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127 results on '"Osterberg, R."'

1. Particle size of humic acid

Author

Osterberg, R., Lindqvist, I., and Mortensen, K.

Subjects
Humic acid -- Research, Particles -- Research, Earth sciences
Abstract

The largest humic acid particles that can exist in solutions of the same acidity as most Scandinavian soil and water systems (but at a higher concentration, 1-4 mg/mL) are approximately equal to 110 nm in their largest dimension; these particles, thus, are of about the same magnitude as large viruses. This is shown by small-angle neutron scattering at 10 degrees C, pH 5, and 0.10 M ionic strength (NaCl). The mean radii of gyration of humic acids obtained from three different soil samples were found to be of the same magnitude: 21.4, 29.7, and 28.3 nm; the mean molecular masses were 500, 2000, and 1500 kDa. The radius of gyration of the cross section for the particles in solution was found to be constant, 2.1 nm; thus, the humic acid particles might essentially vary only in regard to length. A contrast variation study of one of the samples was found to be consistent with the particles in solution having a cross section with less than average scattering density in its central part. This supports the idea that the particles might contain a central 'core' with a different structure than the peripheral parts.

Published
1993

3. Atomic Force Microscopy of Humic Acids

Author

Ikai, A. and Osterberg, R.

Subjects
humic acids, particles, Atomic force microscopy, cluster-cluster interaction, size, Biology
Abstract

Atomic force microscopic (AFM) images of humic acids show discrete, globular particles, where particles of the order of magnitude 100 to 300 nm dominate the image fields; the humic acids had been grown to a steady state at pH 5.0. The AFM data are consistent with our previously reported small-angle neutron scattering (SANS) study done under similar conditions. In further agreement, the cluster-cluster interactions shown in our previous SANS study may have their counterparts in closely interacting particles appearing as twin particles in the AFM images.

Published
1996

9. PARTICLE-SIZE OF HUMIC-ACID

Author

OSTERBERG, R, LINDQVIST, I, Mortensen, Kell, OSTERBERG, R, LINDQVIST, I, and Mortensen, Kell

Published
1993

14. Conformational change of human prothrombin induced by calcium ions: an x-ray scattering study

Author

Osterberg P, Stenflo J, Osterberg R, and Sjöberg B

Subjects
Conformational change, Materials science, Distance distribution function, Protein Conformation, Scattering, X-ray, chemistry.chemical_element, Calcium, Biochemistry, Ion, Crystallography, X-Ray Diffraction, chemistry, Radius of gyration, Humans, Molecule, Prothrombin, Protein Binding
Abstract

The scattered X-ray intensities from dilute solutions of prothrombin and Ca2+-prothrombin at 21 degrees C in 0.1 M Tris-HCl buffer of pH 7.4 indicate that the prothrombin molecule attains a more extended conformation when Ca2+ ions are bound. This is indicated from the distance distribution function: the largest distance within the prothrombin molecule increases from 130 to 150 A when Ca2+ ions are bound; the radius of gyration increases from 35.5 to 39.5 A. A comparison of the experimental scattering curves with theoretical scattering curves calculated for various triaxial bodies shows that the shape of the prothrombin molecule can be represented by two ellipsoids and that the effect of Ca2+ binding can be represented by a change in the angle between their major axes.

Published
1980
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15. Small-angle X-ray scattering study of the protein complex of L7/L12 and L10 fromEscherichia coliribosomes

Author

Sjöberg B, Charles G. Kurland, Anders Liljas, Ingvar Pettersson, and Osterberg R

Subjects
Ribosomal Proteins, Macromolecular Substances, Protein Conformation, Prokaryotic initiation factor-2, Small-angle X-ray scattering, Chemistry, Stereochemistry, Biophysics, Cell Biology, Ribosomal RNA, medicine.disease_cause, Biochemistry, Ribosome, Electrophoresis, X-Ray Diffraction, Structural Biology, Escherichia coli, Genetics, medicine, Protein biosynthesis, Ribosomes, Molecular Biology, EF-Tu, Protein Binding
Abstract

The protein L12 from Escherichia coli ribosomes and its ar-aminoacetylated form L7 play a key role in protein biosynthesis [l] : they are necessary for the binding of most soluble factors, such as the initiation factor 2 (IF-2) [2], the elongation factor Tu (EF-Tu), the elongation factor G (EF-G) [3] and the release factors 1 and 2 (RF-l, RF-2) [4] to the E. coli ribosomal surface. The protein L7/Ll2 is probably present in four copies per ribosome [5-71, and previous studies of various L7/L12 preparations indicate presence of dimers in solution [8lo] . Using the small-angle X-ray scattering method, we recently reported that highly elongated dimers are the only species of L7/L12 that can be detected in solutions of the native protein [ 1 l] . In this study we have extended the previous small-angle X-ray scattering investigation on L7/Ll2 [l l] to include the complex formed between L7/ L12 and Ll 0. This L7/L12-LIO complex is normally extracted from ribosomes as a single species, which does not dissociate under the conditions of twodimensional electrophoresis; it migrates to the position denoted L8 [ 121. The complex very probably exists within the ribosome. This is indicated by the fact that L7/L12 does not rebind properly to 50 S particles when L6 and LIO have been removed or blocked by specific antibodies [ 13161. The present study deals with the molecular weight and volume

Published
1977
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16. Renal and testicular damage following dermal application of the flame retardant tris(2,3-dibromopropyl) phosphate

Author

Osterberg, R. E., Bierbower, G. W., and Hehir, R. M.

Abstract

Tris(2,3-dibromopropyl) phosphate (TRIS) was the most popular flame retardant chemical used in children's sleepwear. Acute toxicological data indicated that TRIS was low in toxicity. Since human exposure to TRIS-treated fabrics could occur for long periods of time, a subchronic study was undertaken to obtain additional information. The dermal application of TRIS (neat) at a dose of 1 ml/kg (2.27 g/kg) to the clipped backs of albino rabbits, once each week for 3 months, resulted in testicular atrophy and chronic interstitial nephritis in males. Females did not show any adverse effects.

Published
1977
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17. Dimerization of human complement proteins C3 and C4 in dilute lauryl sulfate buffer after reaction with methylamine.

Author

Osterberg, R, Nilsson, U R, and Eggertsen, G

Abstract

In the presence of methylamine and dilute lauryl sulfate (pH 8.0), the human C3 and C4 complement proteins dimerize almost completely. Under these conditions, the related complement protein C5 does not show any tendency to form dimers. This is shown by x-ray and neutron scattering at 9 degrees C and 0.15 M ionic strength. The radii of gyration of the C3 and C4 dimers are very similar, 7.7 and 7.4 nm, and the cross-sectional radii of gyration are the same, 3.4 nm. The scattering curves of the C3 and C4 dimers as well as their Fourier transforms, the p(r)-curves, can be explained by scattering from a model consisting of an elongated elliptic cylinder with semiaxes 6.5 and 2.1 nm and length of 23 nm. This elongated elliptic cylinder model is consistent with the elliptic cylinder model of C4 (Osterberg, R., Eggertsen, G., Lundwall, A., and Sjöquist, J. (1984) Int. J. Biol. Macromol. 6, 195-198) provided that the protein molecules dimerize via their cross-sectional surfaces. Also, the model is consistent with the model of the related protein, alpha 2-macroglobulin, where the four subunits are supposed to form pairwise dimers of an elliptic cylindrical form (Osterberg, R., and Malmensten, B. (1984) Eur. J. Biochem. 143, 541-544).

Published
1985
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20. 1ST CFN SYMPOSIUM LD50 AND POSSIBLE ALTERNATIVES - PROCEEDINGS OF A SYMPOSIUM HELD AT UPPSALA-BIO-MEDICAL-CENTER, SWEDEN, SEPTEMBER 15-16, 1981 - DISCUSSION

Author

Obrink, K.J., Osterberg, R., Brown, V.K., Nardone, R., Malmfors, T., Vannoordwijk, J., Johansson, K., Dayan, A., Fowler, J.S.L., Lindgren, P., Werner, B., Carstensen, J., Wold, S., Balls, M., Lindahl, E., Rothlin, B., Heilbronn, E., Carlsson, B., Holmstedt, B.R., Obrink, K.J., Osterberg, R., Brown, V.K., Nardone, R., Malmfors, T., Vannoordwijk, J., Johansson, K., Dayan, A., Fowler, J.S.L., Lindgren, P., Werner, B., Carstensen, J., Wold, S., Balls, M., Lindahl, E., Rothlin, B., Heilbronn, E., Carlsson, B., and Holmstedt, B.R.

