli, P, Mannocchi, G, Murtas, F, Murtas, Gp, Passalacqua, L, Pepealtarelli, M, Curtis, L, Dorris, Sj, Halley, Aw, Knowles, Ig, Lynch, Jg, Oshea, V, Raine, C, Scarr, Jm, Smith, K, Teixeiradias, P, Thompson, A, Thomson, E, Thomson, F, Turnbull, Rm, Becker, U, Geweniger, C, Graefe, G, Hanke, P, Hansper, G, Hepp, V, Kluge, Ee, Putzer, A, Schmidt, M, Sommer, J, Tittel, K, Werner, S, Wunsch, M, Beuselinck, R, Binnie, Dm, Cameron, W, Dornan, Pj, Girone, M, Goodsir, S, Martin, Eb, Moutoussi, A, Nash, J, Sedgbeer, Jk, Stacey, Am, Williams, Md, Dissertori, G, Girtler, P, Kuhn, D, Rudolph, G, Betteridge, Ap, Bowdery, Ck, Colrain, P, Crawford, G, Finch, Aj, Foster, F, Hughes, G, Sloan, T, Williams, Mi, Galla, A, Giehl, I, Greene, Am, Hoffmann, C, Jakobs, K, Kleinknecht, K, Quast, G, Renk, B, Rohne, E, Sander, Hg, Vangemmeren, P, Zeitnitz, C, Aubert, Jj, Benchouk, C, Bonissent, A, Bujosa, G, Calvet, D, Carr, J, Coyle, P, Diaconu, C, Etienne, F, Konstantinidis, N, Leroy, O, Payre, P, Rousseau, D, Talby, M, Sadouki, A, Thulasidas, M, Trabelsi, K, Aleppo, M, Ragusa, F, Berlich, R, Blum, W, Buscher, V, Dietl, H, Dydak, F, Ganis, G, Gotzhein, C, Kroha, H, Lutjens, G, Lutz, G, Manner, W, Moser, Hg, Richter, R, Rosadoschlosser, A, Schael, S, Settles, R, Seywerd, H, Denis, R, Stenzel, H, Wiedenmann, W, Wolf, G, Boucrot, J, Callot, O, Chen, S, Choi, Y, Cordier, A, Davier, M, Duflot, L, Grivaz, Jf, Heusse, P, Hocker, A, Jacholkowska, A, Jacquet, M, Kim, Dw, Lediberder, F, Lefrancois, J, Lutz, Am, Nikolic, I, Park, Hj, Schune, Mh, Simion, S, Veillet, Jj, Videau, I, Zerwas, D, Azzurri, P, Bagliesi, G, Batignani, G, Bettarini, S, Bozzi, C, Calderini, G, Carpinelli, M, Ciocci, Ma, Ciulli, V, Dellorso, R, Fantechi, R, Ferrante, I, Foa, L, Forti, F, Giassi, A, Giorgi, Ma, Gregorio, A, Ligabue, Franco, Lusiani, Alberto, Marrocchesi, P, Messineo, A, Palla, F, Sanguinetti, G, Sciaba, A, Spagnolo, P, Steinberger, J, Tenchini, R, Tonelli, G, Vannini, C, Venturi, A, Verdini, Pg, Blair, Ga, Bryant, Lm, Chambers, Jt, Gao, Y, Green, Mg, Medcalf, T, Perrodo, P, Strong, Ja, Vonwimmerspergtoeller, Jh, Botterill, Dr, Clifft, Rw, Edgecock, Tr, Haywood, S, Maley, P, Norton, Pr, Thompson, Jc, Wright, Ae, Blochdevaux, B, Colas, P, Emery, S, Kozanecki, W, Lancon, E, Lemaire, Mc, Locci, E, Perez, P, Rander, J, Renardy, Jf, Roussarie, A, Schuller, Jp, Schwindling, J, Trabelsi, A, Vallage, B, Black, Sn, Dann, Jh, Johnson, Rp, Kim, Hy, Litke, Am, Mcneil, Ma, Taylor, G, Booth, Cn, Boswell, R, Brew, Caj, Cartwright, S, Combley, F, Kelly, M, Lehto, M, Newton, Wm, Reeve, J, Thompson, Lf, Bohrer, A, Brandt, S, Cowan, G, Grupen, C, Saraiva, P, Smolik, L, Stephan, F, Apollonio, M, Bosisio, L, Dellamarina, R, Giannini, G, Gobbo, B, Musolino, G, Rothberg, J, Wasserbaech, S, Armstrong, Sr, Elmer, P, Feng, Z, Ferguson, Dp, Gonzalez, S, Grahl, J, Greening, Tc, Hayes, Oj, Hu, H, Mcnamara, Pa, Nachtman, Jm, Orejudos, W, Pan, Yb, Saadi, Y, Scott, Ij, Walsh, J, Wu, Sl, Wu, X, Yamartino, Jm, Zheng, M, Zobernig, G., Lees, J, Minard, M, Nief, J, Casado, M, Crespo, J, Mir, L, Park, I, Perlas, J, Bazarko, A, Forty, R, Pusztaszeri, J, Rolandi, L, Tomalin, I, Montret, J, Rossignol, J, Hansen, J, Hansen, P, Brient, J, Candlin, D, Parsons, M, Jaffe, D, Murtas, G, Dorris, S, Halley, A, Knowles, I, Lynch, J, Scarr, J, Turnbull, R, Kluge, E, Binnie, D, Dornan, P, Martin, E, Sedgbeer, J, Stacey, A, Williams, M, Betteridge, A, Bowdery, C, Finch, A, Greene, A, Sander, H, Aubert, J, Moser, H, Grivaz, J, Kim, D, Lutz, A, Park, H, Schune, M, Veillet, J, Ciocci, M, Giorgi, M, Ligabue, F, Lusiani, A, Verdini, P, Blair, G, Bryant, L, Chambers, J, Green, M, Strong, J, Vonwimmerspergtoeller, J, Botterill, D, Clifft, R, Edgecock, T, Norton, P, Thompson, J, Wright, A, Lemaire, M, Renardy, J, Schuller, J, Black, S, Dann, J, Johnson, R, Kim, H, Litke, A, Mcneil, M, Booth, C, Brew, C, Newton, W, Thompson, L, Armstrong, S, Ferguson, D, Greening, T, Hayes, O, Mcnamara, P, Nachtman, J, Pan, Y, Scott, I, Wu, S, Yamartino, J, and Zobernig, G
Subjects: Quantum chromodynamics, Physics, Gluino, Particle physics, Physics and Astronomy (miscellaneous), Electron–positron annihilation, High Energy Physics::Phenomenology, Lower limit, Nuclear physics, Strong coupling, High Energy Physics::Experiment, Limit (mathematics), Particle Physics - Experiment, Particle Physics - Phenomenology
Abstract: Using data collected from 1992 to 1995 with the ALEPH detector at LEP, a measurement of the colour factor ratios C-A/C-F and T-F/C-F and the strong coupling constant = C-F alpha(s), (M-Z)/(2 pi) has been performed by fitting theoretical predictions simultaneously to the measured differential two-jet rate and angular distributions in four-jet events. The result is found to be in excellent agreement with QCD. C-A/C-F = 2.20 +/- 0.09 (stat) +/- 0.13 (syst), T-F/C-F = 0.29 +/- 0.05 (stat) +/- 0.06 (syst). Fixing C-A/C-F and T-F/C-F to the QCD values permits a determination of alpha(s) (M-Z) and n(f), the number of active flavours. With this measurement the existence of a gluino with mass below 6.3 GeV/c(2) is excluded at 95% confidence level. RI ANTONELLI, ANTONELLA/C-6238-2011; Passalacqua, Luca/F-5127-2011; Murtas, Fabrizio/B-5729-2012; Sanchez, Federico/F-5809-2012; Forti, Francesco/H-3035-2011; Ferrante, Isidoro/F-1017-2012

5. Quantification of hypoxia-related gene expression as a potential approach for clinical outcome prediction in breast cancer.

