Author: "Knobloch, B" - Searchworks@Jio Institute Digital Library Search Results

34 results on '"Knobloch, B"'

1. Arc-to-pocket transition and quantitative understanding of transport properties in cuprate superconductors

Author: Tabiś, W., Popčević, P., Klebel-Knobloch, B., Biało, I., Kumar, C. M. N., Vignolle, B., Greven, M., and Barišić, N.
Subjects: Condensed Matter - Superconductivity
Abstract: Despite immense efforts, the cuprate Fermi surface (FS) has been unambiguously determined in only two distinct, low-temperature regions of the phase diagram: a large hole-like FS at high doping, and a small electron-like pocket associated with charge-density-wave driven FS reconstruction at moderate doping. Moreover, there exists incomplete understanding of the reconstructed state, which is stabilized by high magnetic fields, and its connection with the normal state that consists of arc-like remnants of the large underlying FS. Part of the problem is that compound-specific idiosyncrasies, such as disorder effects and low structural symmetry, can obscure the fundamental properties of the quintessential CuO$_2$ planes. Here we present planar magnetotransport measurements for moderately-doped HgBa$_2$CuO$_{4+{\delta}}$ that enable a quantitative understanding of the phase transition between the normal and reconstructed states and of the charge transport in the latter, and that demonstrate that the quasiparticle scattering rate in both states is due to Umklapp scattering. Building on prior insights, we furthermore arrive at a comprehensive understanding of the evolution of the planar transport properties throughout the entire cuprate phase diagram.
Published: 2021

2. Transport properties and doping evolution of the Fermi surface in cuprates

Author: Klebel-Knobloch, B., Tabiś, W., Gala, M. A., Barišić, O. S., Sunko, D. K., and Barišić, N.
Published: 2023
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3. Characterization of two electronic subsystems in cuprates through optical conductivity

Author: Kumar, C. M. N., primary, Akrap, A., additional, Homes, C. C., additional, Martino, E., additional, Klebel-Knobloch, B., additional, Tabis, W., additional, Barišić, O. S., additional, Sunko, D. K., additional, and Barišić, N., additional
Published: 2023
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4. NOT RESOURCE CURSE NOR RESOURCE BENEFIT, BUT 'RESOURCE NEGATION'? COMMUNITIES AGAINST COAL SEAM GAS ON THE FOSSIL FRONTIER

Author: Goodman, J, Heikkinen, R, and Knobloch, B
Subjects: 12 Built Environment and Design, 14 Economics, 16 Studies in Human Society
Abstract: Overcoming the problems of resource dependency has been a major preoccupation for mainstream and critical economists at least since the wave of decolonisation in the middle of the Twentieth Century. Newly independent countries, ostensibly masters of their own destiny, were bound hand and foot to international resource extraction. Unequal relations of production, on a world scale, created a form of structural servitude for the post-colonial world (Amin 1976). Escaping unequal development – or at least ameliorating it – became the key preoccupation of the thenemergent field of development studies. That development conundrum was directly transposed into debates about the ‘resource curse’, and how to overcome it. As with developmentalism more widely, the central debate is between ‘modernising’ approaches aiming to civilise resource dependence and more critical approaches seeking to break with it (Collins, this issue). More recently, in the context of widescale socio-ecological crisis, most notably climate disruption, the very idea of ‘resources’, whether as a curse or as a benefit has been radically revised. The implications of this transformation are directly played-out today in community-level struggles against extractivism - and nowhere more so than on the ‘fossil frontier’.
Published: 2022

5. Anisotropy of electronic correlations: On the applicability of local theories to layered materials

Author: Klebel-Knobloch, B., primary, Schäfer, T., additional, Toschi, A., additional, and Tomczak, J. M., additional
Published: 2021
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6. Rolle von Omentin als kardioprotektives Adipokin: V 38

Author: Greulich, S., Mueller, H., De Wiza, D., Knobloch, B., Flörke, R., Eckel, J., and Ouwens, M.
Published: 2012

7. Effects of Glucocorticoids on Immunological Parameters and on Fat Metabolism During Short Time Treatment

Author: Schwarzer U, Schäfer K, Sattler T, Leidel I, Krüger M, Knobloch B, Kirbach H, Jäkel L, Jäckel F, Fürll B, Dabbagh MN, Fürll M, and Witteck Th
Subjects: Veterinary medicine, SF600-1100
Published: 2003
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8. Effects of Glucocorticoids on Immunological Parameters and on Fat Metabolism During Short Time Treatment

Author: Fürll, M., Dabbagh, M. N., Fürll, B., Jäckel, F., Jäkel, L., Kirbach, H., Knobloch, B., Krüger, M., Leidel, I., Sattler, T., Schäfer, K., Schwarzer, U., and Witteck, Th.
Published: 2003
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9. Accurate analysis of Mg2+ binding to RNA: From classical methods to a novel iterative calculation procedure

Author: Erat, M C, Coles, J, Finazzo, C, Knobloch, B, Sigel, Roland K O, University of Zurich, and Sigel, Roland K O
Subjects: 10120 Department of Chemistry, 1604 Inorganic Chemistry, 540 Chemistry, 1606 Physical and Theoretical Chemistry, 2505 Materials Chemistry
Abstract: Mg2+ acts as a catalytic cofactor in many ribozymes and specifically bound divalent metal ions have been implicated in the stabilization of structural motifs that are essential for RNA folding. The accurate calculation of intrinsic affinity constants of M2+ to specific binding sites in nucleic acids is therefore of high importance. Methods classically applied to determine the affinity constants of metal ions to RNAs are summarized in the first part of this review e.g. hydrolytic cleavage experiments equilibrium dialysis and spectroscopic techniques like EPR and NMR. However the fact that several binding sites of similar affinities are often present in a single RNA molecule is mostly neglected. The most immediate consequence of several binding sites is that less than the total amount of M2+ is available to bind to a particular binding site at a given total concentration. We have recently introduced a new iterative procedure that tackles this problem and have developed a rapid calculation tool (ISTAR) that is available from the authors. Here we explain this procedure in detail under different assumptions and illustrate how the intrinsic affinity constants for Mg2+ to a short RNA hairpin a minimal domain 6 from the group II intron Sc.ai5? change. We use ISTAR to calculate intrinsic affinities and to validate a particular binding stoichiometry by judging the quality of the fit to the experimental data for a given model. This is important since weak coordination sites exhibiting similar binding affinities and being thus in direct competition to each other are a characteristic feature of nucleic acids. With ISTAR these binding affinities can be calculated more accurately within minutes and we can gain a better understanding of these crucial metal ion–nucleic acid interactions.
Published: 2012

10. Stability and Structure of Mixed-Ligand Metal Ion Complexes That Contain Ni(2+), Cu(2+), or Zn(2+), and Histamine, as well as Adenosine 5 '-Triphosphate (ATP(4-)) or Uridine 5 '-Triphosphate (UTP(4-)): An Intricate Network of Equilibria