Published
1983

21. Detergent toxicity survey.

Author

Seabaugh, V M, primary, Bayard, S P, additional, Osterberg, R E, additional, Porter, W K, additional, McCaulley, D F, additional, Hoheisel, C A, additional, Hehir, R M, additional, and Bierbower, G W, additional

Published
1977
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23. Metal and Hydrogen-Ion Binding Properties of O-Phosphoserine

Author

Osterberg R

Subjects
Hydrogen ion binding, Multidisciplinary, Chemistry, Inorganic chemistry, Biophysical Phenomena, Metal, Phosphoserine, chemistry.chemical_compound, Metals, visual_art, Ionization, Serine, visual_art.visual_art_medium, Chelation, Metal aquo complex, Hydrogen
Abstract

As pointed out by Mellander1, organic phosphoryl compounds derived from phosphoproteins may behave as effective chelating agents and therefore may be of great biological importance. For the study of the chelating ability of such compounds, synthetic model substances of similar structure are under investigation. Apparent ionization constants of synthetic O-phosphoserine, and apparent stability constants of some metal complexes of that compound have been examined.

Published
1957
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29. Combination of Tevatron searches for the standard model Higgs boson in the W+W- decay mode

Author

Maxim Perfilov, B. Carls, V. Sorin, P. Lukens, Kevin Lannon, P. Verdier, Guenakh Mitselmakher, Guillelmo Gomez-Ceballos, Marcelo Vogel, V. A. Kuzmin, U. K. Yang, Chris Hays, W. T. Fedorko, Y. A. Yatsunenko, M. Mussini, Y. C. Yang, J. Keung, G. C. Blazey, D. Torretta, A. F. Barfuss, L. Bellantoni, Viatcheslav Stolin, Frank Würthwein, M. Shochet, C. Plager, F. Canelli, V. A. Bezzubov, A. Hocker, P. D. Grannis, Jun Guo, Q. Z. Li, Mark Kruse, Alison Lister, J. P. Fernandez, J. P. Negret, J. Nett, Stefano Giagu, Paul Tipton, G. L. Strycker, C. Mesropian, R. Yamada, D. N. Brown, P. Squillacioti, Kazuhiko Hara, J. Osta, Carlos Avila, L. E. Kirsch, Ricardo Eusebi, J. Galyardt, Alexei Safonov, R. Luna-Garcia, Raimund Ströhmer, V. Simak, D. Krop, Sabine Lammers, Jonas Rademacker, D. Amidei, J. M. Heuser, J. Sekaric, Michael A. Strauss, Jean-Francois Grivaz, K. Devaughan, A. T. Goshaw, P. Padley, Michael Hildreth, P. Skubic, A. Semenov, D. Clark, J. Boudreau, Wendy Taylor, M. Pangilinan, Jason Nielsen, G. Introzzi, B. Casal, Mitchell Wayne, N. Miladinovic, Y. Tu, H. Schellman, J. M. Kohli, K. Potamianos, Z. Gunay-Unalan, Darren Price, A. Sanchez-Hernandez, M. Wiok, Sergo Jindariani, Fedor Prokoshin, P. Jonsson, Thomas Hebbeker, Katsufumi Sato, A. J. Slaughter, Stefan Grünendahl, S. Cihangir, V. Zutshi, Yasuyoshi Nagai, Francesco Crescioli, S. Uzunyan, S. W. Lee, P. Ttito-Guzmán, T. Okusawa, B. Gómez, R. Madrak, Chong-Yu Xu, J. Naganoma, B. Tuchming, P. Wagner, V. Bunichev, Shinhong Kim, J. Budagov, Fabrice Couderc, K. Makhoul, Manfred Paulini, B. Tiller, Dmitri Tsybychev, R. L. McCarthy, Thomas LeCompte, Manuela Campanelli, I. Lazzizzera, Eva Halkiadakis, M. Gold, Tetsuo Arisawa, C. Neu, Amnon Harel, W. M. Lee, K. Kondo, Mary Beth Adams, D. Whiteson, I. Shreyber, K. Yamamoto, Malte Renz, Andrew Askew, R. L. Lander, G. De Lorenzo, A. Savoy-Navarro, Allan G Clark, Roger Moore, D. O. Litvintsev, S. Söldner-Rembold, A. Anastassov, G. Giurgiu, L. Sartori, Sooran Kim, O. Poukhov, A. Jonckheere, H. E. Fisk, P. Lebrun, M. N. Mondragon, I. Hall, A. Lobodenko, Wolfgang Wagner, Liang Li, J. C. Yun, J. Lueck, Stephen Wimpenny, S. Carrillo, J. Backusmayes, Martin Grunewald, Nicola D'Ascenzo, J. A. Appel, P. H. Beauchemin, M. Heck, D. Beecher, Peter McIntyre, G. Pauletta, M. Martínez, J. Patrick, E. Strauss, Guennadi Borissov, M. Jones, C. Pagliarone, D. Menezes, Intae Yu, Oliver Stelzer-Chilton, Th Muller, D. W. Jang, R. Van Kooten, B. Y. Han, I. Heredia-De La Cruz, Michael L. Norman, Yongsun Kim, Lev Dudko, Milos Lokajicek, D. Karmanov, M. M. Deninno, Markus Wobisch, R. Magaña-Villalba, S. W. Cho, G. Obrant, B. Whitehouse, S. Y. Jun, Julia Thom, W. C. Fisher, Adrian Buzatu, V. Boisvert, Daria Zieminska, Suneel Dutt, J. E. Kim, Aran Garcia-Bellido, M. D. Corcoran, S. Cabrera, D. E. Pellett, M. Binkley, R. D. Schamberger, M. Corbo, Y. C. Chen, F. Guo, A. J. Martin, C. Vellidis, Darien Wood, Y. Shon, D. K. Cho, T. R. Wyatt, E. Brubaker, Shabnam Jabeen, S. De Cecco, A. Dubey, G. Grenier, Hwi Dong Yoo, Zdenek Hubacek, L. Santi, A. Alton, Meng Wang, Neeti Parashar, L. Pondrom, E. Wicklund, Christoph Paus, C. P. Buszello, S. Hou, A. Das, M. Sosebee, A. Manousakis-Katsikakis, Emily Nurse, M. Merkin, L. Han, Giorgio Chiarelli, A. Rahaman, J. Huston, J. D. Lewis, Yuehong Xie, T. Scanlon, S. Kermiche, W. H. Chung, M. Rominsky, L. Brigliadori, V. M. Abazov, D. Buchholz, I. Ripp-Baudot, R. McNulty, M. Hare, M. Tecchio, A. Gessler, Helio Nogima, I. Razumov, S. Blessing, M. Zielinski, V. Rusu, A. Elagin, Vyacheslav Krutelyov, G. S. Muanza, Jay Dittmann, W. Ashmanskas, D. Hirschbuehl, H. C. Fang, Frederic Deliot, Michele Gallinaro, G. Savage, Peter Wittich, A. Napier, A. Meyer, Scott Snyder, J. Hays, S. Tokar, Suman Bala Beri, C.S. Johnson, G. Sajot, V. Hynek, Robert Hirosky, Alberto Annovi, P. Murat, Y. Hu, D. J. Cox, A. Di Canto, V. Khotilovich, Y. Seiya, O. Atramentov, Elizaveta Shabalina, M. Lancaster, G. Alkhazov, Y. Zheng, Jian Tang, L. Oakes, A. Gresele, Y. N. Kharzheev, A. Varganov, Sudhir Malik, E. G. Zverev, M. Vidal, Ia Iashvili, G. Manca, P. Roy, Raymond Brock, Robin Erbacher, M. Datta, R. Beuselinck, C. Cuenca Almenar, Javier Cuevas, Jean-Arcady Meyer, J. Mülmenstädt, D. V. Bandurin, S. Greder, Y. W. Liu, Iain Alexander Bertram, Virgil E Barnes, M. Padilla, L. Bagby, M. S. Rangel, Jahred Adelman, Jane Nachtman, Graham Wilson, Sergio F Novaes, S. Hossain, B. Jayatilaka, Kyung-Suk Cho, R. E. Hughes, P. Rich, T. Rodriguez, D. Gillberg, H. Wolfe, B. Sanghi, Suyong Choi, J. Parsons, G. Velev, J. M. Hauptman, Cecilia Elena Gerber, V. M. Podstavkov, G. Chlachidze, Michael Rijssenbeek, S. Zelitch, Jeannine Wagner-Kuhr, M. A. Strang, Brajesh C Choudhary, D. Lucchesi, Bernd Stelzer, S. Tkaczyk, F. Vázquez, P. Svoisky, C. Zeitnitz, J. Yamaoka, Arnulf Quadt, Petar Maksimovic, A. Juste, E. De La Cruz-Burelo, A. Attal, E. Pueschel, T. Wright, S. Grinstein, Todd Adams, K. M. Chan, A. S. Ito, A. Melnitchouk, T. Aaltonen, J. Antos, Thorsten Chwalek, Elemer Nagy, C. J. Lin, W. M. Van Leeuwen, M. Fortner, Sarah Catherine Eno, Horst Severini, Tiehui Liu, Rodolfo Carosi, A. Barbaro-Galtieri, R. G. Feild, J. S. Suh, K. Osterberg, D. Mietlicki, S. Richter, Michal Kreps, T. Nunnemann, B. Baldin, Corrinne Mills, G. P. Yeh, C. S. Moon, M. J. Kim, S. J. Park, A. Menzione, M. E. Convery, E. Palencia, J. C. Cully, Aron Soha, M. Cordelli, G. Busetto, Brian L Winer, G. Ginther, G. Bauer, G. Golovanov, M. J. Morello, F. D. Snider, J. Y. Han, N. Giokaris, Junjie Zhu, S. Wolbers, V. V. Tokmenin, L. S. Vertogradov, R. J. Miller, J. Martínez-Ortega, M. Weinberger, Bjoern Penning, G. Facini, M. Kurata, Andrea Castro, G. D. Alexeev, Flera Rizatdinova, M. Milnik, U. Husemann, B. Álvarez González, V. N. Evdokimov, A. Bridgeman, K. Sliwa, S. Klimenko, Evelyn Thomson, C. Deluca, Fabrizio Scuri, D. Wicke, Dennis Stephen Mackin, Andrew Brandt, Kirti Ranjan, Jianming Qian, J. L. Gimmell, V. V. Lipaev, J. Lellouch, H. A. Neal, Ivan-Kresimir Furic, Y. D. Oh, D. Bauer, M. C. Cousinou, V. A. Giakoumopoulou, Carsten Hensel, A. Mukherjee, C. Belanger-Champagne, B. S. Acharya, Nicola Turini, J. Pursley, H. Nilsen, R. G. Wagner, B. Spurlock, G. Piacentino, M. Buehler, A. T. Laasanen, Zeno Dixon Greenwood, Y. Arnoud, Richard B. Lipton, D. W. Gerdes, Pedro G Mercadante, Ph Gris, T. Kuhr, P. Houben, M. H. Kirby, H. Miyake, F. Happacher, Kristian Harder, Dario Bisello, G. Gutierrez, M. D'Errico, Joe Kroll, B. C.K. Casey, X. Wu, T. A. Schwarz, A. Bhatti, P. A. Kasper, Hugh Williams, M. P. Sanders, Ignacio Redondo, Hyun-Chul Kim, Yurii Maravin, Vladimir Gavrilov, A. Aurisano, Teresa Rodrigo, D. Boline, K. Chung, Peter Love, Pushpalatha C Bhat, W. Geng, N. Ranjan, R. Jesik, S. Carron, L. Demortier, S. Dube, S. H. Oh, M. A. Schmidt, Mark Richard James Williams, R. Bernhard, W. E. Cooper, P. N. Dong, D. Khatidze, Giovanni Bellettini, M. Rossi, J. Slaunwhite, D. Cutts, J. T. Linnemann, David T. Johnston, Gordon Watts, Daniela Bortoletto, O. Mundal, K. Yip, P. E. Karchin, P. Haefner, Roman Lysak, M. Iori, C. Bromberg, Duncan Carlsmith, K. A. Johns, Anna Goussiou, Elisabetta Pianori, A. V. Kotwal, Gregorio Bernardi, Andrea Bocci, D. Denisov, X. Zhang, A. Scribano, D. Onoprienko, T. J. Phillips, A. A. Paramanov, K. Ebina, G. Otero y Garzon, M. Trovato, M. Cavalli-Sforza, W. M. Yao, Aaron Dominguez, Jochen Jens Heinrich, W. Geist, Tiefu Zhao, S. Budd, G. A. Thompson, Je Jung, S. W. Youn, P. Polozov, Koji Nakamura, Arnaud Duperrin, S. Neubauer, S. Y. Tsai, Sharon Hagopian, S. Torre, S. Amerio, S. Zucchelli, A. K.A. Maciel, W. Johnson, K. T. Pitts, A. Simonenko, V. Sirotenko, S. Wilbur, J. K. Kraus, J. Weinelt, Greg