Author: El Guerrab A, Cayre A, Kwiatkowski F, Privat M, Rossignol JM, Rossignol F, Penault-Llorca F, and Bignon YJ
Subjects: Breast Neoplasms genetics, Female, Humans, Neoplasm Recurrence, Local, Retrospective Studies, Breast Neoplasms pathology, Cell Hypoxia, Gene Expression
Abstract: Breast cancers are solid tumors frequently characterized by regions with low oxygen concentrations. Cellular adaptations to hypoxia are mainly determined by "hypoxia inducible factors" that mediate transcriptional modifications involved in drug resistance and tumor progression leading to metastasis and relapse occurrence. In this study, we investigated the prognostic value of hypoxia-related gene expression in breast cancer. A systematic review was conducted to select a set of 45 genes involved in hypoxia signaling pathways and breast tumor progression. Gene expression was quantified by RT-qPCR in a retrospective series of 32 patients with invasive ductal carcinoma. Data were analyzed in relation to classical clinicopathological criteria and relapse occurrence. Coordinated overexpression of selected genes was observed in high-grade and HER2+ tumors. Hierarchical cluster analysis of gene expression significantly segregated relapsed patients (p = 0.008, Chi2 test). All genes (except one) were up-regulated and six markers were significantly expressed in tumors from recurrent patients. The expression of this 6-gene set was used to develop a basic algorithm for identifying recurrent patients according to a risk score of relapse. Analysis of Kaplan-Meier relapse-free survival curves allowed the definition of a threshold score of 2 (p = 0.021, Mantel-Haenszel test). The risk of recurrence was increased by 40% in patients with a high score. In addition to classical prognostic factors, we showed that hypoxic markers have potential prognostic value for outcome and late recurrence prediction, leading to improved treatment decision-making for patients with early-stage invasive breast cancer. It will be necessary to validate the clinical relevance of this prognostic approach through independent studies including larger prospective patient cohorts.
Published: 2017
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6. Conserved aromatic residues of the hepatitis B virus Precore propeptide are involved in a switch between distinct dimeric conformations and essential in the formation of heterocapsids.

Author: Duriez M, Thouard A, Bressanelli S, Rossignol JM, and Sitterlin D
Subjects: Amino Acid Substitution, Cell Line, Hepatitis B Core Antigens genetics, Hepatitis B virus genetics, Humans, Models, Molecular, Mutagenesis, Site-Directed, Mutant Proteins genetics, Mutant Proteins metabolism, Protein Conformation, Protein Precursors genetics, Conserved Sequence, Hepatitis B Core Antigens metabolism, Hepatitis B virus physiology, Protein Multimerization, Protein Precursors metabolism
Abstract: The Hepatitis B virus Precore protein, present in the secretory pathway as the HBeAg precursor, can associate in the cytoplasm with the Core protein to form heterocapsids, likely to favor viral persistence. Core and Precore proteins share their primary sequence except for ten additional aminoacids at the N-terminus of Precore. To address the role of this propeptide sequence in the formation of Precore heterocapsids, we designed a Precore mutant in which the two propeptide tryptophans are replaced by glycines. This mutant retains the properties of the wild-type Precore, notably cell trafficking and ability to interact with Core. However, it is not incorporated into heterocapsids and forms stable dimers distinct from the labile HBe dimers and the presumably Core-like dimers assembled into heterocapsids. Our data highlights the essential role of Precore׳s propeptide in switching between different conformations for different functions and pinpoint the propeptide Tryptophan residues as central in these properties., (Copyright © 2014 Elsevier Inc. All rights reserved.)
Published: 2014
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7. Rôle(s) de la protéine cellulaire gC1qR dans les cycles viraux.

Author: Lagaudrière-Gesbert C, Purvina M, Assrir N, and Rossignol JM
Abstract: The cellular protein gC1qR (also named HABP1, p32, p33 or TAP) has been identified as a partner of several viral proteins belonging to different virus families. gC1qR is a mitochondrial protein also present at the cell surface and in the nucleus. In normal cells, gC1qR seems involved in diverse biological processes related to its cellular localization. gC1qR could be involved in apoptosis in mitochondria, in RNA splicing in the nucleus or in immune and inflammatory responses at the cell surface. The multiple functions of gC1qR, as the variety of its viral partners, raise the question of its possible function(s) in the viral cycle. The goal of this review is to: (i) summarize what is known about gC1qR, (ii) focus on the demonstrated or hypothetical functions of the gC1qR-viral proteins complexes reported in the literature and (iii) propose a model on the possible roles of gC1qR in the viral life cycles.
Published: 2012
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8. Human hepatitis B viral e antigen and its precursor P20 inhibit T lymphocyte proliferation.

Author: Purvina M, Hoste A, Rossignol JM, and Lagaudrière-Gesbert C
Subjects: Amino Acid Sequence, Carrier Proteins immunology, Cells, Cultured, Hepatitis B e Antigens chemistry, Hepatitis B e Antigens genetics, Humans, Interleukin-1 Receptor Accessory Protein immunology, Mitochondrial Proteins immunology, Molecular Sequence Data, Cell Proliferation, Hepatitis B e Antigens immunology, Hepatitis B virus immunology, Lymphocyte Activation, T-Lymphocytes immunology, T-Lymphocytes virology
Abstract: The hepatitis B virus (HBV) Precore protein is processed through the secretory pathway directly as HBeAg or with the generation of an intermediate (P20). Precore gene has been shown to be implicated in viral persistence, but the functions of HBeAg and its precursors have not been fully elucidated. We show that the secreted proteins HBeAg and P20 interact with T cell surface and alter Kit-225 and primary T cells proliferation, a process which may facilitate the establishment of HBV persistence. Our data indicate that the N-terminal end of Precore is important for these inhibitory effects and exclude that they are dependent on the association of HBeAg and P20 with two characterized cell surface ligands, the Interleukin-1 Receptor Accessory Protein and gC1qR (present study)., (Copyright © 2012 Elsevier Inc. All rights reserved.)
Published: 2012
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9. Role of the hepatitis B virus proteins in pro- and anti-apoptotic processes.

Author: Assrir N, Soussan P, Kremsdorf D, and Rossignol JM
Subjects: Animals, Hepatitis B virus genetics, Hepatitis B virus metabolism, Hepatocytes cytology, Hepatocytes virology, Host-Pathogen Interactions, Humans, Liver cytology, Models, Biological, Viral Proteins metabolism, Apoptosis, Hepatitis B virus physiology, Liver virology, Viral Proteins physiology
Abstract: The Hepatitis B virus (HBV) can induces severe liver diseases as chronic hepatitis and hepatocellular carcinoma. Actually, apoptosis can play an important role in the progress of these diseases. As apoptosis goes through various extrinsic or intrinsic pathways, with activation of caspases and the possible involvement of mitochondria, HBV proteins can interfere with the various apoptosis processes. So far, four HBV proteins were reported to have such effect: the Large envelope protein, a truncated form of the Middle envelope protein, the HBx protein and HBSP, a protein generated from a spliced mRNA. In addition, our recent results suggest that indirectly the precore protein could have a function in apoptosis. This review focuses on the putative roles of HBV proteins as pro- or anti-apoptotic factors and the relationship which could exist with the HBV life cycle.
Published: 2010
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10. The hepatitis B virus precore protein is retrotransported from endoplasmic reticulum (ER) to cytosol through the ER-associated degradation pathway.