Author: Knobloch, B, Mucha, A, Operschall, B P, Sigel, Helmut, Jeżowska‐Bojczuk, Małgorzata, Kozlowski, H, Sigel, Roland K O, and University of Zurich
Subjects: 10120 Department of Chemistry, 1503 Catalysis, 540 Chemistry, 1605 Organic Chemistry
Published: 2011
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11. Comparison of the acid-base properties of ribose and 2'-deoxyribose nucleotides

Author: Mucha, A, Knobloch, B, Jezowska-Bojczuk, M, Kozłowski, H, Sigel, Roland K O, and University of Zurich
Subjects: 10120 Department of Chemistry, 1503 Catalysis, 540 Chemistry, 1605 Organic Chemistry, acidity • nucleic acids • nucleotides • purines • ribozymes
Published: 2008
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12. Metal-Ion-Coordinating Properties of the Dinucleotide 2′-Deoxyguanylyl(5′→3′)-2′-deoxy-5′-guanylate (d(pGpG)3−): Isomeric Equilibria Including Macrochelated Complexes Relevant for Nucleic Acids

Author: Knobloch, B, Sigel, Helmut, Okruszek, A, Sigel, Roland K O, University of Zurich, and Sigel, Roland K O
Subjects: 10120 Department of Chemistry, 1503 Catalysis, 540 Chemistry, General Chemistry, 1605 Organic Chemistry
Published: 2007