Landsberg, I. Suslov, K. Herner, N. Khalatyan, S. Yacoob, A. Schmidt, B. Hoeneisen, Lee Sawyer, Maria Agnese Ciocci, A. Mitra, Michael Schmitt, N. Kimura, Hal Evans, Thomas Ferbel, M. Prewitt, Cristina Galea, M. Hartz, T. Wakisaka, Lars Sonnenschein, Zhanqiang Liu, M. Cooke, Tommaso Dorigo, S. Hewamanage, Sinead Farrington, M. P. Schmidt, P. L.M. Podesta-Lerma, D. H. Kim, V. Kaushik, J. F. Bartlett, J. Lys, Stephan Lammel, Lucio Cerrito, R. E. Blair, Jong-Sung Yu, F. Rimondi, Pavol Bartos, N. Ershaidat, E. E. Boos, E. E. Schmidt, Marco Verzocchi, Theodoros Christoudias, S. Lami, Emanuela Barberis, Avraham Yagil, Dean Hidas, Heriberto Castilla-Valdez, J. Morlock, S. Seidel, R. Unalan, L. Stutte, A. Canepa, C. Ferrazza, C. P. Marino, G. Flanagan, A. N. Sisakyan, E. Rogers, P. Totaro, R. Nayyar, Robert Kehoe, Maxwell Chertok, A. Patwa, W. Badgett, J. Clutter, Md. Naimuddin, V. Papadimitriou, M. Kirsch, A.S. Dyshkant, D. Smirnov, George Alverson, K. Tollefson, E. J. Jeon, A. Sukhanov, R. Vilar, N. Krumnack, P. K. Teng, K. S. McFarland, Federico Sforza, Mark Owen, S. Somalwar, Deepak Kar, R. Piegaia, V. V. Glagolev, MarioPaolo Giordani, S. J. De Jong, K. Soustruznik, Ashok Kumar, E. Carrera, I. Bizjak, J. Conway, E. Lee, M. Stanitzki, A. Papaikonomou, M. E. Mattson, M. Arov, Andre Sopczak, G. Hesketh, B. Brau, D. Hedin, Brad Abbott, P. Catastini, T. Tomura, A. Evdokimov, S. Pagan Griso, Robert Snihur, Marcia Begalli, Ulysses Grundler, C. I. Ciobanu, R. L. Wagner, Jiri Kvita, D. Gerbaudo, D. Lam, S. Z. Shalhout, Victoria Jane Martin, R. Martínez-Ballarín, Thomas Peiffer, Alexander Grohsjean, Phillip Gutierrez, Pierre Petroff, A. Golossanov, Shih-Fu Chang, Rainer Wallny, M. Demarteau, Andreas Warburton, Satoru Uozumi, U. Bassler, Andrew Beretvas, R. F. Harr, M. Mathis, Meenakshi Narain, A. Pronko, Arie Bodek, S. Moed, P. J. Van Den Berg, Lev Uvarov, Marc Besancon, D. Benjamin, K. Goulianos, J. Snow, M. Abolins, S. Rolli, Elliott Cheu, T. Schliephake, A. Taffard, Victor Daniel Elvira, Marvin Johnson, K. Peters, Sung Keun Park, Massimo Casarsa, Sergey Burdin, S. Robinson, J. Deng, Gregory R Snow, A. A. Shchukin, P. Movilla Fernandez, M. Shimojima, J. P. Chou, Heimo Saarikko, A. Sedov, M. A. Carrasco-Lizarraga, M. Feindt, M. Eads, Y. Takeuchi, Regina Demina, J. Strologas, C. Calancha, B. Di Ruzza, P. Sinervo, P. Schlabach, S. P. Denisov, V. Parihar, Frank Fiedler, A. L. Lyon, Philip Baringer, F. Garberson, H. W. Kim, N. K. Mondal, Mauro Dell'Orso, Tulika Bose, S. Pashapour, A. Apresyan, E. Kajfasz, Song-Ming Wang, A. V. Kozelov, Samuel Calvet, H. T. Diehl, T. A. Bolton, P. Neustroev, V. Saveliev, F. Azfar, R. Culbertson, C. Haber, O. Norniella, V. V. Shary, A. Boehnlein, M. Lindgren, J. Piper, S. Banerjee, E. Vataga, Dorothee Schaile, Michael Mulhearn, R. St. Denis, J. R. Smith, G. B. Yu, J. Ellison, W. Ketchum, D. Hare, G. Williams, D. Edmunds, Igor Volobouev, Jeroen Hegeman, J. Linacre, T. Moulik, P. de Barbaro, Avto Kharchilava, C. A. Cox, Fumihiko Ukegawa, Sa. Jain, A. Penzo, S. Fuess, K. K. Joo, T. Kurca, Marc Weber, B. Parks, James Russ, Kohei Yorita, T. Hoang, Franco Bedeschi, R. Otec, D. Glenzinski, Alexander Khanov, Jonas Strandberg, P. B. Renton, J. Orduna, S. S. Yu, Tomoko Yoshida, A. B. Wicklund, D. Jamin, Grigory Safronov, S. Chevalier-Théry, J. Thome, S. Chakrabarti, V. Cavaliere, D. Waters, M. Hohlfeld, P. N. Ratoff, D. Toback, Y. Peters, P. Vint, Zhenyu Ye, Maksym Titov, Yuri Gershtein, N. P. Kulkarni, Y. Zeng, P. Rubinov, Daniel Duggan, Ernest Aguilo, Tara Shears, Hua-Lei Yin, A. V. Popov, W. C. Wester, M. Campbell, D. Stentz, A. Loginov, S. Desai, T. Dorland, D. Dagenhart, M. Jaffré, Gustaaf Brooijmans, M. Rescigno, L. S. Ancu, Petr Vokac, Joseph Haley, J. Warchol, P. Lujan, P. Garosi, Christophe Royon, V. Ramakrishnan, Alexander Leflat, J. Asaadi, Y. S. Chung, E. Camacho-Pérez, C. Wolfe, P. Barria, E. James, B. Calpas, L. Lovas, Reinhard Schwienhorst, S. Behari, Luca Scodellaro, H. D. Wahl, Alexander Kupco, F. Badaud, K. L. Byrum, P. Giromini, Andrew White, Gilvan Alves, L. Sexton-Kennedy, R. Forrest, I. Katsanos, Anna Zanetti, G. Compostella, Maxim Goncharov, N. Huske, N. Parua, D. 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Kwang, M. Hurwitz, S. R. Hahn, M. Vesterinen, N. Osman, A. Deisher, T. R. Junk, Patrick Slattery, A. Chandra, J. Yoh, D. A. Stoyanova, C. L. McGivern, Gervasio Gomez, Michael Begel, Andrey Korytov, Eduardo De Moraes Gregores, Luiz Mundim, R. Takashima, T. H. Burnett, Amitabh Lath, Anna Sfyrla, Paola Giannetti, B. A. Barnett, Giorgio Apollinari, J. A. Benitez, Teruki Kamon, P. Mazzanti, Craig Blocker, Ulrich Heintz, D. Cauz, Kaori Maeshima, P. K. Mal, H. S. Lee, Frank Filthaut, Paolo Mastrandrea, M. Diesburg, P. Wilson, J. E. Garcia, A. Tanasijczuk, T. Davies, C. S. Hill, Sandra Leone, S. Uvarov, B. Quinn, W. K. Sakumoto, C. Schwanenberger, Alice Bean, C. Grosso-Pilcher, I. Oksuzian, N. Goldschmidt, Volker Buescher, Peter Bussey, T. Gadfort, Maria Elena Pol, Kai Yi, C. M. Ginsburg, R. Roser, Ivan Vila, P. F. Shepard, B. Rutherford, Alexander Ivanov, N. Van Remortel, S. C. Hsu, Reisaburo Tanaka, Guido Volpi, Nikos Varelas, O. González, Bing Zhou, Luis Mendoza, R. K. Shivpuri, S. Donati, Kenichi Hatakeyama, M. Franklin, D. R. Claes, Gavin Davies, Philippe Calfayan, Itsuo Nakano, Harald Fox, S. M. Lietti, Y. Scheglov, J. C. Freeman, Kaushik De, A. Ruiz, Giuseppe Latino, Alan Garfinkel, Jan Stark, Fabrizio Margaroli, S. Errede, Maiko Takahashi, Henry Lubatti, J. Cammin, I. A. Vasilyev, Vipin Bhatnagar, A. Cerri, R. Partridge, Markus Frank, P. M. Tuts, D. MacQueen, H. Gerberich, Kenneth Bloom, V. L. Malyshev, Mark Neubauer, R. Orava, G. Lungu, R. D. Field, D. J. Kong, W. C. Yang, Department of Physics, Helsinki Institute of Physics, CDF Collaboration, D0 Collaboration, Laboratoire de Physique Subatomique et de Cosmologie (LPSC), Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Institut Polytechnique de Grenoble - Grenoble Institute of Technology-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Université Joseph Fourier - Grenoble 1 (UJF)-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), 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), Institut de Recherches sur les lois Fondamentales de l'Univers (IRFU), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, Laboratoire de Physique Nucléaire et de Hautes Énergies (LPNHE), Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Université Pierre et Marie Curie - Paris 6 (UPMC), 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), Institut de Physique Nucléaire de Lyon (IPNL), Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3), CDF, D0, Université Joseph Fourier - Grenoble 1 (UJF)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Institut Polytechnique de Grenoble - Grenoble Institute of Technology-Centre National de la Recherche Scientifique (CNRS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Université Paris Diderot - Paris 7 (UPD7)-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), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Universidad de Cantabria, T. 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LOVE, H. J. LUBATTI, D. LUCCHESI, J. LUECK, P. LUJAN, P. LUKENS, R. LUNA-GARCIA, G. LUNGU, A. L. LYON, R. LYSAK, J. LYS, A. K. A. MACIEL, D. MACKIN, D. MACQUEEN, R. MADRAK, K. MAESHIMA, R. MAGAÑA-VILLALBA, K. MAKHOUL, P. MAKSIMOVIC, P. K. MAL, S. MALDE, S. MALIK, S. MALIK, V. L. MALYSHEV, G. MANCA, A. MANOUSAKIS-KATSIKAKIS, Y. MARAVIN, F. MARGAROLI, C. MARINO, C. P. MARINO, A. MARTIN, V. MARTIN,E, M. MARTÍNEZ, R. MARTÍNEZ-BALLARÍN, J. MARTÍNEZ-ORTEGA, P. MASTRANDREA, M. MATHIS, P. MÄTTIG, M. E. MATTSON, P. MAZZANTI, R. MCCARTHY, K. S. MCFARLAND, C. L. MCGIVERN, P. MCINTYRE, R. MCNULTY, A. MEHTA, P. MEHTALA, M. M. MEIJER, A. MELNITCHOUK, L. MENDOZA, D. MENEZES, A. MENZIONE, P. G. MERCADANTE, M. MERKIN, C. MESROPIAN, A. MEYER, J. MEYER, T. MIAO, D. MIETLICKI, N. MILADINOVIC, R. MILLER, C. MILLS, M. MILNIK, A. MITRA, G. MITSELMAKHER, H. MIYAKE, S. MOED, N. MOGGI, N. K. MONDAL, M. N. MONDRAGON, C. S. MOON, R. MOORE, M. J. MORELLO, J. MORLOCK, T. MOULIK, P. MOVILLA FERNANDEZ, G. S. MUANZA, A. MUKHERJEE, M. MULHEARN, TH. MULLER, J. MÜLMENSTÄDT, O. MUNDAL, L. MUNDIM, P. MURAT, M. MUSSINI, J. NACHTMAN,I, Y. NAGAI, J. NAGANOMA, E. NAGY, M. NAIMUDDIN, K. NAKAMURA, I. NAKANO, A. NAPIER, M. NARAIN, R. NAYYAR, H. A. NEAL, J. P. NEGRET, J. NETT, C. NEU, M. S. NEUBAUER, S. NEUBAUER, P. NEUSTROEV, J. NIELSEN, H. NILSEN, L. NODULMAN, H. NOGIMA, M. NORMAN, O. NORNIELLA, S. F. NOVAES, T. NUNNEMANN, E. NURSE, L. OAKES, G. OBRANT, S. H. OH, Y. D. OH, I. OKSUZIAN, T. OKUSAWA, D. ONOPRIENKO, R. ORAVA, J. ORDUNA, N. OSMAN, J. OSTA, K. OSTERBERG, R. OTEC, G. J. OTERO Y GARZÓN, M. OWEN, M. PADILLA, P. PADLEY, S. PAGAN GRISOB,A, C. PAGLIARONE, E. PALENCIA, M. PANGILINAN, V. PAPADIMITRIOU, A. PAPAIKONOMOU, A. A. PARAMANOV, N. PARASHAR, V. PARIHAR, S.