Author: Duriez M, Rossignol JM, and Sitterlin D
Subjects: Biological Transport, Cell Line, Cytoplasm metabolism, Endoplasmic Reticulum Chaperone BiP, Heat-Shock Proteins metabolism, Hepatitis B Core Antigens chemistry, Humans, Models, Biological, Models, Genetic, Molecular Chaperones metabolism, Protein Binding, Protein Denaturation, Protein Transport, Viral Core Proteins chemistry, Cytosol metabolism, Endoplasmic Reticulum metabolism, Hepatitis B Core Antigens metabolism, Hepatitis B virus metabolism, Viral Core Proteins metabolism, Viral Proteins chemistry
Abstract: The hepatitis B virus precore protein is closely related to the nucleocapsid core protein but is processed distinctly in the cell and plays a different role in the viral cycle. Precore is addressed to the endoplasmic reticulum (ER) through a signal peptide, and the form present in the ER is the P22 protein. P22 is then cleaved in its C-terminal part to be secreted as HBe antigen. In addition, a cytosolic form of 22 kDa less characterized has been observed. Precore gene was shown to be implicated in viral persistence, but until now, the actual protein species involved has not been determined. Our work focuses on the cytosolic form of precore. Using human cells expressing precore and a convenient fractionation assay, we demonstrated that the cytosolic form is identical to the ER form and retrotransported in the cytoplasm through the ER-associated degradation pathway. This cellular machinery translocates misfolded proteins to the cytoplasm, where they are ubiquitinated on lysine residues and degraded by proteasome. We showed that precore escapes proteasome due to its low lysine content and accumulates in the cytosol. The role of this retrotransport was investigated. In the presence of precore, we found a specific redistribution of the Grp78/BiP chaperone protein to cytosol and demonstrated a specific interaction between precore and Grp78/BiP. Altogether, these data support the idea that the hepatitis B virus develops a strategy to take advantage of the ER-associated degradation pathway, allowing distinct subcellular localization and probably distinct roles for the viral precore protein.
Published: 2008
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11. Ribosome can resume the translation in both +1 or -1 frames after encountering an AGA cluster in Escherichia coli.

Author: Lainé S, Thouard A, Komar AA, and Rossignol JM
Subjects: Base Sequence, Codon genetics, DNA Primers genetics, DNA, Bacterial genetics, Escherichia coli metabolism, Frameshifting, Ribosomal, Molecular Sequence Data, Open Reading Frames, Plasmids genetics, Protein Biosynthesis, RNA, Bacterial genetics, RNA, Bacterial metabolism, RNA, Messenger genetics, RNA, Messenger metabolism, Recombinant Proteins genetics, Ribosomes metabolism, Escherichia coli genetics
Abstract: In Escherichia coli the rare codons AGG, AGA and CGA are reported to have a detrimental effect on protein synthesis, especially during the expression of heterologous proteins. In the present work, we have studied the impact of successive clusters of these rare codons on the accuracy of mRNA translation in E. coli. For this purpose, we have analyzed the expression of an mRNA which contains in its 3' region a triplet and a tandem of AGA codons. This mRNA is derived from the human hepatitis B virus (HBV) preC gene. Both in eukaryotic cells and in eukaryotic cell-free translation system, this mRNA, directs the synthesis of a single 25 kDa protein. However, in a conventional E. coli strain BL 21 (DE3), transformed with a plasmid expressing this protein the synthesis of four polypeptides ranging from 30 to 21.5 kDa can be observed. Using different approaches, notably expression of i) precore mutated proteins or ii) chimeric proteins containing HA- and Myc-tags downstream of the AGA clusters (respectively in the -1 or +1 frame), we have found that when the ribosome encounters the AGA clusters, it can then resume the translation in both +1 and -1 frames. This result is in agreement with the model proposed recently by Baranov et al. (Baranov, P.V., Gesteland, R.F., Atkins, J.F., 2004. P-site tRNA is a crucial initiator of ribosomal frameshifting. RNA 10, 221-230), thus confirming that AGA/AGG codons can serve as sites for -1 frameshifting events. Only +1 frameshifting was suggested previously to occur at the AGA/AGG clusters.
Published: 2008
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12. "DNA, more than just a ladder". A tribute to Michel Duguet (1943-2005).

Author: Rossignol JM, Jacquet M, and Arimondo PB
Subjects: DNA Replication, France, History, 20th Century, History, 21st Century, DNA chemistry, DNA genetics, Genetics history
Published: 2007
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13. In vitro and in vivo interactions between the hepatitis B virus protein P22 and the cellular protein gC1qR.

Author: Lainé S, Thouard A, Derancourt J, Kress M, Sitterlin D, and Rossignol JM
Subjects: Amino Acid Sequence, Carrier Proteins, Cell Nucleus metabolism, Cells, Cultured, Cytoplasm metabolism, Fluorescent Antibody Technique, Humans, Mitochondria metabolism, Mitochondrial Proteins, Molecular Sequence Data, Sequence Homology, Amino Acid, Viral Proteins chemistry, Hyaluronan Receptors, Membrane Glycoproteins, Receptors, Complement metabolism, Viral Proteins metabolism
Abstract: gC1qR, a mitochondrial matrix protein, was identified as the main cellular partner of the hepatitis B virus P22 protein. We demonstrated by immunofluorescence studies that some P22 molecules were colocalized with the endogenous gC1qR in both the cytoplasm and the nucleus but never in the mitochondria. We also showed that the last 34 amino acids of P22 were involved in the association with gC1qR.
Published: 2003
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14. Proteolytic processing of the hepatitis B virus e antigen precursor. Cleavage at two furin consensus sequences.

Author: Messageot F, Salhi S, Eon P, and Rossignol JM
Subjects: Amino Acid Sequence, Furin, Hepatitis B e Antigens chemistry, Molecular Sequence Data, Proprotein Convertases, Hepatitis B e Antigens biosynthesis, Protein Precursors metabolism, Subtilisins physiology
Abstract: The Hepatitis B virus P22 protein is a nonstructural protein that is the precursor of the 17-kDa secreted e antigen (HBeAg). The mature HBeAg is obtained after the removal of the C-terminal region of P22, a process which involves a proprotein convertase. Our studies show first that the protease could cleave P22 at the C-terminal side of Arg(167) or Arg(154) and second, that the maturation process can be either done in one step or in two steps with the generation of a processing intermediate (P20). Our data also demonstrate that the removal of the P22 C terminus, which occurs mainly in the trans-Golgi network, can also be achieved after exocytosis. Keeping in mind this characteristic and the amino acid sequence of the cleavage sites, we concluded that furin is involved in the maturation of the HBeAg. In addition, we show that in our experimental system, the HBeAg is a 164-amino acid protein and not a 159-amino acid protein as previously reported.
Published: 2003
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15. Overexpression and purification of the hepatitis B e antigen precursor.

Author: Lainé S, Salhi S, and Rossignol JM
Subjects: Base Sequence, Chromatography, Affinity, Codon genetics, Escherichia coli, Gene Expression Regulation, Bacterial, Genetic Vectors genetics, Hepatitis B e Antigens biosynthesis, Humans, Molecular Sequence Data, Protein Folding, Protein Precursors biosynthesis, RNA, Bacterial genetics, Recombinant Fusion Proteins metabolism, Hepatitis B e Antigens genetics, Hepatitis B e Antigens isolation & purification, Protein Precursors genetics, Protein Precursors isolation & purification
Abstract: Circumstantial evidence suggests that the secreted hepatitis B virus (HBV) e antigen (HBeAg) and/or its 22 kDa precursor (P22) have an essential role in the establishment of persistent infection. In order to identify cellular proteins that could interact with P22, large amounts of this protein are required to perform pull-down assays. A plasmid was constructed encoding a recombinant P22 with a Histidine-tag at its N-terminal extremity (P22r). The initial attempts to overexpress P22r in a conventional Escherichia coli strain failed, most likely due to the presence of rare AGA/AGG codon clusters in the 3' part of the gene. To overcome this difficulty, P22r was overexpressed in the Epicurian coli BL21-codonplus (DE3)-RIL strain, which possesses extra copies of the ArgU gene that encodes the tRNA(AGA/AGG). In this strain, P22r was overexpressed successfully and then purified in milligram quantities by metal affinity chromatography on Ni2+-chelated His-Bind resin. The purified recombinant protein P22r was able to interact with a cellular protein (P32), which had previously been shown to co-immunoprecipitate with native P22, indicating that at least some of the P22r molecules were folded correctly.
Published: 2002
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16. Identification of a cellular protein specifically interacting with the precursor of the hepatitis B e antigen.