13. Precision electroweak measurements on the Z resonance

Author: Schael, S, Barate, R, Bruneliere, R, Buskulic, D, Bonis, De, Decamp, I, Ghez, D, Goy, P, Jezequel, C, Lees, S, Lucotte, Jp, Martin, A, Merle, F, Minard, E, Nief, Mn, Odier, Jy, Pietrzyk, P, Trocme, B, Bravo, B, Casado, S, Chmeissani, Mp, Comas, M, Crespo, P, Fernandez, Jm, E, Fernandez, Bosman, Garrido, M, Grauges, L, Juste, E, Martinez, A, Merino, M, Miquel, G, Mir, R, Orteu, Lm, Pacheco, S, Park, A, Perlas, Ic, Riu, J, Ruiz, I, Sanchez, H, Colaleo, F, Creanza, A, D, Filippis, De, N, Palma, De, Iaselli, M, Maggi, G, Nuzzo, M, Ranieri, S, Raso, A, Ruggieri, G, Selvaggi, F, Silvestris, G, Tempesta, L, Tricomi, P, Zito, A, Huang, G, Lin, X, Ouyang, J, Wang, Q, Xie, T, Xu, Y, Xue, R, Zhang, S, Zhang, J, Zhao, L, Abbaneo, W, Bazarko, D, Becker, A, Boix, U, Bird, G, Blucher, F, Bonvicini, E, B, Bright, Thomas, Barklow, P, Buchmuller, T, Cattaneo, O, Cerutti, M, Ciulli, F, Clerbaux, V, Drevermann, B, Forty, H, Frank, Rw, Greening, M, Hagelberg, Tc, Halley, R, Gianotti, Aw, Girone, F, Hansen, M, Harvey, Jb, Jacobsen, J, Hutchcroft, R, Janot, De, Jost, R, Knobloch, B, Kado, J, Lehraus, M, Lazeyras, I, Maley, P, Mato, R, May, P, Moutussi, J, A, Pepe, Altarelli, Ranjard, M, Rolandi, F, Schlatter, L, Schmitt, D, Schneider, B, Tejessy, O, Teubert, W, Tomalin, F, Tournefier, Ir, Veenhof, E, Valassi, R, Wiedenmann, A, Wright, W, Ajaltouni, Ae, Badaud, Z, Chazelle, F, Deschamps, G, Dessagne, O, Falvard, S, Ferdi, A, Fayolle, C, Gay, D, Guicheney, P, Henrard, C, Jousset, P, Michel, J, Monteil, B, Montret, S, Pallin, Jc, Pascolo, D, Perret, Jm, Podlyski, P, Bertelsen, F, Fernley, H, Hansen, T, Hansen, Jd, Hansen, Jr, Kraan, Ph, Lindahl, Ac, Mollerud, A, Nilsson, R, Rensch, Bs, Waananen, B, Daskalakis, A, Kyriakis, G, Markou, A, Simopoulou, C, Siotis, E, Vayaki, I, Zachariadou, A, Blondel, K, Bonneaud, A, Brient, G, Machefert, Jc, Rouge, E, Rumpf, A, Swynghedauw, M, Tanaka, M, Verderi, R, Videau, M, Focardi, H, Parrini, E, Corden, G, Georgiopoulos, M, Antonelli, C, Antonelli, A, Bencivenni, M, Bologna, G, Bossi, G, Campana, F, Capon, P, Chiarella, G, Felici, V, Laurelli, G, Mannocchi, P, Murtas, G, Passalacqua, Gp, Picchi, L, Colrain, P, P, Ten, Have, Hughes, I, Kennedy, Is, Knowles, J, Lynch, Ig, Morton, Jg, Negus, Wt, Oshea, P., Raine, V, Reeves, C, Scarr, P, Smith, Jm, Thompson, K., Turnbull, As, Wasserbaech, Rm, Cavanaugh, S, Dhamotharan, R, Geweniger, S, Hanke, C, Hansper, P, Hepp, G, Kluge, V, Putzer, Ee, Sommer, A, Stenzel, J, Tittel, H, Werner, K, Wunsch, W, Beuselinck, M, Binnie, R, Cameron, Dm, Davies, W, Dornan, G, Goodsir, Pj, Marinelli, S, Martin, N, Nash, Eb, Nowell, J, Rutherford, J, Sedgbeer, Sa, Thompson, Jk, White, Jc, Williams, R, Ghete, Md, Girtler, Vm, Kneringer, P, Kuhn, E, Rudolph, D, G, Bouhova, Thacker, Bowdery, E, Buck, Ck, Clarke, Pg, Ellis, Dp, Finch, G, Foster, Aj, Hughes, F, Jones, G, Rwl, Keemer, Pearson, Nr, Robertson, Mr, Sloan, Na, Smizanska, T, Snow, M, Williams, Sw, van der Aa, Delaere, O, Leibenguth, C, Lemaitre, G, Bauerdick, V, Lat, Blumenschein, U, Van, Gemmeren, Giehl, P, Holldorfer, I, Jakobs, F, Kasemann, K, Kayser, M, Kleinknecht, F, Muller, K, Quast, As, Renk, G, Rohne, B, Sander, E, Schmeling, Hg, Wachsmuth, S, Wanke, H, Zeitnitz, R, Ziegler, C, Aubert, T, Benchouk, Jj, Bonissent, C, Carr, A, Coyle, J, Curtil, P, Ealet, C, Etienne, A, Fouchez, F, Motsch, D, Payre, F, Rousseau, P, Tilquin, D, Talby, A, Thulasides, M, Aleppo, M, Ragusa, M, Buscher, F, David, V, Dietl, A, Ganis, H, Huttmann, G, Lutjens, K, Mannert, G, Manner, C, Moser, W, Settles, Hg, Seywerd, R, Villegas, H, Wolf, M, Azzurri, G, Boucrot, P, Callot, J, Chen, O, Cordier, S, Davier, A, Duflot, M, Grivaz, L, Heusse, Jf, Jacholkowska, P, Diberder, Le, Lefrancois, F, Mutz, J, Schune, Am, Serin, Mh, Veillet, L, Videau, Jj, Zerwas, I, Bagliesi, D, Bettarini, G, Boccali, S, Bozzi, T, Calderini, C, Dellorso, G, Fantechi, R, Ferrante, R, Fidecaro, I, Foa, F, Giammanco, L, Giassi, A, Gregorio, A, Ligabue, A, Lusiani, F, Marrocchesi, PIER SIMONE, Messineo, Ps, Palla, A, Rizzo, F, Sanguinetti, G, Sciaba, G, Sguazzoni, A, Spagnolo, G, Steinberger, P, Tenchini, J, Venturi, R, Vannini, A, Verdini, C, Awunor, Pg, Blair, O, Cowan, Ga, Garcia, Bellido, Green, A, Medcalf, Mg, Misiejuk, T, Strong, A, Teixeira, Dias, Botterill, P, Clifft, Dr, Edgecock, Rw, Edwards, Tr, Haywood, M, Norton, Sj, Ward, Pr, Bloch, Devaux, Boumediene, B, Colas, D, Emery, P, Fabbro, S, Kozanecki, B, Lancon, W, Lemaire, E, Locci, Mc, Perez, E, Rander, P, Renardy, J, Roussarie, Jf, Schuller, A, Schwindling, Jp, Tuchming, J, Vallage, B, Black, B, Dann, Sn, Kim, Jh, Konstantinidis, Hy, Litke, N, Mcneil, Am, Taylor, Ma, Booth, G, Cartwright, Cn, Combley, S, Hodgson, F, Lehto, Pn, Thompson, M, Affholderbach, Lf, Barberio, K, Bohrer, E, Brandt, A, Burkhardt, S, Feigl, H, Grupen, E, Hess, C, Lutters, J, Meinhard, G, H, Minguet, Rodriguez, Mirabito, J, Neugebauer, L, Ngac, E, Prange, A, Rivera, G, Saraiva, F, Schafer, P, Sieler, U, Smolik, U, Stephan, L, Trier, F, Apollonio, H, Borean, M, Bosisio, C, L, Della, Marina, Giannini, R, Gobbo, G, Musolino, B, Pitis, G, He, L, Kim, H, Putz, H, Rothberg, J, Armstrong, J, Bellantoni, Sr, Berkelman, L, Cinabro, K, Conway, D, Cranmer, Js, Elmer, K, Feng, P, Ferguson, Z, Dps, Gao, Gonzalez, Y, Grahl, S, Harton, J, Hayes, Jl, Hu, Oj, Jin, H, Johnson, S, Kile, Rp, Mcnamara, J, Nielsen, Pa, Orejudos, J, Pan, W, Saadi, Y, Scott, Y, Sharma, Ij, Walsh, V, Walsh, Am, Wear, J, J, von Wimmersperg