-J. PARK, S. K. PARK, B. PARKS, J. PARSONS, R. PARTRIDGE, N. PARUA, S. PASHAPOUR, J. PATRICK, A. PATWA, G. PAULETTA, M. PAULINI, C. PAUS, T. PEIFFER, D. E. PELLETT, B. PENNING, A. PENZO, M. PERFILOV, K. PETERS, Y. PETERS, P. PÉTROFF, T. J. PHILLIPS, G. PIACENTINO, E. PIANORI, R. PIEGAIA, L. PINERA, J. PIPER, K. PITTS, C. PLAGER, M.-A. PLEIER, P. L. M. PODESTA-LERMA, V. M. PODSTAVKOV, M.-E. POL, P. POLOZOV, L. PONDROM, A. V. POPOV, K. POTAMIANOS, O. POUKHOV, M. PREWITT, D. PRICE, F. PROKOSHIN,U, A. PRONKO, S. PROTOPOPESCU, F. PTOHOS, E. PUESCHEL, G. PUNZI, J. PURSLEY, J. QIAN, A. QUADT, B. QUINN, J. RADEMACKER,§, A. RAHAMAN, V. RAMAKRISHNAN, M. S. RANGEL, K. RANJAN, N. RANJAN, P. N. RATOFF, I. RAZUMOV, I. REDONDO, P. RENKEL, P. RENTON, M. RENZ, M. RESCIGNO, P. RICH, S. RICHTER, M. RIJSSENBEEK, F. RIMONDI, I. RIPP-BAUDOT, L. RISTORIA, F. RIZATDINOVA, S. ROBINSON, A. ROBSON, T. RODRIGO, T. RODRIGUEZ, E. ROGERS, S. ROLLI, M. ROMINSKY, R. ROSER, M. ROSSIA, R. ROSSIN, P. ROY, C. ROYON, P. RUBINOV, R. RUCHTI, A. RUIZ, J. RUSS, V. RUSU, B. RUTHERFORD, H. SAARIKKO, A. SAFONOV, G. SAFRONOV, G. SAJOT, W. K. SAKUMOTO, A. SÁNCHEZ-HERNÁNDEZ, M. P. SANDERS, B. SANGHI, L. SANTI, L. SARTORIA, K. SATO, G. SAVAGE, V. SAVELIEV, A. SAVOY-NAVARRO, L. SAWYER, T. SCANLON, D. SCHAILE, R. D. SCHAMBERGER, Y. SCHEGLOV, H. SCHELLMAN, P. SCHLABACH, T. SCHLIEPHAKE, S. SCHLOBOHM, A. SCHMIDT, E. E. SCHMIDT, M. A. SCHMIDT, M. P. SCHMIDT, M. SCHMITT, C. SCHWANENBERGER, T. SCHWARZ, R. SCHWIENHORST, L. SCODELLARO, A. SCRIBANO, F. SCURIA, A. SEDOV, S. SEIDEL, Y. SEIYA, J. SEKARIC, A. SEMENOV, H. SEVERINI, L. SEXTON-KENNEDY, F. SFORZA, A. SFYRLA, E. SHABALINA, S. Z. SHALHOUT, V. SHARY, A. A. SHCHUKIN, T. SHEARS, P. F. SHEPARD, M. SHIMOJIMA,O, S. SHIRAISHI, R. K. SHIVPURI, M. SHOCHET, Y. SHON, I. SHREYBER, V. SIMAK, A. SIMONENKO, P. SINERVO, V. SIROTENKO, A. SISAKYAN, P. SKUBIC, P. SLATTERY, A. J. SLAUGHTER, J. SLAUNWHITE, K. SLIWA, D. SMIRNOV, J. R. SMITH, F. D. SNIDER, R. SNIHUR, G. R. SNOW, J. SNOW, S. SNYDER, A. SOHA, S. SÖLDNER-REMBOLD, S. SOMALWAR, L. SONNENSCHEIN, A. SOPCZAK, V. SORIN, M. SOSEBEE, K. SOUSTRUZNIK, B. SPURLOCK, P. SQUILLACIOTIC,A, M. STANITZKI, J. STARK, R. ST. DENIS, B. STELZER, O. STELZER-CHILTON, D. STENTZ, V. STOLIN, D. A. STOYANOVA, J. STRANDBERG, M. A. STRANG, E. STRAUSS, M. STRAUSS, R. STRÖHMER, J. STROLOGAS, D. STROM, G. L. STRYCKER, L. STUTTE, J. S. SUH, A. SUKHANOV, I. SUSLOV, P. SVOISKY, A. TAFFARD, M. TAKAHASHI, R. TAKASHIMA, Y. TAKEUCHI, R. TANAKA, A. TANASIJCZUK, J. TANG, W. TAYLOR, M. TECCHIO, P. K. TENG, J. THOM, J. THOME, G. A. THOMPSON, E. THOMSON, B. TILLER, P. TIPTON, M. TITOV, S. TKACZYK, D. TOBACK, S. TOKAR, V. V. TOKMENIN, K. TOLLEFSON, T. TOMURA, D. TONELLI, S. TORRE, D. TORRETTA, P. TOTARO, M. TROVATO, S.-Y. TSAI, D. TSYBYCHEV, P. TTITO-GUZMÁN, B. TUCHMING, Y. TU, C. TULLY, N. TURINI, P. M. TUTS, F. UKEGAWA, R. UNALAN, S. UOZUMI, L. UVAROV, S. UVAROV, S. UZUNYAN, P. J. VAN DEN BERG, R. VAN KOOTEN, W. M. VAN LEEUWEN, N. VAN REMORTEL, N. VARELAS, A. VARGANOV, E. W. VARNES, I. A. VASILYEV, E. VATAGAD,A, F. VÁZQUEZ,H, G. VELEV, C. VELLIDIS, P. VERDIER, L. S. VERTOGRADOV, M. VERZOCCHI, M. VESTERINEN, M. VIDAL, I. VILA, D. VILANOVA, R. VILAR, P. VINT, M. VOGEL, P. VOKAC, I. VOLOBOUEV,S, G. VOLPI, P. WAGNER, R. G. WAGNER, R. L. WAGNER, W. WAGNER,W, J. WAGNER-KUHR, H. D. WAHL, T. WAKISAKA, R. WALLNY, M. H. L. S. WANG, S. M. WANG, A. WARBURTON, J. WARCHOL, D. WATERS, G. WATTS, M. WAYNE, G. WEBER, M. WEBER, M. WEINBERGER, J. WEINELT, W. C. WESTER, III, M. WETSTEIN, A. WHITE, B. WHITEHOUSE, D. WHITESON, D. WICKE, A. B. WICKLUND, E. WICKLUND, S. WILBUR, G. WILLIAMS, H. H. WILLIAMS, M. R. J. WILLIAMS, G. W. WILSON, P. WILSON, S. J. WIMPENNY, B. L. WINER, P. WITTICH, M. WOBISCH, S. WOLBERS, C. WOLFE, H. WOLFE, D. R. WOOD, T. WRIGHT, X. WU, F. WÜRTHWEIN, T. R. WYATT, Y. XIE, C. XU, S. YACOOB, A. YAGIL, R. YAMADA, K. YAMAMOTO, J. YAMAOKA, U. K. YANG,M, W.-C. YANG, Y. C. YANG, W. M. YAO, T. YASUDA, Y. A. YATSUNENKO, Z. YE, G. P. YEH, K. YI,I, H. YIN, K. YIP, J. YOH, H. D. YOO, K. YORITA, T. YOSHIDA,F, S. W. YOUN, G. B. YU, I. YU, J. YU, S. S. YU, J. C. YUN, A. ZANETTIA, C. ZEITNITZ, S. ZELITCH, Y. ZENG, X. ZHANG, T. ZHAO, Y. ZHENG, B. ZHOU, J. ZHU, M. ZIELINSKI, D. ZIEMINSKA, L. ZIVKOVIC, S. ZUCCHELLI, V. ZUTSHI, E. G. ZVEREV, D0 (Tevatron, IHEF, IOP, FNWI), Universidad de Buenos Aires, Centro Brasileiro de Pesquisas Físicas, Universidade do Estado do Rio de Janeiro (UERJ), Universidade Federal do ABC (UFABC), Universidade Estadual Paulista (UNESP), McGill University, Simon Fraser University, University of Science and Technology of China, Academia Sinica, Universidad de los Andes, Faculty of Mathematics and Physics, Czech Technical University in Prague, Academy of Sciences, Universidad San Francisco de Quito, University of Helsinki, CNRS/IN2P3, Institut National Polytechnique de Grenoble, Irfu/SPP, RWTH Aachen University, Universität Bonn, Universität Freiburg, Georg-August-Universität Göttingen, Karlsruhe Institute of Technology, Universität Mainz, Ludwig-Maximilians-Universität München, University of Wuppertal, University of Athens, Panjab University, Delhi University, Tata Institute of Fundamental Research, University College Dublin, Istituto Nazionale di Fisica Nucleare Bologna, University of Bologna, Istituto Nazionale di Fisica Nucleare, Sezione di Padova-Trento, University of Padova, Istituto Nazionale di Fisica Nucleare Pisa, University of Pisa, University of Siena, Scuola Normale Superiore, Sezione di Roma 1, Sapienza Università di Roma, Istituto Nazionale di Fisica Nucleare Trieste/Udine, University of Trieste, Okayama University, Osaka City University, University of Tsukuba, Waseda University, Kyungpook National University, Korea University, SungKyunKwan University, CINVESTAV, NIKHEF, Radboud University Nijmegen/NIKHEF, Joint Institute for Nuclear Research, Institution for Theoretical and Experimental Physics, Moscow State University, Institute for High Energy Physics, Petersburg Nuclear Physics Institute, Comenius University, Universitat Autonoma de Barcelona, Medioambientales y Tecnologicas, University of Cantabria, Stockholm University, University of Geneva, Glasgow University, Lancaster University, University of Liverpool, Imperial College London, University College London, The University of Manchester, University of Oxford, University of Arizona, Ernest Orlando Lawrence Berkeley National Laboratory, University of California, Yale University, University of Florida, Florida State University, Argonne National Laboratory, Fermi National Accelerator Laboratory, University of Chicago, University of Illinois at Chicago, Northern Illinois University, Northwestern University, University of Illinois, Indiana University, Purdue University Calumet, University of Notre Dame, Purdue University, Iowa State University, University of Kansas, Kansas State University, Louisiana Tech University, The Johns Hopkins University, University of Maryland, Boston University, Northeastern University, Harvard University, Massachusetts Institute of Technology, Tufts University, Brandeis University, University of Michigan, Wayne State University, Michigan State University, University of Mississippi, University of Nebraska, Rutgers University, Princeton University, University of New Mexico, State University of New York, Columbia University, The Rockefeller University, University of Rochester, Brookhaven National Laboratory, Duke University, The Ohio State University, Langston University, University of Oklahoma, Oklahoma State University, University of Pennsylvania, Carnegie Mellon University, University of Pittsburgh, Brown University, University of Texas, Texas A and M University, Southern Methodist University, Rice University, Baylor University, University of Virginia, University of Washington, University of Wisconsin, Sezione di Cagliari, University of Toronto, TRIUMF, York University, Seoul National University, Sungkyunkwan University, Institute of Science and Technology Information, Chonnam National University, Chonbuk National University, Institute of Experimental Physics, University of Cyprus, University of Edinburgh, Fukui Prefecture, Kinki University, Universidad Iberoamericana, University of Iowa, University of California Irvine, Cornell University, University of London, University of Manchester, Inc., Nagasaki Institute of Applied Science, Obninsk State University, University de Oviedo, Texas Tech University, CSIC-Universitat de Valencia, Universidad Tecnica Federico Santa Maria, Bergische Universität Wuppertal, Yarmouk University, J. Stefan Institute, Augustana College, SLAC, ICREA/IFAE, Centro de Investigacion en Computacion-IPN, Universidad Autonoma de Sinaloa, Universiẗt Bern, University of Massachusetts Amherst, Universiteit Antwerpen, University of Bristol, University of California Santa Cruz, Chinese Academy of Sciences, Clark, Allan Geoffrey, Garcia Navarro, Jose Enrique, Lister, Alison, and Wu, Xin