Author: Salhi S, Messageot F, Carlier D, Jean-Jean O, and Rossignol JM
Subjects: Animals, Antibodies, Viral immunology, Cells, Cultured, Hepatitis B metabolism, Hepatitis B e Antigens metabolism, Hepatitis B virus metabolism, Hepatitis C Antigens, Humans, Radioimmunoprecipitation Assay, Substrate Specificity, Transfection, Viral Core Proteins metabolism, Viral Proteins metabolism, Hepatitis B immunology, Hepatitis B e Antigens immunology, Hepatitis B virus immunology, Viral Core Proteins immunology, Viral Proteins immunology
Abstract: In hepatitis B virus (HBV) the precore gene encodes a protein from which derives P22, the precursor of the mature secreted hepatitis B virus e antigen (HBeAg). Circumstantial evidences suggest that HBeAg and/or its precursor P22 are important for establishing persistent infection. Although P22 is essentially present in the secretory pathway, a substantial fraction has been found in the cytosol. In order to get new insights into the biological function of P22, we looked for cellular proteins which could strongly associate with this protein. Using immunoprecipitation studies on human cell extracts, we found that a non-secreted cellular protein of about 32 kDa (P32) bound with a high specificity to P22. P32 associated neither with HBeAg nor with the viral core protein P21 which exhibits the same amino acids sequence as P22 but is N-terminally shorter by 10 residues. We also demonstrated that this interaction depended on the presence of the P22 C-terminal domain. Our data argues for a potential biological function of P22.
Published: 2001
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17. The C terminus of the hepatitis B virus e antigen precursor is required for a tunicamycin-sensitive step that promotes efficient secretion of the antigen.

Author: Messageot F, Carlier D, and Rossignol JM
Subjects: Amino Acid Sequence, Cell Line, Glycosylation, Hepatitis B e Antigens chemistry, Humans, Molecular Sequence Data, Protein Precursors chemistry, Structure-Activity Relationship, Transfection, beta-Galactosidase metabolism, Antiviral Agents pharmacology, Hepatitis B e Antigens metabolism, Protein Precursors metabolism, Tunicamycin pharmacology
Abstract: The Hepatitis B virus encodes the secreted e antigen (HBe) whose function in the viral life cycle is unknown. HBe derives from a 25-kDa precursor that is directed to the secretory pathway. After cleavage of the signal sequence, the resulting 22-kDa protein (P22) is processed in a post-endoplasmic reticulum compartment to mature HBe by removal of the 34-amino acid C-terminal domain. The efficiency of HBe secretion is specifically decreased in cells grown in the presence of tunicamycin, an inhibitor of N-glycosylation. Inasmuch as HBe precursor is not N-glycosylated, our data suggest that a cellular tunicamycin-sensitive protein increases the intracellular transport through the HBe secretory pathway. The study of the secretion of HBe derived from C-terminal-truncated precursors demonstrates that the tunicamycin-sensitive secretion absolutely requires a part of the C-terminal region that is removed to form mature HBe, indicating that the cellular tunicamycin-sensitive protein increases the efficiency of the intracellular transport of P22. We have also shown that the Escherichia coli beta-galactosidase can be secreted when fused to the HBe precursor signal sequence and that the P22 C-terminal domain renders the secretion of this reporter protein also tunicamycin-sensitive.
Published: 1998
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18. Translational stop codons in the precore sequence of hepatitis B virus pre-C RNA allow translation reinitiation at downstream AUGs.

Author: Fouillot N and Rossignol JM
Subjects: Base Sequence, Cell Line, Codon, Hepatitis B virus genetics, Humans, Kidney, Open Reading Frames, RNA-Directed DNA Polymerase biosynthesis, Restriction Mapping, Transcription, Genetic, Transfection, Viral Core Proteins biosynthesis, beta-Galactosidase biosynthesis, Genes, Viral, Hepatitis B e Antigens biosynthesis, Hepatitis B virus metabolism, Protein Biosynthesis, RNA Precursors metabolism, RNA, Viral metabolism
Abstract: Hepatitis B virus (HBV) wild-type pre-C RNA directs the synthesis of the HBeAg precursor but does not serve as mRNA for translation of the adjacent downstream C gene which encodes the core protein. Using bicistronic mRNA constructs that mimick pre-C RNA, we have demonstrated that this RNA likewise does not serve as messenger for translation of the P gene, which is located downstream of the C gene. However, when the pre-C RNA contains a translational stop codon at position 2 or 28 of the pre-C sequence (as in certain HBV mutants), it no longer directs synthesis of the HBeAg precursor but instead translation is initiated at downstream C and P gene AUGs. We propose that this occurs by a translation reinitiation mechanism.
Published: 1996
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19. Importance of the C terminus of the hepatitis B virus precore protein in secretion of HBe antigen.

Author: Carlier D, Jean-Jean O, Fouillot N, Will H, and Rossignol JM
Subjects: Amino Acid Sequence, Cell Line, Transformed, Hepatitis B Core Antigens genetics, Humans, Molecular Sequence Data, Protein Precursors genetics, Sequence Deletion, Hepatitis B Core Antigens metabolism, Hepatitis B e Antigens biosynthesis, Hepatitis B virus metabolism, Protein Precursors metabolism
Abstract: The hepatitis B virus (HBV) e antigen (HBeAg) is a 15 kDa soluble antigen derived from a precursor protein (precore protein) by two processing events, cleavage of the N-terminal signal peptide and cleavage of the C-terminal 34 amino acids. So far, the role of the C-terminal sequences in secretion has not been analysed in full. In this study deletion of the last 60 amino acids was found to abrogate HBeAg secretion whereas deletions of the last 10, 25 or 39 amino acids decreased its secretion rate. These data demonstrate that C-terminal precore protein sequences are crucial for HBe secretion and determine its secretion rate.
Published: 1995
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20. Characterization and biosynthesis of the woodchuck hepatitis virus e antigen.

Author: Carlier D, Jean-Jean O, and Rossignol JM
Subjects: Amino Acid Sequence, Cell Line, Glycosylation, Hepatitis B e Antigens biosynthesis, Humans, Molecular Sequence Data, Protein Processing, Post-Translational, Recombinant Fusion Proteins chemistry, Hepatitis B Virus, Woodchuck immunology, Hepatitis B e Antigens chemistry
Abstract: The biosynthesis of the secretory core gene product of the woodchuck hepatitis virus (WHV) was studied in human cells. We have shown that the WHV e antigen was a N-glycosylated (most likely a diglycosylated) protein, with an apparent M(r) of 24K. To demonstrate that the WHV precore protein was correctly processed in human cells, we engineered chimeric proteins in which signal peptides or arginine-rich domains of WHV and hepatitis B virus (HBV) precore proteins were exchanged. Our results showed that both the signal peptide and the arginine-rich region of WHV precore protein were cleaved off during the secretion pathway, as previously reported for precore protein of human HBV and duck HBV. These observations demonstrate that the maturation process of the e antigen is conserved in hepadnaviruses. In addition, on the basis of inhibition experiments, we suggest that the cleavage of the carboxy terminus of the WHV precore protein occurred in a post-endoplasmic reticulum compartment, most likely beyond the medial Golgi, and that this cleavage was catalysed by an aspartyl protease.
Published: 1994
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21. Advantages of the scanning ion microscopy for mapping halogen corticoids in normal and transformed cells in culture.