Toeller, Wu, Jh, Wu, J, Wu, Sl, Yamartino, X, Zobernig, Jm, Dissertori, G, Abdallah, G, Abreu, J, Adam, P, Adye, W, Adzic, T, Ajinenko, P, Albrecht, I, Alderweireld, T, Alekseev, T, Alemany, Fernandez, Allmendinger, R, Allport, T, Almehed, Pp, Amaldi, S, Amapane, U, Amato, N, Anashkin, S, Anassontzis, E, Andersson, Eg, Andreazza, P, Andringa, A, Anjos, S, Antilous, N, Apel, P, Arnoud, Wd, Ask, Y, Asman, S, Augustin, B, Augustinus, Je, Baillon, A, Ballestrero, P, Bambade, A, Barao, P, Barbiellini, F, Barbier, G, Bardin, R, Barker, D, Baroncelli, G, Battaglia, A, Baubillier, M, Becks, M, Begalli, Kh, Behrmann, M, Beilliere, A, Belokopytov, P, Belous, Y, K, Ben, Haim, Benekos, E, Benvenuti, N, Berat, A, Berggren, C, Berntzon, M, Bertini, L, Bertrand, D, Besancon, D, Besson, M, Bianchi, N, Bigi, F, Bilenky, M, Bizouard, Ms, Bloch, Ma, Blom, D, Bluj, M, Bonesini, M, Bonivento, M, Boonekamp, W, Booth, M, Psl, Borgland, Borisov, Aw, Bosio, G, Botner, C, Boudinov, O, Bouquet, E, Bourdarios, B, Bowcock, C, Tjv, Boyko, Bozovic, I, Bozzo, I, Bracko, M, Branchini, M, Brenke, P, Brenner, T, Brodet, R, Bruckman, E, Brunet, P, Bugge, Jm, Buran, L, Burgsmueller, T, Buschbeck, T, Buschmann, B, Cabrera, P, Caccia, S, Calvi, M, Rozas, M, Ajc, Camporesi, Canale, T, Canepa, V, Carena, M, Carroll, F, Caso, L, Gimenez, C, Mvc, Castro, Cattai, N, Cavallo, A, Cerruti, F, Chabaud, C, Chapkin, V, Charpentier, M, Chaussard, P, Checchia, L, Chelkov, P, Chen, Ga, Chierici, M, Chliapnikov, R, Chochula, R, Chorowicz, P, Chudoba, V, Chung, J, Cieslik, Su, Collins, K, Colomer, P, Contri, M, Cortina, R, Cosme, E, Cossuti, G, Costa, F, Cowell, Mj, Crawley, Jh, Crennell, Hb, Crepe, D, Crosetti, S, Cuevas, G, Czellar, J, Dhondt, S, Dalmagne, J, Dalmau, B, Damgaard, J, Davenport, G, M, Silva, Da, T, Deghorain, W, Della, Ricca, Delpierre, G, Demaria, P, Angelis, De, Boer, De, W, Brabandere, De, S, Clercq, De, C, Lotto, De, Maria, De, Min, De, Paula, De, Dijkstra, L, Ciaccio, Di, Diodato, Di, Simone, Di, Djannati, A, Dolbeau, A, Doroba, J, Dracos, K, Drees, M, Drees, J, Dris, Ka, Duperrin, M, Durand, A, Ehret, Jd, Eigen, R, Ekelof, G, Ekspong, T, Ellert, G, Elsing, M, Engel, M, Erzen, Jp, Santo, B, Mce, Falk, Fanourakis, E, Fassouliotis, G, Fayot, D, Feindt, J, Fenyuk, M, Fernandez, A, Ferrari, J, Ferrer, P, Ferrer, Ribas, Ferro, E, Fichet, F, Firestone, S, Fischer, A, Flagmeyer, Pa, Foeth, U, Fokitis, H, Fontanelli, E, Franek, F, Frodesen, B, Fruhwirth, Ag, R, Fulda, Quenzer, Fuster, F, Galloni, J, Gamba, A, Gamblin, D, Gandelman, S, Garcia, M, Garcia, C, Gaspar, J, Gaspar, C, Gasparini, M, Gavillet, U, Gazis, P, Gele, E, Gerber, D, Gerdyukov, Jp, Ghodbane, L, Gil, N, Glege, I, Gokieli, F, Golob, R, Gomez, Ceballos, Goncalves, G, Caballero, P, Gopal, Ig, Gorn, G, Gorski, L, Gouz, M, Gracco, Y, Graziani, V, Green, E, Grefrath, C, Grimm, A, Gris, Hj, Grosdidier, P, Grzelak, G, Gunther, K, Guy, M, Haag, J, Hahn, C, Hahn, F, Hallgren, S, Hamacher, A, Hamilton, K, Hansen, K, Harris, J, Haug, Fj, Hauler, S, Hedberg, F, Heising, V, Hennecke, S, Henriques, M, Hernandez, R, Herquet, Jj, Herr, P, Hessing, H, Heuser, Tl, Higon, Jm, Hoffman, E, Holmgren, J, Holt, So, Holthuizen, Pj, Hoorelbeke, D, Houlden, S, Hrubec, Ma, Huber, J, Huet, M, Hughes, K, Hultqvist, Gj, Jackson, K, Jacobsson, Jn, Jalocha, R, Janik, P, Jarlskog, R, Jarlskog, C, Jarry, G, Jean, Marie, Jeans, B, Johansson, D, Johansson, Ek, Jonsson, Pd, Joram, P, Juillot, C, Jungermann, P, Kapusta, L, Karafasoulis, F, Katsanevas, K, Katsoufis, S, Keranen, E, Kernel, R, Kersevan, G, Kerzel, Bp, Khomenko, U, Khovanski, Ba, Kiiskinen, Nn, King, A, Kinvig, Bt, Kjaer, A, Klapp, Nj, Klein, O, Kluit, H, Knoblauch, P, Kokkinias, D, Konopliannikov, P, Koratzinos, A, Kostioukhine, M, Kourkoumelis, V, Kouznetsov, C, Krammer, O, Kreuter, M, Kriznic, C, Krstic, E, Krumstein, J, Kubinec, Z, Kucewicz, P, Kucharczyk, W, Kurowska, M, Kurvinen, J, Lamsa, K, Lanceri, J, Lane, L, Langefeld, Dw, Lapin, P, Laugier, V, Lauhakangas, Jp, Leder, R, Ledroit, G, Lefebure, F, Leinonen, V, Leisos, L, Leitner, A, Lemonne, R, Lenzen, J, Lepeltier, G, Lesiak, V, Lethuillier, T, Libby, M, Liebig, J, Liko, W, Lipniacka, D, Lippi, A, Loerstad, I, Lokajicek, B, Loken, M, Lopes, Jg, Lopez, Jh, Lopez, Femandez, Loukas, R, Lutz, D, Lyons, P, Macnaughton, L, Mahon, J, Maio, Jr, Malek, A, Malmgren, A, Tgm, Maltezos, Malychev, S, Mandl, V, Marco, F, Marco, J, Marechal, R, Margoni, B, Marin, M, Mariotti, Jc, Markou, C, Martinez, Rivero, Martinez, Vidal, 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R, Coyle, Rf, Coyne, Pa, Crawford, Dg, Doliveira, G, Damerell, A, Cjs, Daoudi, Dasu, M, Groot, De, Sangro, De, Simone, De, Dervan, S, Dima, Pj, Dong, M, Doser, Dn, Du, M, Pyc, Dubois, Eisenstein, R, Elia, Bi, Erdos, R, Erofeeva, E, Eschenburg, I, Fahey, V, Falciai, S, Fan, D, Fernandez, C, Fero, Jp, Flood, Mj, Frey, K, Friedman, R, Furuno, Ji, Garwin, K, Gillman, El, Gladding, T, Hallewell, G, Hart, Gd, Hasegawa, El, Hasuko, Y, Hedges, K, Hertzbach, S, Hitlin, Ss, Honma, Dg, Huber, A, Huffer, Js, Hughes, Me, Huynh, Ew, Hwang, X, Iwasaki, H, Iwasaki, M, Izen, Y, Jackson, Jm, Jacques, Dj, Jaros, P, Jiang, Ja, Johnson, Zy, Johnson, As, Johnson, Jr, Junk, Ra, Kajikawa, T, Kalelkar, R, Kamyshkov, M, Kang, Ya, Karliner, Hj, Kawahara, I, Kelsey, H, Kendall, Mh, Kim, Hw, King, Yd, King, M, Kofler, R, Krishna, R, Kwon, Nm, Labs, Y, Kroeger, Jf, Langston, Rs, Lath, M, Lauber, A, Leith, Ja, Dwg, Lia, Lin, V, Liu, C, Loreti, Mx, Lu, M, Lynch, A, Ma, Hl, Mancinelli, J, Manly, G, Mantovani, S, 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Thaler, Fe, Thom, Jj, Trandafir, J, Turk, Ai, Usher, Jd, Vavra, T, Vella, J, Venuti, E, Verdier, Jp, Wagner, R, Waite, Sr, Walston, Ap, Wang, S, Watts, J, Weidemann, Sj, Weiss, Aw, Whitaker, Er, White, Js, Wickens, Sl, Williams, Fj, Williams, Da, Williams, Dc, Willocq, Sh, Wilson, S, Wisniewski, Rj, Wittlin, Wj, Woods, Jl, Word, M, Wright, Gb, Wyss, Tr, Yamamoto, J, Yang, Rk, Yashima, Xq, Yellin, J, Young, Sj, Yuta, Cc, Zapalac, H, Zdarko, G, Zeitlin, Rw, Zhou, C, Blondel, Alain, Schael, S, Barate, R, Bruneliere, R, Spagnolo, Stefania Antonia, S., Schael, Aloisio, Alberto, Alviggi, Mariagrazia, Canale, Vincenzo, Chiefari, Giovanni, DELLA VOLPE, Domenico, Merola, Leonardo, Napolitano, Marco, Patricelli, Sergio, Sciacca, Crisostomo, Lista, Luca, 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 de Physique Théorique et Astroparticules (LPTA), Université Montpellier 2 - Sciences et Techniques (UM2)-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), Laboratoire de Physique Nucléaire et de Hautes Énergies (LPNHE), 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), Laboratoire de Physique Subatomique et de Cosmologie (LPSC), 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), Institut de Physique Nucléaire de Lyon (IPNL), 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), Institut de Recherches Subatomiques (IReS), Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Cancéropôle du Grand Est-Université Louis Pasteur - Strasbourg I-Centre National de la Recherche Scientifique (CNRS), Physique Corpusculaire et Cosmologie - Collège de France (PCC), Collège de France (CdF (institution))-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), ALEPH, DELPHI, L3, OPAL, SLD, BARBIELLINI AMIDEI, Guido, Bosisio, Luciano, DELLA RICCA, Giuseppe, Giannini, Gianrossano, Gregorio, Anna, Lanceri, Livio, Poropat, Paolo, Vitale, Lorenzo, Buskulic, D, De Bonis, I, Decamp, D, Ghez, P, Goy, C, Jezequel, S, Lees, J, Lucotte, A, Martin, F, Merle, E, Minard, M, Nief, J, Odier, P, Pietrzyk, B, Trocme, B, Bravo, S, Casado, M, Chmeissani, M, Comas, P, Crespo, J, Fernandez, E, Fernandez Bosman, M, Garrido, L, Grauges, E, Juste, A, Martinez, M, Merino, G, Miquel, R, Mir, L, Orteu, S, Pacheco, A, Park, I, Perlas, J, Riu, I, Ruiz, H, Sanchez, F, Colaleo, A, Creanza, D, De Filippis, N, De Palma, M, Iaselli, G, Maggi, G, Maggi, M, 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, Bazarko, A, Becker, U, Boix, G, Bird, F, Blucher, E, Bonvicini, B, Bright Thomas, P, Barklow, T, Buchmuller, O, Cattaneo, M, Cerutti, F, Ciulli, V, Clerbaux, B, Drevermann, H, Forty, R, Frank, M, Greening, T, Hagelberg, R, Halley, A, Gianotti, F, Girone, M, Hansen, J, Harvey, J, Jacobsen, R, Hutchcroft, D, Janot, R, Jost, B, Knobloch, J, Kado, M, Lehraus, I, Lazeyras, P, Maley, R, Mato, P, May, J, Moutussi, A, Pepe Altarelli, M, Ranjard, F, Rolandi, L, Schlatter, D, Schmitt, B, Schneider, O, Tejessy, W, Teubert, F, Tomalin, I, Tournefier, E, Veenhof, R, Valassi, A, Wiedenmann, W, Wright, A, Ajaltouni, Z, Badaud, F, Chazelle, G, Deschamps, O, Dessagne, S, Falvard, A, Ferdi, C, Fayolle, D, Gay, P, Guicheney, C, Henrard, P, Jousset, J, Michel, B, Monteil, S, Montret, J, Pallin, D, Pascolo, J, Perret, P, Podlyski, F, Bertelsen, H, Fernley, T, Hansen, P, Kraan, A, Lindahl, A, Mollerud, R, 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, Machefert, E, Rouge, A, Rumpf, M, Swynghedauw, M, Tanaka, R, Verderi, M, Videau, H, Focardi, E, Parrini, G, Corden, M, Georgiopoulos, C, Antonelli, A, Antonelli, M, Bencivenni, G, Bologna, G, Bossi, F, Campana, P, Capon, G, Chiarella, V, Felici, G, Laurelli, P, Mannocchi, G, Murtas, G, Passalacqua, L, Picchi, P, Colrain, P, Ten Have, I, Hughes, I, Kennedy, J, Knowles, I, Lynch, J, Morton, W, Negus, P, 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THACKRAY, M. THIERGEN, J. THOMAS, M.A. THOMSON, E. VON TORNE, S. TOWERS, D. TOYA, Z. TROCSANYI, P. TRAN, G. TRANSTROMER, T. TREFZGER, N.J. TRESILIAN, I. TRIGGER, M. TSCHEULIN, T. TSUKAMOTO, E. TSUR, A.S. TURCOT, M.F. TURNER-WATSON, G. TYSARCZYK-NIEMEYER, I. UEDA, B. UJVARI, P. UTZAT, B. VACHON, D. VAN DEN PLAS, R. VAN KOOTEN, G.J. VAN DALEN, P. VANNEREM, G. VASSEUR, R. VERTESI, M. VERZOCCHI, P. VIKAS, M. VINCTER, C.J. VIRTUE, E.H. VOKURKA, C.F. VOLLMER, H. VOSS, J. VOSSEBELD, F. WACKERLE, A. WAGNER, C. WAHL, J.P. WALKER, D. WALLER, C.P. WARD, D.R. WARD, J.J. WARD, P.M. WATKINS, A.T. WATSON, N.K. WATSON, M. WEBER, P. WEBER, S. WEISZ, P.S. WELLS, T. WENGLER, N. WERMES, D. WETTERLING, M. WEYMANN, M.A. WHALLEY, J.S. WHITE, B. WILKENS, J.A. WILSON, G.W. WILSON, I. WINGERTER, V.-H. WINTERER, T. WLODEK, G. WOLF, N.C. WOOD, S. WOTTON, T.R. WYATT, R. YAARI, S. YAMASHITA, Y. YANG, A. YEAMAN, G. YEKUTIELI, M. YURKO, V. ZACEK, I. ZACHAROV, D. ZER-ZION, W. ZEUNER, L. ZIVKOVIC, G.T. ZORN, KENJI ABE, KOYA ABE, T. ABE, I. ABT, P.D. ACTON, I. ADAM, G. AGNEW, T. AKAGI, H. AKIMOTO, N.J. ALLEN, W.W. ASH, D. ASTON, N. BACCHETTA, K.G. BAIRD, C. BALTAY, H.R. BAND, M.B. BARAKAT, G.J. BARANKO, O. BARDON, T.L. BARKLOW, G.L. BASHINDZHAGIAN, R. BATTISTON, J.M. BAUER, A.O. BAZARKO, A. BEAN, G. BELLODI, R. BEN-DAVID, A.C. BENVENUTI, R. BERGER, M. BIASINI, T. BIENZ, G.M. BILEI, D. BISELLO, G. BLAYLOCK, J.R. BOGART, B. BOLEN, T. BOLTON, G.R. BOWER, J.E. BRAU, M. BREIDENBACH, W.M. BUGG, D. BURKE, T.H. BURNETT, P.N. BURROWS, W. BUSZA, A. CALCATERRA, D.O. CALDWELL, B. CAMANZI, M. CARPINELLI, J. CARR, R. CASSELL, R. CASTALDI, A. CASTRO, M. CAVALLI-SFORZA, G.B. CHADWICK, A. CHOU, E. CHURCH, R. CLAUS, H.O. COHN, J.A. COLLER, M.R. CONVERY, V. COOK, R. COTTON, R.F. COWAN, P.A. COYLE, D.G. COYNE, G. CRAWFORD, A. D’OLIVEIRA, C.J.S. DAMERELL, M. DAOUDI, S. DASU, N. DE GROOT, R. DE SANGRO, P. DE SIMONE, S. DE SIMONE, R. DELL’ORSO, P.J. DERVAN, M. DIMA, D.N. DONG, M. DOSER, P.Y.C. DU, R. DUBOIS, J.E. DUBOSCQ, G. EIGEN, B.I. EISENSTEIN, R. ELIA, E. ERDOS, I. EROFEEVA, V. ESCHENBURG, E. ETZION, S. FAHEY, D. FALCIAI, C. FAN, J.P. FERNANDEZ, M.J. FERO, K. FLOOD, R. FREY, J.I. FRIEDMAN, K. FURUNO, E.L. GARWIN, T. GILLMAN, G. GLADDING, S. GONZALEZ, G.D. HALLEWELL, E.L. HART, J.L. HARTON, A. HASAN, Y. HASEGAWA, K. HASUKO, S. HEDGES, S.S. HERTZBACH, M.D. HILDRETH, D.G. HITLIN, A.HONMA, J. S. HUBER, M.E. HUFFER, E.W. HUGHES, X. HUYNH, H.HWANG, M. IWASAKI, Y. IWASAKI, J.M. IZEN, D.J. JACKSON, P. JACQUES, J.A. JAROS, Z.Y. JIANG, A.S. JOHNSON, J.R. JOHNSON, R.A. JOHNSON, T. JUNK, R. KAJIKAWA, M. KALELKAR, Y.A. KAMYSHKOV, H.J. KANG, I. KARLINER, H. KAWAHARA, M.H. KELSEY, H.W. KENDALL, Y.D. KIM, M. KING, R. KING, R. KOFLER, N.M. KRISHNA, Y. KWON, J.F. LABS, R.S. KROEGER, M. LANGSTON, A. LATH, J.A. LAUBER, D.W.G. LEITH, V.LIA, C. LIN, M.X. LIU, M. LORETI, A. LU, H.L. LYNCH, J. MA, G. MANCINELLI, S. MANLY, G. MANTOVANI, T.W. MARKIEWICZ, T. MARUYAMA, H. MASUDA, E. MAZZUCATO, J.F. MCGOWAN, A.K. MCKEMEY, B.T. MEADOWS, R. MESSNER, P.M. MOCKETT, K.C. MOFFEIT, T.B. MOORE, M. MORII, B. MOURS, D. MULLER, G. MUELLER, V. MURZIN, T. NAGAMINE, S. NARITA, U. NAUENBERG, H. NEAL, G. NESOM, M. NUSSBAUM, Y. OHNISHI, N. OISHI, D. ONOPRIENKO, L.S. OSBORNE, R.S. PANVINI, C.H.PARK, H. PARK, T.J. PAVEL, I. PERUZZI, L. PESCARA, M. PICCOLO, L. PIEMONTESE, E. PIERONI, K.T. PITTS, R.J. PLANO, R. PREPOST, C.Y. PRESCOTT, G. PUNKAR, J. QUIGLEY, B.N. RATCLIFF, K. REEVES, T.W. REEVES, J. REIDY, P.L. REINERTSEN, P.E. RENSING, L.S. ROCHESTER, J.E. ROTHBERG, P.C. ROWSON, J.J. RUSSELL, O.H. SAXTON, T. SCHALK, R.H. SCHINDLER, U. SCHNEEKLOTH, B.A. SCHUMM, J. SCHWIENING, A. SEIDEN, S. SEN, V.V. SERBO, L. SERVOLI, M.H. SHAEVITZ, J.T. SHANK, G. SHAPIRO, D.J. SHERDEN, K.D. SHMAKOV, C. SIMOPOULOS, N.B. SINEV, S.R. SMITH, M.B. SMY, J.A. SNYDER, M.D. SOKOLOFF, H. STAENGLE, A. STAHL, P. STAMER, H. STEINER, R. STEINER, M.G. STRAUSS, D. SU, F. SUEKANE, A. SUGIYAMA, A. SUZUKI, S. SUZUKI, M. SWARTZ, A. SZUMILO, T. TAKAHASHI, F.E. TAYLOR, J.J. THALER, J. THOM, E. TORRENCE, A.I. TRANDAFIR, J.D. TURK, T. USHER, J. VA