Subjects
Particle physics, Astrophysics::High Energy Astrophysical Phenomena, Tevatron, FOS: Physical sciences, General Physics and Astronomy, Elementary particle, ddc:500.2, PARTON DISTRIBUTIONS, HADRON COLLIDERS, QCD, NNLO, 7. Clean energy, 01 natural sciences, 114 Physical sciences, High Energy Physics - Experiment, Standard Model, Nuclear physics, High Energy Physics - Experiment (hep-ex), Particle decay, 0103 physical sciences, [PHYS.HEXP]Physics [physics]/High Energy Physics - Experiment [hep-ex], Grand Unified Theory, Fermilab, TEVATRON, Nuclear Experiment, 010306 general physics, Boson, Physics, HIGGS BOSON, 010308 nuclear & particles physics, High Energy Physics::Phenomenology, 3. Good health, Higgs boson, CDF, Physics::Accelerator Physics, High Energy Physics::Experiment, +W%2B+W-+|+W%3A+pair+production+|+W%3A+leptonic+decay+|+dilepton%3A+final+state+|+jet%3A+multiplicity+|+cross+section%3A+upper+limit+|+mass+dependence+|+Higgs+particle%3A+mass+|+background+|+DZERO+|+CDF+|+Batavia+TEVATRON+Coll+|+anti-p+p+-->+Higgs+particle+anything+|+anti-p+p+-->+Higgs+particle+anything+intermediate+boson+anything+|+anti-p+p+-->+Higgs+particle+anything+quark+antiquark+anything+|+1960+GeV-cms%22">Anti-p p: interaction | Higgs particle: search for | gluon gluon: fusion | intermediate boson: fusion | quark antiquark: annihilation | Higgs particle: decay | Higgs particle --> W+ W- | W: pair production | W: leptonic decay | dilepton: final state | jet: multiplicity | cross section: upper limit | mass dependence | Higgs particle: mass | background | DZERO | CDF | Batavia TEVATRON Coll | anti-p p --> Higgs particle anything | anti-p p --> Higgs particle anything intermediate boson anything | anti-p p --> Higgs particle anything quark antiquark anything | 1960 GeV-cms
Abstract