Author: Berry JP, Chaintreau M, Chassoux D, Dennebouy R, Escaig F, Galle P, Rossignol JM, Slodzian G, and Tlouzeau S
Subjects: 3T3 Cells, Animals, Cell Nucleus ultrastructure, Flumethasone metabolism, Fluocinolone Acetonide metabolism, Humans, Mice, Spectrometry, Mass, Secondary Ion, Structure-Activity Relationship, Tumor Cells, Cultured, Cell Nucleus metabolism, Fluorine analysis, Glucocorticoids metabolism, Microscopy, Electron, Scanning methods, Steroids, Fluorinated metabolism, Triamcinolone metabolism
Abstract: The intra-cellular distribution of eight halogen glucocorticoids was investigated by ion microscopy in two cellular varieties of cultured non-cancer cells (fibroblast 3T3) and cancer cells (human breast tumor cells MCF-7). Two types of ion microscopy helped to determine this distribution, a direct imaging ion microscope (SMI 300) with low spatial resolution, and a scanning ion microscope (IMS4F), featuring high resolution, serving to obtain maps representing the intra-cellular distribution of the fluorine elements and drugs present in these monolayer cultured cells. The fluorine images representative of the drugs containing fluorine showed that these drugs are essentially concentrated in the cell nuclei. In these nuclei, the distribution of these drugs is different from that of heterochromatin and of the nucleolus.
Published: 1994
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22. Translation of the hepatitis B virus P gene by ribosomal scanning as an alternative to internal initiation.

Author: Fouillot N, Tlouzeau S, Rossignol JM, and Jean-Jean O
Subjects: Base Sequence, Capsid genetics, Cell Line, Transformed, Chloramphenicol O-Acetyltransferase genetics, Chloramphenicol O-Acetyltransferase metabolism, Cloning, Molecular, Escherichia coli genetics, Gene Deletion, Genes, Bacterial, Hepatitis B virus metabolism, Humans, Molecular Sequence Data, Plasmids, RNA, Messenger metabolism, RNA-Directed DNA Polymerase biosynthesis, Recombinant Proteins metabolism, Restriction Mapping, Sequence Homology, Nucleic Acid, beta-Galactosidase genetics, beta-Galactosidase metabolism, Genes, Viral, Genome, Viral, Hepatitis B virus genetics, Peptide Chain Initiation, Translational, Protein Biosynthesis, RNA-Directed DNA Polymerase genetics, Ribosomes metabolism, Viral Structural Proteins genetics
Abstract: The hepatitis B virus (HBV) P gene which encodes the reverse transcriptase and other proteins required for replication is expressed on the bicistronic mRNA pregenome which also encodes the capsid protein in its first cistron. Recent results have suggested that the hepadnaviral P gene is translated by internal entry of ribosomes upstream from the P gene, in the overlapping C gene. Using a reporter gene fused to the HBV C or P gene, we demonstrate that the C sequence does not allow internal initiation of translation. Alternatively, our results support a model in which the HBV P gene is translated by ribosomes which scan from the capped extremity of the bicistronic mRNA pregenome. The mechanism by which the ribosomes scan past four AUGs before they initiate translation at the P AUG was analyzed. Our results show that these AUGs are skipped via two mechanisms: leaky scanning on AUGs in a weak or suboptimal initiation context and translation of an out-of-C-frame minicistron followed by reinitiation at P AUG. The minicistron translation allows ribosomes to bypass an AUG in a favorable context that would otherwise be used as a start codon for translation of a truncated capsid protein. Our results suggest that this elaborated scanning mechanism permits the coordinate expression of the HBV C and P genes on the viral bicistronic mRNA pregenome.
Published: 1993
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23. Lack of discrimination between DNA ligases I and III by two classes of inhibitors, anthracyclines and distamycins.

Author: Montecucco A, Lestingi M, Rossignol JM, Elder RH, and Ciarrocchi G
Subjects: Animals, DNA Ligase ATP, Humans, Poly-ADP-Ribose Binding Proteins, Rats, Structure-Activity Relationship, Xenopus Proteins, Antibiotics, Antineoplastic pharmacology, DNA Ligases antagonists & inhibitors, Distamycins pharmacology
Abstract: We have measured the effects of eight distamycin and two anthracycline derivatives on polynucleotide joining and self-adenylating activities of human DNA ligase I and rat DNA ligases I and III. All test drugs show good inhibitory activity against the three enzymes in the poly[d(A-T)] joining assay. Several distamycins also inhibit the DNA-independent self-adenylation reaction catalysed by the human enzyme and, to a lesser extent, by rat DNA ligases. These results confirm that anthracyclines and distamycins express their inhibitory action against DNA joining activities mainly via specific interactions with the substrate, and suggest that the three test DNA ligases utilize similar, if not identical, mechanisms of recognition and interaction with DNA-drug complexes. Our findings also indicate that distamycins have a greater affinity for human DNA ligase I than for rat enzymes, suggesting that, in this respect, rat DNA ligase I is more similar to rat DNA ligase III than to human DNA ligase I.
Published: 1993
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24. Rat liver DNA ligases. Catalytic properties of a novel form of DNA ligase.

Author: Elder RH, Montecucco A, Ciarrocchi G, and Rossignol JM
Subjects: Adenosine Monophosphate metabolism, Animals, Binding Sites, Catalysis, DNA metabolism, Deoxyadenine Nucleotides metabolism, Electrophoresis, Agar Gel, Electrophoresis, Polyacrylamide Gel, Hot Temperature, Rats, Thionucleotides metabolism, DNA Ligases metabolism, Liver enzymology
Abstract: A novel form of rat liver DNA ligase (molecular mass 100 kDa) can be differentiated from DNA ligase I by several biochemical parameters. It is a more heat-labile enzyme and unable to join blunt-ended DNA, even in the presence of poly(ethylene glycol) concentrations which stimulate such joining by DNA ligase I and T4 DNA ligase. It also lacks the AMP-dependent nicking/closing reaction, which is a property of all other DNA ligases tested so far, including DNA ligase I from rat liver. Both rat liver DNA ligases were inhibited by deoxyadenosinetriphosphate, however this inhibition was competitive with respect to ATP, for DNA ligase I (Ki 22 microM) and non-competitive for the 100-kDa DNA ligase (Ki 170 microM). These results support the idea that, when compared with other DNA ligases, the novel form of DNA ligase has a unique AMP-binding site, may have an absolute requirement for single-strand breaks and, furthermore, may have an altered reaction mechanism to that which is conserved from bacteriophage to mammalian DNA ligase I.
Published: 1992
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25. DNA ligases from rat liver. Purification and partial characterization of two molecular forms.

Author: Elder RH and Rossignol JM
Subjects: Adenosine Monophosphate metabolism, Animals, Antibodies immunology, DNA Ligase ATP, DNA Ligases immunology, DNA Ligases metabolism, Isoenzymes immunology, Isoenzymes metabolism, Liver analysis, Molecular Weight, Phosphorus Radioisotopes, Rabbits, Rats, Sulfur Radioisotopes, DNA Ligases isolation & purification, Isoenzymes isolation & purification, Liver enzymology, Polynucleotide Ligases isolation & purification
Abstract: The differential ability of mammalian DNA ligases to use oligo(dT).poly(rA) as a substrate has been used to detect, and thereby extensively purify, two immunologically distinct forms of DNA ligase from rat liver. The activity of DNA ligase I, which is unable to use this template, is uniquely increased during liver regeneration, while that of DNA ligase II remains at a low level. Both enzymes require ATP and Mg2+ for activity and form an adenylylated intermediate which is stable and reactive. After SDS-PAGE, such radiolabeled complexes correspond to polypeptides of 130,000 and 80,000 Da for DNA ligase I and to 100,000 Da for DNA ligase II. That these labeled polypeptides do indeed correspond to active polypeptides of two different forms of DNA ligase is shown by the removal of the radiolabeled AMP, only when the intermediate is incubated with an appropriate substrate. In contrast to other eukaryotic DNA ligases, rat liver DNA ligase II has a lower Km for ATP (1.2 X 10(-5) M) than DNA ligase I (6 X 10(-5) M). Also, DNA ligase II can use ATP alpha S as a cofactor in the ligation reaction much more efficiently than DNA ligase I, further discriminating the ATP binding sites of these enzymes. Finally, antibodies raised against the 130,000-Da polypeptide of DNA ligase I specifically recognize this species in an immunoblot and inhibit only the activity of DNA ligase I.
Published: 1990
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26. The DNA polymerase from the archaebacterium Sulfolobus acidocaldarius: a thermophilic and thermoresistant enzyme which can perform automated polymerase chain reaction.