VRA, C. VANNINI, E. VELLA, J.P. VENUTI, R. VERDIER, P.G. VERDINI, D.L. WAGNER, S.R. WAGNER, A.P. WAITE, S. WALSTON, J. WANG, S.J. WATTS, A.W. WEIDEMANN, E.R. WEISS, J.S. WHITAKER, S.L. WHITE, F.J. WICKENS, D.A. WILLIAMS, D.C. WILLIAMS, S.H. WILLIAMS, S. WILLOCQ, R.J. WILSON, W.J. WISNIEWSKI, J.L. WITTLIN, M. WOODS, G.B. WORD, T.R. WRIGHT, J. WYSS, R.K. YAMAMOTO, J.M. YAMARTINO, X.Q. YANG, J. YASHIMA, S.J. YELLIN, C.C.YOUNG, H.YUTA, G. ZAPALAC, R.W. ZDARKO, C. ZEITLIN, J. ZHOU, 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), 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), 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), 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), Laboratoire d'Annecy de Physique des Particules (LAPP/Laboratoire d'Annecy-le-Vieux de Physique des Particules), Centre National de la Recherche Scientifique (CNRS)-Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry])-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)-Aix Marseille Université (AMU), 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 Grenoble Alpes (UGA), Collège de France (CdF)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), GRUNEVALD M, NEWALD M, SCHAEL S, BARATE R, BRUNELIE, RE R, BUSKULIC D, DE BONIS I, DECAMP D, GHEZ P, GOY C, JE, ZE, QUEL S, LEES J, LUCOTTE A, MARTIN M, MERLE E, MINARD M, NIEF J, ODIER P, PIETRZYK B, TROCME, BRAVO S, CASADO MP, CHMEISSANI M, COMAS P, CRESPO JM, FERNANDEZ E, FERNANDEZ-BOSMAN M, GARRIDO L, GRAUGES E, JUSTE A, MARTINEZ M, MERINO G, MIQUEL R, MIR LM, ORTEU S, PACHECO A, PARK IC, PERLAS J, RIU I, RUIZ H, SANCHEZ F, COLALEO A, CREANZA D, DE FILIPPIS N, DE PALMA M, IASELLI G, MAGGI G, MAGGI M, 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, BAZARKO A, BECKER U, BOIX G, BIRD F, BLUCHER E, BONVICINI B, BRIGHT-THOMAS P, BARKLOW T, BUCHMU, LLER O, CATTANEO M, CERUTTI F, CIULLI V, CLERBAUX B, DREVERMANN H, FORTY RW, FRANK M, GREENING TC, HAGELBERG R, HALLEY AW, GIANOTTI F, GIRONE M, HANSEN JB, HARVEY J, JACOBSEN J, HUTCHCROFT DE, JANOT P, JOST B, KNOBLOCH J, KADO M, LEHRAUS I, LAZEYRAS P, and MALEY P
Subjects: Top quark, FORWARD-BACKWARD ASYMMETRY, PARTICLE PHYSICS, LARGE ELECTRON POSITRON COLLIDER, ALEPH, DELPHI, L3, OPAL, General Physics and Astronomy, 01 natural sciences, 7. Clean energy, High Energy Physics - Experiment, Settore FIS/04 - Fisica Nucleare e Subnucleare, High Energy Physics - Experiment (hep-ex), High Energy Physics - Phenomenology (hep-ph), electron-positron physics, [PHYS.HEXP]Physics [physics]/High Energy Physics - Experiment [hep-ex], Electroweak interaction, Physics, Quantum chromodynamics, Electron–positron physics, Electroweak interactions, Decays of heavy intermediate gauge bosons, Fermion–antifermion production, Precision measurements at the Z resonance, Tests of the Standard Model, Radiative corrections, Effective coupling constants, Neutral weak current, Z boson, W boson, Higgs boson, Particle physics - Experiment, Settore FIS/01 - Fisica Sperimentale, FERMION-PAIR PRODUCTION, HADRONIC-Z-DECAYS, TOP-QUARK MASS, ANGLE BHABHA SCATTERING, W-BOSON MASS, CROSS-SECTION ASYMMETRY, Z-LINE-SHAPE, SEMILEPTONIC BRANCHING RATIOS, CARLO EVENT GENERATOR, decays of heavy intermediate gauge bosons, effective coupling constants, electroweak interactions, fermion-antifermion production, higgs boson, neutral weak current, precision measurements at the z resonance, radiative corrections, tests of the standard model, top quark, w boson, z boson, Radiative correction, High Energy Physics - Phenomenology, FIS/01 - FISICA SPERIMENTALE, Física nuclear, Neutrino, Particle physics, FOS: Physical sciences, ddc:500.2, Elementary particle physics, LEP, electroweak, Decays of heavy intermediate gauge boson, Effective coupling constant, Partícules (Física nuclear), Standard Model, electroweak theory, Z boson, DELPHI, ALEPH, OPAL, L3, 0103 physical sciences, 010306 general physics, Coupling constant, 010308 nuclear & particles physics, High Energy Physics::Phenomenology, Fermion, FORWARD-BACKWARD ASYMMETRY, FERMION-PAIR PRODUCTION, HADRONIC-Z-DECAYS, TOP-QUARK MASS, ANGLE BHABHA SCATTERING, W-BOSON MASS, CROSS-SECTION ASYMMETRY, Z-LINE-SHAPE, SEMILEPTONIC BRANCHING RATIOS, CARLO EVENT GENERATOR, [PHYS.HPHE]Physics [physics]/High Energy Physics - Phenomenology [hep-ph], Experimental High Energy Physics, Electron–positron physic, High Energy Physics::Experiment, FIS/04 - FISICA NUCLEARE E SUBNUCLEARE
Abstract: We report on the final electroweak measurements performed with data taken at the Z resonance by the experiments operating at the electron-positron colliders SLC and LEP. The data consist of 17 million Z decays accumulated by the ALEPH, DELPHI, L3 and OPAL experiments at LEP, and 600 thousand Z decays by the SLD experiment using a polarised beam at SLC. The measurements include cross-sections, forward-backward asymmetries and polarised asymmetries. The mass and width of the Z boson, $\MZ$ and $\GZ$, and its couplings to fermions, for example the $\rho$ parameter and the effective electroweak mixing angle, are precisely measured. The number of light neutrino species is determined to be 2.9840+/-0.0082. The results are compared to the predictions of the Standard Model. Electroweak radiative corrections beyond the running of the QED and QCD coupling constants are observed with a significance of five standard deviations, and in agreement with the Standard Model. Of the many Z-pole measurements, the forward-backward asymmetry in b-quark production shows the largest difference with respect to its Standard Model expectation, at the level of 2.8 standard deviations. Through radiative corrections evaluated in the framework of the Standard Model, the masses of the top quark and the W Boson are predicted. These indirect constraints are compared to the direct measurements, providing a stringent test of the Standard Model. Using in addition the direct measurements of $\Mt$ and $\MW$, the mass of the as yet unobserved Standard Model Higgs boson is predicted., Comment: 302 pages, v2: minor corrections and updates of references. Accepted for publication by Physics Reports, v3: further small corrections and journal version
Published: 2006
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14. Acid–base properties of the nucleic-acid model 2′-deoxyguanylyl(5′→3′)-2′-deoxy-5′-guanylate, d(pGpG)3–, and of related guanine derivatives