11 páginas, 4 figuras, 1 tabla.-- CDF Collaboration: et al., We combine searches by the CDF and D0 Collaborations for a Higgs boson decaying to W+W-. The data correspond to an integrated total luminosity of 4.8 (CDF) and 5.4 (D0) fb(-1) of p (p) over bar collisions at root s = 1.96 TeV at the Fermilab Tevatron collider. No excess is observed above background expectation, and resulting limits on Higgs boson production exclude a standard model Higgs boson in the mass range 162-166 GeV at the 95% C.L., We thank the Fermilab staff and the technical staffs of the participating institutions for their vital contributions. This work was supported by DOE and NSF (USA), CONICET and UBACyT (Argentina), CNPq, FAPERJ, FAPESP and FUNDUNESP (Brazil), CRC Program, CFI, NSERC and WestGrid Project (Canada), CAS and CNSF (China), Colciencias (Colombia), MSMT and GACR (Czech Republic), Academy of Finland (Finland), CEA and CNRS/IN2P3 (France), BMBF and DFG (Germany), Ministry of Education, Culture, Sports, Science and Technology (Japan), World Class University Program, National Research Foundation (Korea), KRF and KOSEF (Korea), DAE and DST (India), SFI (Ireland),INFN (Italy), CONACyT (Mexico), NSC(Republic of China), FASI, Rosatom and RFBR (Russia), Slovak R&D Agency (Slovakia), Ministerio de Ciencia e Innovación, and Programa Consolider-Ingenio 2010 (Spain), The Swedish Research Council (Sweden), Swiss National Science Foundation (Switzerland), FOM (The Netherlands), STFC and the Royal Society (UK), and the A.P. Sloan Foundation (USA).

Published
2010
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30. CDER photosafety guidance for industry.

Author

Jacobs AC, Brown PC, Chen C, Ellis A, Farrelly J, and Osterberg R

Subjects
3T3 Cells, Animals, Drug Evaluation, Mice, Toxicity Tests, Acute, United States, United States Food and Drug Administration, Guidelines as Topic, Industry, Photosensitizing Agents adverse effects, Safety standards
Abstract

In the Federal Register of January 10, 2000 (65 FR 1399), FDA published a draft guidance entitled "Photosafety Testing." The notice gave interested persons an opportunity to submit comments. As a result of the comments, certain sections of the guidance were reworded to improve clarity. A final guidance was published in May 2003. The final guidance further emphasizes that a flexible approach can be used to address adverse photoeffects and that specific assays are not required. Moreover, it encourages the development of methods that can efficiently be used to evaluate human safety. The guidance describes a consistent, science-based approach for testing of topically and systemically administered drug products.

Published
2004
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31. Standardized protocols for photocarcinogenesis safety testing.

Author

Forbes PD, Beer JZ, Black HS, Cesarini JP, Cole CA, Davies RE, Davitt JM, deGruijl F, Epstein J, Fourtanier A, Green A, Koval T, Ley RD, Mascotto R, Morison W, Osterberg R, Sliney D, Urbach F, van der Leun JC, and Young AR

Subjects
Animals, Humans, Carcinogenicity Tests methods, Carcinogenicity Tests standards, Drug Screening Assays, Antitumor methods, Drug Screening Assays, Antitumor standards, Neoplasms, Radiation-Induced chemically induced, Ultraviolet Rays
Abstract

Solar ultraviolet radiation (UVR) is recognized as a major cause of non-melanoma skin cancer in man. Skin cancer occurs most frequently in the most heavily exposed areas and correlates with degree of outdoor exposure. The incidence of skin cancer is also increased by contact with photosensitizing drugs and chemicals such as psoralens, coal tars and petroleum stocks. Other substances which do not act as photosensitizers, such as immunosuppressants taken by organ transplant recipients, also increase the risk of skin cancer. The U.S. Food and Drug Administration requests, on a case-by-case basis, that risk of enhanced photocarcinogenesis is assessed for many classes of drugs. Health Canada's Therapeutic Products Programme has issued a Notice of Intent to regulate pharmaceutical products which may enhance carcinogenicity of the skin induced by ultraviolet radiation. Other national regulatory agencies review such data when they exist, but their own requirements emphasize batteries of short-term in vitro and in vivo tests. While they may support drug development strategies, short-term tests have yet to be validated as predictors of the ability of drugs or chemicals to enhance photocarcinogenesis. Published protocols now describe study designs and procedures capable of determining whether test agents enhance the rate of formation of UVR-induced skin tumors.

Published
2003
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32. Regulatory science: a special update from the United States Food and Drug Administration: Preclinical issues and status of investigation of botanical drug products in the United States.