Author: Salhi S, Elie C, Jean-Jean O, Meunier-Rotival M, Forterre P, Rossignol JM, and de Recondo AM
Subjects: Adenoviruses, Human genetics, Base Sequence, DNA genetics, DNA-Directed DNA Polymerase isolation & purification, Enzyme Stability, Escherichia coli genetics, Genes, Bacterial, Genes, Viral, Hepatitis B virus genetics, Hot Temperature, Information Systems, Molecular Sequence Data, Plasmids, Restriction Mapping, Bradyrhizobiaceae enzymology, DNA-Directed DNA Polymerase metabolism, Nucleic Acid Amplification Techniques, Polymerase Chain Reaction methods
Abstract: A DNA polymerase purified from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius was used to perform automated DNA amplification at 70 degrees C as well as site directed mutagenesis by Polymerase Chain Reaction (P.C.R.). The yield of amplification performed at optimum MgCl2 concentration for the Taq or the S. acidocaldarius DNA polymerase, for the same DNA target, was equivalent. The ability of S. acidocaldarius DNA polymerase to perform P.C.R. under less stringent requirement of MgCl2 concentration gives this enzyme a non-negligible advantage over the Taq DNA polymerase.
Published: 1990
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27. DNA polymerase from Sulfolobus acidocaldarius. Replication at high temperature of long stretches of single-stranded DNA.

Author: Salhi S, Elie C, Forterre P, de Recondo AM, and Rossignol JM
Subjects: Archaea genetics, Time Factors, Bacteriophages genetics, DNA Replication, DNA, Single-Stranded, DNA-Directed DNA Polymerase metabolism, Temperature
Abstract: The activity of a homogeneous DNA polymerase from the thermophilic archaebacterium, Sulfolobus acidocaldarius, on a singly primed, single-stranded recombinant phage M13 DNA has been examined. At the optimal temperature (70 to 75 degrees C) this template is efficiently replicated in ten minutes using a ratio of enzyme molecule to primed-template of 0.8. Analysis of DNA products during the course of polymerization shows that species of quite homogeneous size are observed and that the number of primers extended by the enzyme is constant, whatever the enzyme molecule to primed template ratio is in the range 1/50 to 2, indicating that the 100 x 10(3) Mr DNA polymerase from S. acidocaldarius is randomly recycled on the template molecules. At non-optimal temperature (60 degrees C and 80 degrees C) the distribution of products observed indicated the presence of arrest sequences; some have been shown to be reversible. One of these pausing signals detected at 80 degrees C has been further analysed, and has been found to be DNA sequence-dependent.
Published: 1989

28. A rapid technique to separate DNA polymerase-alpha and -beta activity from a cytosol extract.

Author: Duguet M, Méchali M, and Rossignol JM
Subjects: Animals, Chemical Precipitation, Liver enzymology, Male, Methods, Polyethylene Glycols, Rats, Cytosol enzymology, DNA Polymerase I isolation & purification, DNA Polymerase II isolation & purification, DNA-Directed DNA Polymerase isolation & purification
Published: 1978
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29. Mammalian DNA ligase. Structure and function in rat-liver tissues.

Author: Mezzina M, Rossignol JM, Philippe M, Izzo R, Bertazzoni U, and Sarasin A
Subjects: Animals, DNA Ligases isolation & purification, Isoenzymes isolation & purification, Isoenzymes metabolism, Liver Regeneration, Macromolecular Substances, Male, Molecular Weight, Rats, Rats, Inbred Strains, DNA Ligases metabolism, Liver enzymology, Polynucleotide Ligases metabolism
Abstract: DNA ligase was partially purified from normal and regenerating rat liver. Its structure was studied using the activity gel procedure that identifies the functional polypeptides. Two slightly different purification procedures were followed leading to the isolation of one or two peaks (fractions A and B) of DNA ligase by hydroxyapatite chromatography. When analyzed on activity gels, all these enzyme fractions corresponded to a single active 130-kDa polypeptide both in normal and regenerating liver. A limited trypsin digestion of ligase fractions A and B gave rise to an identical pattern of smaller polypeptides of 110 kDa, 100 kDa and 75 kDa. Also storage at 4 degrees C of fractions A and B produced smaller polypeptides of 110 kDa, 100 kDa, 85 kDa and 60 kDa, which were identical for the two fractions. Our results indicate that the same ligase polypeptide of 130 kDa can be isolated from stationary or regenerating rat liver cells. However, physiological or artifactual proteolysis during various purification procedures can lead to the isolation of two enzyme fractions with different chromatographic behaviour but with the same molecular mass.
Published: 1987
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30. Isolation of an intact DNA polymerase-primase from embryos of Drosophila melanogaster.

Author: Kaguni LS, Rossignol JM, Conaway RC, and Lehman IR
Subjects: Animals, Centrifugation, Chromatography, DNA Primase, Drosophila melanogaster embryology, Macromolecular Substances, Molecular Weight, DNA-Directed DNA Polymerase isolation & purification, Drosophila melanogaster enzymology, RNA Nucleotidyltransferases isolation & purification
Abstract: A procedure has been devised for the purification of intact DNA polymerase alpha from early embryos of Drosophila melanogaster. The purified enzyme consists of at least three polypeptides with Mrs of 182,000, 60,000, and 50,000. These are related antigenically to the alpha (Mr 148,000), beta (Mr 58,000), and gamma (Mr 46,000) subunits, respectively, of the DNA polymerase described previously [Banks, G. R., Boezi, J. A. & Lehman, I. R. (1979) J. Biol. Chem. 254, 9886-9892]. The alpha subunit (Mr 182,000) has a molecular weight indistinguishable from that observed in extracts of freshly harvested embryos and presumably present in vivo. As in the previous preparation, the alpha subunit is required for DNA polymerase activity and is very likely the catalytic subunit of the enzyme. The ratio of primase to polymerase remains constant throughout the purification. Thus, the primase is very likely an integral component of the Drosophila DNA polymerase alpha. The purified DNA polymerase-primase contains no detectable endo- or exodeoxyribonuclease and has pH, MgCl2, (NH4)2SO4, and NaCl optima identical to those reported previously. In contrast, the Km for dTTP is 3.7 microM as compared with 17.5 microM for the previous enzyme. Sensitivities to aphidicolin and N-ethylmaleiimide and resistance to dideoxy TTP are unchanged.
Published: 1983
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31. Stimulation of rat liver alpha- and beta-type DNA polymerases by an homologous DNA-unwinding protein.

Author: Duguet M, Soussi T, Rossignol JM, Méchali M, and De Recondo AM
Subjects: Animals, Enzyme Activation, Kinetics, Magnesium pharmacology, Molecular Weight, Proteins isolation & purification, Rats, Templates, Genetic, DNA Polymerase I metabolism, DNA Polymerase II metabolism, DNA-Directed DNA Polymerase metabolism, Liver enzymology, Proteins physiology
Published: 1977
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32. Biosynthesis of hepatitis B virus e antigen: directed mutagenesis of the putative aspartyl protease site.