Author: Knobloch, B, Sigel, Helmut, Okruszek, A, Sigel, Roland K O, University of Zurich, and Sigel, Roland K O
Subjects: 10120 Department of Chemistry, 1303 Biochemistry, 540 Chemistry, 1606 Physical and Theoretical Chemistry, 1605 Organic Chemistry
Published: 2006
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15. Two metal ions coordinated to a purine residue tolerate each other well

Author: Knobloch, B, Sigel, Roland K O, Lippert, B, Sigel, Helmut, University of Zurich, and Sigel, Roland K O
Subjects: 10120 Department of Chemistry, 1503 Catalysis, 540 Chemistry, 1600 General Chemistry, General Chemistry, Catalysis
Published: 2004
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16. Effect of the ribose versus 2'-deoxyribose residue on the metal ion-binding properties of purine nucleotides

Author: Mucha, A, Knobloch, B, Jezowska-Bojczuk, M, Kozłowski, H, Sigel, Roland K O; https://orcid.org/0000-0002-1307-7993, Mucha, A, Knobloch, B, Jezowska-Bojczuk, M, Kozłowski, H, and Sigel, Roland K O; https://orcid.org/0000-0002-1307-7993
Abstract: The interaction between metal ions and nucleotides is well characterized, as is their importance for metabolic processes, e.g. in the synthesis of nucleic acids. Hence, it is surprising to find that no detailed comparison is available of the metal ion-binding properties between nucleoside 5'-phosphates and 2'-deoxynucleoside 5'-phosphates. Therefore, we have measured here by potentiometric pH titrations the stabilities of several metal ion complexes formed with 2'-deoxyadenosine 5'-monophosphate (dAMP2-), 2'-deoxyadenosine 5'-diphosphate (dADP3-) and 2'-deoxyadenosine 5'-triphosphate (dATP4-). These results are compared with previous data measured under the same conditions and available in the literature for the adenosine 5'-phosphates, AMP(2-), ADP(3-) and ATP(4-), as well as guanosine 5'-monophosphate (GMP(2-)) and 2'-deoxyguanosine 5'-monophosphate (dGMP(2-)). Hence, in total four nucleotide pairs, GMP(2-)/dGMP(2-), AMP(2-)/dAMP(2-), ADP(3-)/dADP(3-) and ATP(4-)/dATP(4-) (= NP/dNP), could be compared for the four metal ions Mg2+, Ni2+, Cu2+ and Zn2+ (= M2+). The comparisons show that complex stability and extent of macrochelate formation between the phosphate-coordinated metal ion and N7 of the purine residue is very similar (or even identical) for the AMP(2-)/dAMP(2-) and ADP(3-)/dADP(3-) pairs. In the case of the complexes formed with ATP(4-)/dATP(4-) the 2'-deoxy complexes are somewhat more stable and show also a slightly enhanced tendency for macrochelate formation. This is different for guanine nucleotides: the stabilities of the M(dGMP) complexes are clearly higher, as are the formation degrees of their macrochelates, than is the case with the M(GMP) complexes. This enhanced complex stability and greater tendency to form macrochelates can be attributed to the enhanced basicity (DeltapKaca. 0.2) of N7 in the 2'-deoxy compound. These results allow general conclusions regarding nucleic acids to be made.
Published: 2008