Author

Wu KM, DeGeorge JG, Atrakchi A, Barry E, Bigger A, Chen C, Du T, Freed L, Geyer H, Goheer A, Jacobs A, Jean D, Rhee H, Osterberg R, Schmidt W, and Farrelly JG

Subjects
Databases, Factual, Humans, Investigational New Drug Application, Legislation, Drug, United States, United States Food and Drug Administration, Drugs, Investigational, Phytotherapy, Plants, Medicinal
Abstract

A recent survey was conducted across the therapeutic divisions within the CDER, U.S. FDA regarding the number of submissions related to botanical drug products over the past ten years. The overall number of botanical submissions as expressed in the parenthesis are as follows: 1990 (1), 1991 (4), 1992 (4), 1993 (5), 1994 (6), 1995 (5), 1996 (13), 1997 (16), 1998 (10). In the total of 64 counted, 50 of them are submitted in original IND and the rest (14) in pre-IND format. The therapeutic categories are focused on dermatological and topical (19), anti AIDS/antiviral (12), oncologic (13), neuropharmacologic (8), endocrine and metabolic (3), urologic (2), tobacco (2), and cardio-renal products (1). The regulatory actions taken on these submissions showed that 68% of them are evaluated as safe to proceed for the human trials, while the rest (32%) of submissions required agency's regulatory guidance. Among the submissions that required further guidance, 81% were deficient in preclinical pharmacology/toxicology information and the rest (19%) lacks information in other areas (chemistry, clinical protocols). Following agency's guidance, 93% of the submissions that were put on hold were allowed to proceed. In summary, a total of 94% of all the botanical INDs submitted to the agency were allowed to proceed without additional animal toxicity studies conducted. In conclusion, this survey indicates that the growing public interest in botanical supplements has prompted more formal evaluation of the efficacy/safety claims of these products.

Published
2000
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33. On the prebiotic role of iron and sulfur.

Author

Osterberg R

Subjects
Earth, Planet, Environmental Microbiology, Evolution, Chemical, Evolution, Planetary, Iron metabolism, Oxidation-Reduction, Oxygen, Sulfur metabolism, Iron chemistry, Sulfur chemistry
Abstract

Thermodynamic data (Sillen, L. G.: 1966, Arkiv Kemi, 25, 159) indicate that there is little support for the idea that metabolic sulfur cycles were involved in prebiotic and early life processes, since under reducing conditions the 'equilibrium' concentration of sulfur in the primordial seas should have been very low, < 10(-8) M. However, it is suggested that metabolic sulfur cycles may have become important when oxygen evolved, when iron(II) ions disappeared from the seas, and when large amounts of sulfur were released from their iron sulfide sources.

Published
1997
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35. Response to Monro and Mehta proposal for use of single-dose toxicology studies to support single-dose studies of new drugs in humans.

Author

Choudary J, Contrera JF, DeFelice A, DeGeorge JJ, Farrelly JG, Fitzgerald G, Goheer MA, Jacobs A, Jordan A, Meyers L, Osterberg R, Resnick C, Sun CJ, and Temple RJ

Subjects
Animals, Humans, Male, Pharmacology, Time Factors, United States, United States Food and Drug Administration, Drug-Related Side Effects and Adverse Reactions, Pharmaceutical Preparations administration & dosage
Published
1996
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36. Defluoridation of drinking water with pottery: effect of firing temperature.

Author

Hauge S, Osterberg R, Bjorvatn K, and Selvig KA

Subjects
Clay, Fluorides analysis, Sodium Fluoride analysis, Sodium Fluoride chemistry, Time Factors, Water chemistry, Aluminum Silicates chemistry, Ceramics chemistry, Fluorides chemistry, Hot Temperature, Water Supply analysis
Abstract

Excessive fluoride (F) in drinking water should be removed, but simple, inexpensive methods of fluoride removal are not readily available. This study examines the F(-)-binding capacity of clay and clayware, especially the effect of the firing temperature on the F(-)-binding process. A series of pots were made from ordinary potter's clay and fired at 500-1000 degrees C. Likewise, small clay bricks were fired and then crushed and sieved. NaF solutions containing 10 mg/l F- (10 ppm F-) were prepared. Suitable aliquots of the solutions were poured into clay pots or exposed to powdered clayware. Samples were taken at storage periods of 30 min to 20 days and analyzed for F- by ion-selective electrodes. The rate and capacity of F(-)-binding in the clayware varied with the firing temperature. Clay fired at approximately 600 degrees C was most effective. Temperatures over 700 degrees C caused a decline in F(-)-binding, and pottery fired at 900 degrees C and above seemed unable to remove F- from water. Pots fired at 500 degrees C or less cracked in water. The findings indicate that clayware, fired at an optimal temperature, may be of practical value for partial defluoridation of drinking water.

Published
1994
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37. Small-angle scattering study of alpha 1 inhibitor III from rat blood plasma.

Author

Osterberg R, Boive T, Wang W, Mortensen K, Saito A, Sinohara H, and Ikai A

Subjects
Animals, Chemical Phenomena, Chemistry, Physical, Chymotrypsin chemistry, Computer Simulation, Male, Methylamines chemistry, Models, Chemical, Neutrons, Rats, Rats, Wistar, Solutions, X-Rays, Acute-Phase Proteins, Protease Inhibitors blood, Scattering, Radiation
Abstract

The alpha 1 proteinase inhibitor III from rat blood plasma, homologous to the alpha 2-macroglobulin family of proteins, has been studied in solution using small-angle scattering of X-rays and of neutrons: the radius of gyration, Rg, was found to be 4.5 nm, and the largest distance within the molecule, Dmax = 14 nm. When the inhibitor reacts with chymotrypsin or methylamine, the resulting derivatives yield slightly higher Rg-values, 4.7 and 4.85 nm, respectively. The data of the native protein are consistent with a model, the projection of which resembles the letter V and which is formed by the two identical halves of an elliptic cylinder with semi-axes of 2.1 and 5.5 nm and a length of 11 nm. This elliptic cylinder model also explained the scattering from the monomeric complement proteins C3 and C4, as well as that from the monomers of the dimeric and tetrameric alpha 2-macroglobulin family of proteins (Osterberg, R., et al. (1991), Biochemistry 30, 7873-7878). Due to the conformational change occurring when the thiol ester bond is split, the cleft in the V-form seems to be closed; and as a result, the models of the chymotrypsin and methylamine derivatives are more compact than that of the native protein.

Published
1994
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38. The growth of fractal humic acids: cluster correlation and gel formation.

Author

Osterberg R and Mortensen K

Subjects
Gels, Neutrons, Soil analysis, Water Supply analysis, Humic Substances chemistry
Abstract

The growth of humic acids, prepared by a gentle method from two different kinds of soils (I and II), has been studied using small-angle neutron scattering at an acidity corresponding to pH 5.0 and 0.10 M ionic strength (NaCl). Humic acids aggregate either to large clusters with a fractal dimension of 2.3 and an average diameter of 1720 A (I) or to clusters with an average diameter of 700 A (II). After storage for 2 days at 4 degrees C, the latter aggregates (II) formed a gel. In a step toward gelation, we observed cluster-cluster interaction from the neutron-scattering data in the form of a correlation peak. These differences in size can be explained by assuming that the smaller particles (II) are trapped into a nonequilibrium state characterized by the temperature-solvent condition. The importance of a humic acid gel network for the conservation of water and nutrients in the environment is discussed.

Published
1994
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39. Correlation between the human and porcine complement system: a small-angle scattering study of cross immunity and methylamine-induced conformational changes of porcine C3 and C4 proteins.

Author

Osterberg R, Malmensten B, Boive T, Nilsson U, Stigbrand T, and Mortensen K

Subjects
Animals, Antibodies, Monoclonal, Complement C3 chemistry, Complement C3 drug effects, Complement C4 chemistry, Complement C4 drug effects, Cross Reactions, Humans, Immunoglobulin Fab Fragments immunology, Molecular Conformation, Scattering, Radiation, Complement C3 immunology, Complement C4 immunology, Methylamines pharmacology, Swine immunology
Abstract

The porcine complement proteins C3 and C4 have been isolated and then characterized using small-angle scattering methods. Within the limits of experimental errors, the porcine proteins are virtually identical with the corresponding human proteins as measured in terms of mol. wt, Mr and radius of gyration, R,: Mr(C3) = 198,000, Mr(C4) = 207,000, and R(C3) = 4.4 nm, R(C4) = 4.5 nm. The C3 and C4 proteins from pigs show cross-immunity with monoclonal antibodies (mAbs) raised against human C3 and C4, respectively. Using the Fab fragments of these mAbs as markers, it is indicated that porcine C3 and C4 undergo a conformational change after reaction with methylamine. The relatively large increase in the radius of gyration observed, delta R = 1.0-1.2 nm, going from the Fab complexes to the Fab complexes of the methylamine derivatives, is similar to that observed for human C3 under similar conditions. This may indicate that methylamine cleaves a labile thiol ester bond supposed to be present within the porcine proteins and that the epitopes interacting with the Fab fragments are very similar to those of the human proteins. Porcine C3 also resembles the human analogue by forming dimers after being subjected to methylamine and dilute lauryl sulphate: Mr = 404,000 and R = 7.9 nm.

Published
1991
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40. X-ray scattering study of hagfish protease inhibitor, a protein structurally related to complement and alpha 2-macroglobulin.