Author: Jean-Jean O, Salhi S, Carlier D, Elie C, De Recondo AM, and Rossignol JM
Subjects: Amino Acid Sequence, Aspartic Acid Endopeptidases, Base Sequence, Hepatitis B virus enzymology, Hepatitis B virus immunology, Information Systems, Molecular Sequence Data, Restriction Mapping, Sequence Homology, Nucleic Acid, Endopeptidases genetics, Genes, Viral, Hepatitis B e Antigens genetics, Hepatitis B virus genetics, Mutation, Viral Structural Proteins genetics
Abstract: The C gene products of all mammalian hepadnaviruses contain a region with sequence similarities to the catalytic center of the aspartyl proteases. This region could have the capacity to cleave precore proteins, leading to the synthesis of e antigen. By site-directed mutagenesis on a plasmid containing the hepatitis B virus C gene, we have replaced either the Asp residue of the putative aspartyl protease catalytic center or an Asp residue located 3 amino acids upstream. Transient expression of the mutated hepatitis B virus C gene in human and mouse cells showed that none of these mutations prevented the secretion of an accurately processed HBe antigen. Thus, we demonstrated that the aspartyl protease responsible for e antigen precursor processing is not C gene encoded but is more likely to be a cellular enzyme. From these results, we suggest a model for the mechanism of e antigen synthesis.
Published: 1989
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33. Expression mechanism of the hepatitis B virus (HBV) C gene and biosynthesis of HBe antigen.

Author: Jean-Jean O, Levrero M, Will H, Perricaudet M, and Rossignol JM
Subjects: Blotting, Western, Cells, Cultured, DNA, Viral genetics, Genetic Vectors, Hepatitis B Core Antigens biosynthesis, Molecular Weight, Peptide Hydrolases metabolism, Protein Biosynthesis, Protein Processing, Post-Translational, Genes, Viral, Hepatitis B e Antigens biosynthesis, Hepatitis B virus genetics
Abstract: The C gene of the hepatitis B virus, which contains two in-phase initiation codons delimiting the pre-C sequence and the C region, directs the synthesis of the major protein of the capsid (HBcAg) and of a precore protein which upon processing results in the secretion of the HBeAg. We used an adenovirus-based vector to study in the human 293 cell line the C gene products, the intermediates of the precore protein processing and the kind of protease involved in this processing. The synthesis of the 21-kDa HBcAg polypeptide was dependent on the deletion of the pre-C sequence suggesting that a pre-C mRNA is not used for the synthesis of the major capsid protein. With the construct containing the complete C gene, two proteins of 25 and 22 kDa were detected intracellularly, corresponding to the unprocessed and partially processed precore protein, respectively. In addition, a 15-kDa protein (HBeAg) was secreted in the culture medium. Using pepstatin, an inhibitor specific for aspartyl proteinases, reduction of HBeAg secretion and accumulation of the 22-kDa processing intermediate were observed, suggesting the involvement of an aspartyl proteinase in the conversion of the 22-kDa protein into HBeAg.
Published: 1989
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34. A DNA polymerase from a thermoacidophilic archaebacterium: evolutionary and technological interests.

Author: Elie C, Salhi S, Rossignol JM, Forterre P, and De Recondo AM
Subjects: Archaea genetics, Base Sequence, Centrifugation, Density Gradient, DNA biosynthesis, DNA, Single-Stranded, DNA-Directed DNA Polymerase isolation & purification, Drug Stability, Escherichia coli enzymology, Gene Amplification, Hot Temperature, Kinetics, Nucleic Acid Conformation, Templates, Genetic, Archaea enzymology, Bacteria enzymology, Biological Evolution, DNA-Directed DNA Polymerase metabolism
Abstract: The archaebacteria constitute a group of prokaryotes with an intermediate phylogenetic position between eukaryotes and eubacteria. The study of their DNA polymerases may provide valuable information about putative evolutionary relationships between prokaryotic and eukaryotic DNA polymerases. As a first step towards this goal, we have purified to near homogeneity a DNA polymerase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. This enzyme is a monomeric protein of 100 kDa which can catalyze DNA synthesis using either activated calf thymus DNA or oligonucleotide-primed single-stranded DNA as a template. The activity is optimal at 70 degrees C and the enzyme is thermostable up to 80 degrees C; however, it can still polymerize up to 200 nucleotides at 100 degrees C. These remarkable thermophilic properties and thermostability permit examination of the mechanism of DNA synthesis under conditions of decreased stability of the DNA helix. Furthermore, these properties make S. acidocaldarius DNA polymerase a very efficient enzyme to be used in DNA amplification by the recently developed polymerase chain reaction method (PCR) as well as in the Sanger DNA sequencing technique.
Published: 1988
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35. Expression of an enzymatically active murine retroviral reverse transcriptase in human cells.

Author: Jean-Jean O, Moyret C, Bernard D, de Recondo AM, and Rossignol JM
Subjects: Animals, Cells, Cultured, Cloning, Molecular, Endoribonucleases genetics, Gene Expression Regulation, Genetic Engineering, Humans, Immunologic Techniques, Mice, Plasmids, RNA-Directed DNA Polymerase genetics, RNA-Directed DNA Polymerase immunology, Regulatory Sequences, Nucleic Acid, Ribonuclease H, Time Factors, Endoribonucleases metabolism, RNA-Directed DNA Polymerase metabolism
Abstract: The region of the pol gene of the Moloney murine leukemia virus (M-MuLV) encoding the reverse transcriptase and RNase H activities was inserted in an eukaryotic expression vector and transiently expressed in human cultured cells. This results in the expression of high levels of reverse transcriptase activity. This enzyme, partially purified, also carries a RNase H activity, has the biochemical requirements of the viral enzyme and is recognized and inhibited by antibodies directed against a M-MuLV reverse transcriptase expressed in Escherichia coli.
Published: 1989
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36. Variation in DNA ligase structure during repair and replication processes in monkey kidney cells.

Author: Mezzina M, Franchi E, Izzo R, Bertazzoni U, Rossignol JM, and Sarasin A
Subjects: Animals, Cells, Cultured, Haplorhini, Kidney enzymology, Peptides analysis, Trypsin pharmacology, DNA Ligases analysis, DNA Repair, DNA Replication, Polynucleotide Ligases analysis
Abstract: Using a method that detects catalytically active DNA ligase in NaDodSO4-polyacrylamide gels (activity gels) we have characterized ligase produced in CV1-P monkey kidney cells infected with SV40 or treated with mitomycin C. Purification on hydroxylapatite columns of DNA ligase from control cells results in two peaks of activity called ligases I and II, respectively. Analysis of ligase I on activity gels revealed major catalytic peptides with Mr of 120, 110, 70 and 58 kDa, while analysis of ligase II revealed two major peptides of 65 and 58 kDa. Infecting CV1-P cells with SV40 produced a significant increase in the 120, 110, 70 and 58 kDa peptides while treating them with mitomycin C produced a significant increase in the 70 and 58 kDa peptides and a decrease in the 120 and 110 kDa ones. Autoproteolysis of partially purified ligase under several conditions resulted in an increase in the 58 kDa peptide and in the disappearance of other peptides. These results suggest that at least one active polypeptide is common to ligases I and II.
Published: 1985
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37. Association of DNA primase with the beta/gamma subunits of DNA polymerase alpha from Drosophila melanogaster embryos.