Author

Osterberg R, Malmensten B, and Ikai A

Subjects
Animals, Hagfishes, Humans, Macromolecular Substances, Models, Structural, Molecular Weight, Protease Inhibitors blood, Protein Conformation, X-Ray Diffraction methods, Protease Inhibitors chemistry, alpha-Macroglobulins chemistry
Abstract

A protease inhibitor from hagfish blood plasma, homologous to human alpha 2-macroglobulin, has been studied in solution using small-angle X-ray scattering; the radius of gyration, R, was found to be 7.0 nm, the molecular weight 340,000 +/- 20,000, and the largest distance within the molecule, Dmax, 22 nm. When the inhibitor reacts with chymotrypsin, its 1:1 chymotrypsin complex is found to be more compact than the native molecule, R = 6.1 nm. A very similar conformational change is observed after the protein is reacted with methylamine. The data are consistent with models consisting of two equal elliptic cylinders with the same size as the one used as a model for the complement proteins C3 and C4 [cf. Osterberg et al. (1989) Eur. J. Biochem. 183, 507-511]. In the model for the native protein, these cylinders are arranged in an extended form, and in the one for the methylamine derivative (or chymotrypsin complex), they are closer together so that the projection of their elliptic surfaces forms an angle of about 70 degrees. These models for the hagfish protease inhibitor were expanded to models for the twice as large human alpha 2-macroglobulin using symmetry operations, and the resulting alpha 2-macroglobulin models were found to agree with those emerged from earlier studies involving electron microscopy and X-ray scattering methods.

Published
1991
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41. Small-angle X-ray titration study on the complex formation between 5-S RNA and the L18 protein of the Escherichia coli 50-S ribosome particle.

Author

Osterberg R and Garrett RA

Subjects
Macromolecular Substances, Mathematics, Nucleic Acid Conformation, Protein Binding, Protein Conformation, Ribosomes metabolism, X-Ray Diffraction, Escherichia coli metabolism, RNA, Ribosomal metabolism, Ribosomal Proteins metabolism
Abstract

The 5-S RNA (A) and the L18 protein (B) from Escherichia coli ribosomes form one single AB complex in the concentration ranges supposed to prevail in vivo; at concentrations of L18 higher than 40 mM there is some indication for a minor species, most probably an AB2 species. This is indicated from the X-ray scattering titration data of the 5-S RNA/L18 system recorded at 21 degrees C in ribosomal reconstitution buffer. As a result of the 1:1 complex formation, there is a relatively small but defined increase in the radius of gyration from 3.61 to 3.85 nm. This result as well as the experimental scattering curve can be explained by models where it is assumed that the elongated L18 model is quite far from the electron density centre and where protein L18 interacts with one or both of the minor arms of the supposed Y-shaped 5-S RNA molecule.

Published
1977
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44. Percutaneous absorption of radiolabeled TRIS from flame-retarded fabric.

Author

Ulsamer AG, Porter WK, and Osterberg RE

Subjects
Animals, Clothing, Female, Hydrocarbons, Brominated metabolism, Hydrocarbons, Brominated urine, Male, Organophosphates urine, Rabbits, Sweat, Time Factors, Tissue Distribution, Flame Retardants metabolism, Organophosphates metabolism, Skin Absorption
Abstract

Surface tris-(2,3-dibromopropyl) phosphate (TRIS) was removed from flame-retarded polyester fabric by benzene-hexane extraction and replaced with 14C-TRIS. Sections of the radiolabeled fabric (10 X 12 cm) were placed in contact with the clipped skins of rabbits, and urine and feces were collected over a 96 hr period. The cloths were allowed to remain dry or were moistened with either urine or simulated sweat. A similar collection of urine and feces was performed following i.v. injection of 14C-TRIS. From the results of these experiments, it can be calculated that up to 17 percent of the radiolabel on the cloth penetrated rabbit skin over the 96 hr period of exposure. Most of the excreted radiolabel appeared in the urine, with the kidney being the organ of highest specific radioactivity. The highest absorption of radiolabel occurred in the urine-moistened cloth group. Moistening the cloth with simulated sweat produced no increase in absorption over that seen with dry cloth.

Published
1978

45. The condensation of DNA by chromium (III) ions.

Author

Osterberg R, Persson D, and Bjursell G

Subjects
DNA, Superhelical ultrastructure, Ethidium, Microscopy, Electron, Nucleic Acid Conformation, Chromium, DNA ultrastructure
Abstract

Cr(III), one of the most potent inorganic carcinogens, induces condensation of DNA into a very compact product at 37 degrees, as shown by electron microscopy. The condensation begins with the appearing of some supercoil structures and complete condensation occurs at relatively low Cr(III) concentrations; for 3 and 30 mM ionic strength they are 4.5 and 45 microM, respectively. Under these conditions, Cr(III) inhibits the interaction between ethidium and DNA as shown by absorption and fluorescence spectra.

Published
1984
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46. Mechanism of chromium carcinogenesis.

Author

Persson D, Osterberg R, and Bjursell G

Subjects
Chromium pharmacology, DNA Restriction Enzymes metabolism, DNA, Superhelical drug effects, In Vitro Techniques, Macromolecular Substances, Nucleic Acid Conformation drug effects, Osmolar Concentration, Plasmids, Chromium toxicity
Published
1986
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47. Small-angle X-ray scattering study of the interaction between human alpha 2-macroglobulin and trypsin.

Author

Branegård B, Osterberg R, and Sjöberg B

Subjects
Humans, Protein Binding, Scattering, Radiation, X-Rays, Trypsin blood, alpha-Macroglobulins analysis
Abstract

The interaction between human alpha 2-macroglobulin and trypsin yields a complex of two trypsin molecules and one alpha 2-macroglobulin molecule as the main product. This is indicated from small-angle X-ray titration measurements in 0.02 M Tris/HCl buffer of pH 7.40 containing 0.2 M NaCl and 5 mM EDTA. The radius of gyration for the complex was determined to be 7.1 nm. The complex formation coincides with a decrease in the first side maximum of the scattering curve for alpha 2-macroglobulin. A comparison of the experimental data with those calculated from various models indicates that the data are consistent with the scattering from a hollow cylinder containing two sites, each of which is partly filled with one trypsin molecule.

Published
1982
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48. Appraisal of existing methodology in aspiration toxicity testing.

Author

Osterberg RE, Bayard SP, and Ulsamer AG

Subjects
Animals, Disease Models, Animal, Guinea Pigs, Lung drug effects, Methods, Rabbits, Rats, Toxicology methods, Petroleum toxicity, Pneumonia, Aspiration chemically induced
Abstract

New methods or modifications of currently used methods in aspiration toxicology must be capable of accurately assessing the hazard and toxicity potentials of those products which are capable of being aspirated. The methods evaluated in the rat were intratracheal injections,intravenous injections, and modifications of the Gerarde technique. A product containing petroleum distillates and a standard viscosity petroleum distillate sample were administered to Osborne-Mendel rats, rabbits, and guinea pigs in ml/kg doses. The utility of the methods was determined by comparing lung weight increases, lung-body weight ratios, gross pathological lung changes, and mortality. The modified Gerarde technique showed the best potential for predicting aspiration hazard and toxicity based on the severity of the reactions which, using a radiolabeled oil, was shown to be a function of the amount of product which enters and reacts with the lungs. The influence of preventing the swallowing reflex to assure aspiration of the oil was assessed in the rat. The results show that less than 10% of the dose is aspirated when the swallowing reflex occurs. Methods of sacrifice were investigated for an effect on rat lung weight. No tested method except stunning with cervical dislocation produced an effect. Tests were conducted on rats and rabbits to determine differences in lung reactivity to the influence of inhalation anesthetics, pentothal sodium, or no anesthesia in response to petroleum distillate administration and to determine which test species is the better animal model. The resuls indicate that the rat is the better test model because of degree of lung reaction, size, and economy, and that inhalation anesthesia with ether is preferable over the other choices.

Published
1976

49. An equilibrium model for the calcium ion reactions of blood plasma.

Author

Branegård B and Osterberg R

Subjects
Amino Acids blood, Bicarbonates blood, Binding Sites, Blood Proteins, Carbon Dioxide blood, Carbonates blood, Carboxylic Acids blood, Citrates blood, Diabetes Mellitus blood, Humans, Hydrogen-Ion Concentration, Kinetics, Mathematics, Models, Biological, Molecular Weight, Phosphates blood, Protein Binding, Serum Albumin, Sulfates blood, Calcium blood
Published
1974
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50. Potential biological hazards of commercially available cleansers for dentures.

Author

Osterberg RE, Bierbower GW, Seabaugh VM, and Porter WK Jr

Subjects
Animals, Caustics, Dose-Response Relationship, Drug, Female, Lethal Dose 50, Male, Rabbits, Dentifrices toxicity, Esophagus drug effects, Eye drug effects, Gastric Mucosa drug effects, Irritants, Skin drug effects
Abstract

Thirteen representative denture cleansers were selected from among more than 32 retail products to be tested for potential hazard and toxicity to humans. Products were subjected to toxicological analyses by using the biological tests (acute oral toxicity in rats, eye and skin irritation in rabbits) specified in the Federal Hazardous Substances Act Regulations. All products were eye irritants with ranges from slight to severe. Three produced a primary skin irritation response (one was corrosive), while five of the denture cleansers produced oral LD50 values below 5 g/kg. Furthermore, a provisional upper gastrointestinal irritancy test used in rabbits indicated that eight of the denture cleansers produced upper gastrointestinal irritation, which was, in general, dose-related.

Published
1977
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