Author: Kaguni LS, Rossignol JM, Conaway RC, Banks GR, and Lehman IR
Subjects: Animals, Centrifugation, Density Gradient, DNA Primase, Drosophila melanogaster enzymology, Electrophoresis, Polyacrylamide Gel, Macromolecular Substances, DNA Polymerase II metabolism, DNA-Directed DNA Polymerase metabolism, Drosophila melanogaster embryology, RNA Nucleotidyltransferases metabolism
Abstract: The DNA polymerase and primase activities of the intact DNA polymerase alpha from early embryos of Drosophila melanogaster co-sediment in native glycerol gradients. However, the activities are separated in glycerol gradients containing 2.8 M urea after treatment of the enzyme with 3.4 M urea. The 182,000-dalton alpha subunit which is required for DNA polymerase activity (Kaguni, L.S., Rossignol, J.-M., Conaway, R. C., and Lehman, I.R. (1983) Proc. Natl. Acad. Sci. U. S.A. 80, 2221-2225) is not required for DNA primase activity. Instead, primase activity resides in the 60,000-dalton (beta) and/or the 50,000-dalton (gamma) subunit. Neither polymerase nor primase has been found in association with the 73,000-dalton polypeptide which co-purifies with the intact enzyme.
Published: 1983

38. Reverse transciptase activity associated with R-type virus-like particles of SV40-transformed hamster cells (TSV5 clone 2).

Author: Rossignol JM, Kress M, and de Recondo AM
Subjects: Animals, Bromodeoxyuridine pharmacology, Cell-Free System, Clone Cells, Cricetinae, DNA Nucleotidyltransferases metabolism, Dexamethasone pharmacology, Endoplasmic Reticulum microbiology, Polynucleotides metabolism, RNA Viruses ultrastructure, Simian virus 40 growth & development, Templates, Genetic, Cell Transformation, Neoplastic, RNA Viruses enzymology, RNA-Directed DNA Polymerase metabolism
Abstract: A line of hamster cells transformed by SV40 (TSV5 clone 2) contains different DNA polymerase activities. One of them has the same template specificity as viral reverse transcriptases. Partial isolation of R-type virus-like particles from TSV5 clone 2 shows that a reverse transcriptase activity is associated with these RNA viruses. This reverse transcriptase was partially purified and its biochemical properties are described.
Published: 1975
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39. [Induction, by 5-bromo-2'-deoxyuridine, of a "foamy" virus previously undetected in hamster cells transformed by SV40].

Author: Rossignol JM, Kress M, and de Vaux Saint Cyr C
Subjects: Cell Line, Cell Transformation, Neoplastic, Microscopy, Electron, RNA-Directed DNA Polymerase metabolism, Simian virus 40, Spumavirus enzymology, Bromodeoxyuridine pharmacology, RNA Viruses growth & development, Spumavirus growth & development, Virus Replication drug effects
Abstract: TSV5 clone 2 cells in normal conditions of culture contain only an expressed RNA virus (R-type virus). However, exposure of the cells to 5-bromo-2'-deoxyuridine with dexamethasone, induced synthesis of a syncitium-forming ("Foamy") virus. In other hamster cell lines, the same treatment fails to induce a "foamy" virus. The origin of this "foamy" virus is discussed.
Published: 1975

40. Rat liver DNA polymerase-beta: thermal inactivation of RNA- and DNA-dependent activities.

Author: Rossignol JM, Tillit J, and de Recondo AM
Subjects: Animals, Hot Temperature, Kinetics, Rats, DNA Polymerase I metabolism, DNA-Directed DNA Polymerase metabolism, Liver enzymology, RNA-Directed DNA Polymerase metabolism
Abstract: Purified DNA polymerase-beta from rat liver was exposed to thermal inactivation and the remaining activities were then measured either with a hybrid template such as poly(A).(dT)12-18 (R-activity) or with a DNA template such as poly(dA).(dT)12-18 (D-activity). Time course of inhibition of R- and D-activities were identical. Neither activity was protected when the thermal treatment was performed in the presence of the template or dNTPs.
Published: 1981
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41. Internal entry of ribosomes and ribosomal scanning involved in hepatitis B virus P gene expression.

Author: Jean-Jean O, Weimer T, de Recondo AM, Will H, and Rossignol JM
Subjects: Amino Acid Sequence, Base Sequence, Cell Line, DNA, Recombinant metabolism, Humans, Molecular Sequence Data, Moloney murine leukemia virus genetics, Plasmids, RNA, Messenger genetics, Restriction Mapping, Transfection, Viral Proteins genetics, Gene Expression, Genes, Viral, Hepatitis B virus genetics, Ribosomes metabolism, Transcription, Genetic, Viral Structural Proteins genetics
Abstract: The recent demonstration that the synthesis of duck hepatitis B virus (HBV) reverse transcriptase does not require translational frameshifting and the finding that poliovirus mRNA translation occurs in a cap-independent manner by internal binding of ribosomes in the 5' noncoding region led us to design experiments to test the hypothesis of internal entry of ribosomes on C gene mRNA for HBV P gene expression. We show that in human cells, translation can be initiated at the first AUG of the HBV P gene by entry of ribosomes in a region located upstream of the P gene. Moreover, the leaky scanning of ribosomes observed on the first AUG of the HBV P gene could be responsible for the synthesis of the two forms of reverse transcriptase described for HBV particles.
Published: 1989
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42. DNA polymerase alpha associated primase from rat liver: physiological variations.

Author: Philippe M, Rossignol JM, and De Recondo AM
Subjects: Animals, DNA Polymerase II isolation & purification, DNA Primase, Kinetics, Liver Regeneration, Male, RNA Nucleotidyltransferases isolation & purification, Rats, Rats, Inbred Strains, DNA Polymerase II metabolism, DNA Replication, Liver enzymology, RNA Nucleotidyltransferases metabolism
Abstract: A primase activity associated to DNA polymerase alpha from rat liver is described. Both activities were absent in normal adult rat liver but were concomitantly induced after partial hepatectomy. As previously shown for polymerase alpha and DNA topoisomerase II, primase activity reached a maximum value 40-43 h after the partial removal of the liver. Primase activity was shown to catalyze dNMP incorporation on unprimed single-stranded DNA template (M13 DNA) in the presence of rNTP. The activity was not detectable on poly(dA) or poly(dG) but was efficient on poly(dT) or poly(dC). However, the reliability of the primase assay in the presence of poly(dC) was dependent upon the degree of purification of the enzyme. The ribo primers were about 10 nucleotides long, and the reaction was completely independent of alpha-amanitin, a strong inhibitor of RNA polymerases II and III. Primase and polymerase were found tightly associated. A cosedimentation on a 5-20% sucrose gradient was always obtained, independent of the ionic strength. There was also a close coincidence between alpha-polymerase and primase activities during phosphocellulose, hydroxylapatite, and single-stranded DNA Ultrogel chromatography. It has been previously demonstrated by us and others that primase and alpha-polymerase are on separated polypeptides. The association of two activities in the replication complex and the conditions allowing their separation are discussed.
Published: 1986
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43. Synthetic template specificity of a deoxyribonucleic acid polymerase from regenerating rat liver.

Author: de Recondo AM, Lepesant JA, Fichot O, Grasset L, Rossignol JM, and Cazillis M
Subjects: Adenine Nucleotides, Ammonium Sulfate, Animals, Chemical Precipitation, Chromatography, Chromatography, DEAE-Cellulose, Cytosine Nucleotides, DNA, Single-Stranded, Hepatectomy, Hydrogen-Ion Concentration, Hydroxyapatites, Kinetics, Liver Regeneration, Male, Nucleic Acid Hybridization, Phosphorus Isotopes, Polynucleotides, Rats, Templates, Genetic, Thymine Nucleotides, Tritium, DNA Nucleotidyltransferases isolation & purification, Liver enzymology
Published: 1973

44. [DNA polymerases in rat liver: thiol groups and enzyme activity].

Author: Rossignol JM, Abadiedebat J, Tillit J, and de Recondo AM
Subjects: Animals, Carcinoma, Hepatocellular enzymology, Chloromercuribenzoates, DNA pharmacology, Dithiothreitol, Imides, Liver Neoplasms enzymology, Liver Regeneration, Maleates, Maleimides, Mercaptoethanol, Rats, Cysteine, DNA Nucleotidyltransferases, Liver enzymology
Published: 1972
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