17. NMR solution structure of the kappa-zeta region of S.cerevisiae group II intron ai5(gamma)

Author: Donghi, D., primary, Pechlaner, M., additional, Finazzo, C., additional, Knobloch, B., additional, and Sigel, R.K.O., additional
Published: 2013
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18. Sekretionsfaktoren von humanem epikardialem Fett können zu Insulinresistenz führen und die Funktion von Kardiomyozyten beeinträchtigen

Author: Greulich, S, primary, Ouwens, DM, additional, Maxhera, B, additional, Herzfeld de Wiza, D, additional, Knobloch, B, additional, Mueller, H, additional, Smiris, K, additional, Lichtenberg, A, additional, and Eckel, J, additional
Published: 2010
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19. The structural stabilization of the κ three-way junction by Mg(II) represents the first step in the folding of a group II intron.

Author: Donghi D, Pechlaner M, Finazzo C, Knobloch B, and Sigel RK
Subjects: Base Sequence, Binding Sites, Cobalt chemistry, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Nucleic Acid Conformation, Protons, RNA Folding, Introns, Magnesium chemistry
Abstract: Folding of group II introns is characterized by a first slow compaction of domain 1 (D1) followed by the rapid docking of other domains to this scaffold. D1 compaction initiates in a small subregion encompassing the κ and ζ elements. These two tertiary elements are also the major interaction sites with domain 5 to form the catalytic core. Here, we provide the first characterization of the structure adopted at an early folding step and show that the folding control element can be narrowed down to the three-way junction with the κ motif. In our nuclear magnetic resonance studies of this substructure derived from the yeast mitochondrial group II intron Sc.ai5γ, we show that a high affinity Mg(II) ion stabilizes the κ element and enables coaxial stacking between helices d' and d'', favoring a rigid duplex across the three-way junction. The κ-element folds into a stable GAAA-tetraloop motif and engages in A-minor interactions with helix d'. The addition of cobalt(III)hexammine reveals three distinct binding sites. The Mg(II)-promoted structural rearrangement and rigidification of the D1 core can be identified as the first micro-step of D1 folding.
Published: 2013
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20. Stability and structure of mixed-ligand metal ion complexes that contain Ni2+, Cu2+, or Zn2+, and Histamine, as well as adenosine 5'-triphosphate (ATP4-) or uridine 5'-triphosphate (UTP(4-): an intricate network of equilibria.

Author: Knobloch B, Mucha A, Operschall BP, Sigel H, Jeżowska-Bojczuk M, Kozłowski H, and Sigel RK
Subjects: Hydrogen-Ion Concentration, Isomerism, Molecular Structure, Adenosine Triphosphate chemistry, Coordination Complexes chemistry, Copper chemistry, Histamine chemistry, Models, Chemical, Nickel chemistry, Uridine Triphosphate chemistry, Zinc chemistry
Abstract: With a view on protein-nucleic acid interactions in the presence of metal ions we studied the "simple" mixed-ligand model systems containing histamine (Ha), the metal ions Ni(2+), Cu(2+), or Zn(2+) (M(2+)), and the nucleotides adenosine 5'-triphosphate (ATP(4-)) or uridine 5'-triphosphate (UTP(4-)), which will both be referred to as nucleoside 5'-triphosphate (NTP(4-)). The stability constants of the ternary M(NTP)(Ha)(2-) complexes were determined in aqueous solution by potentiometric pH titrations. We show for both ternary-complex types, M(ATP)(Ha)(2-) and M(UTP)(Ha)(2-), that intramolecular stacking between the nucleobase and the imidazole residue occurs and that the stacking intensity is approximately the same for a given M(2+) in both types of complexes: The formation degree of the intramolecular stacks is estimated to be 20 to 50%. Consequently, in protein-nucleic acid interactions imidazole-nucleobase stacks may well be of relevance. Furthermore, the well-known formation of macrochelates in binary M(2+) complexes of purine nucleotides, that is, the phosphate-coordinated M(2+) interacts with N7, is confirmed for the M(ATP)(2-) complexes. It is concluded that upon formation of the mixed-ligand complexes the M(2+)-N7 bond is broken and the energy needed for this process corresponds to the stability differences determined for the M(UTP)(Ha)(2-) and M(ATP)(Ha)(2-) complexes. It is, therefore, possible to calculate from these stability differences of the ternary complexes the formation degrees of the binary macrochelates: The closed forms amount to (65±10)%, (75±8)%, and (31±14) % for Ni(ATP)(2-), Cu(ATP)(2-), and Zn(ATP)(2-), respectively, and these percentages agree excellently with previous results obtained by different methods, confirming thus the internal validity of the data and the arguments used in the evaluation processes. Based on the overall results it is suggested that M(ATP)(2-) species, when bound to an enzyme, may exist in a closed macrochelated form only, if no enzyme groups coordinate directly to the metal ion., (Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)
Published: 2011
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21. Effect of the ribose versus 2'-deoxyribose residue on the metal ion-binding properties of purine nucleotides.

Author: Mucha A, Knobloch B, Jezowska-Bojczuk M, Kozłowski H, and Sigel RK
Subjects: Adenosine Diphosphate chemistry, Hydrogen-Ion Concentration, Ions, Kinetics, Models, Chemical, Nucleic Acids chemistry, Nucleosides chemistry, Potentiometry, Protein Binding, Purines chemistry, Temperature, Metals chemistry, Nucleotides chemistry
Abstract: The interaction between metal ions and nucleotides is well characterized, as is their importance for metabolic processes, e.g. in the synthesis of nucleic acids. Hence, it is surprising to find that no detailed comparison is available of the metal ion-binding properties between nucleoside 5'-phosphates and 2'-deoxynucleoside 5'-phosphates. Therefore, we have measured here by potentiometric pH titrations the stabilities of several metal ion complexes formed with 2'-deoxyadenosine 5'-monophosphate (dAMP2-), 2'-deoxyadenosine 5'-diphosphate (dADP3-) and 2'-deoxyadenosine 5'-triphosphate (dATP4-). These results are compared with previous data measured under the same conditions and available in the literature for the adenosine 5'-phosphates, AMP(2-), ADP(3-) and ATP(4-), as well as guanosine 5'-monophosphate (GMP(2-)) and 2'-deoxyguanosine 5'-monophosphate (dGMP(2-)). Hence, in total four nucleotide pairs, GMP(2-)/dGMP(2-), AMP(2-)/dAMP(2-), ADP(3-)/dADP(3-) and ATP(4-)/dATP(4-) (= NP/dNP), could be compared for the four metal ions Mg2+, Ni2+, Cu2+ and Zn2+ (= M2+). The comparisons show that complex stability and extent of macrochelate formation between the phosphate-coordinated metal ion and N7 of the purine residue is very similar (or even identical) for the AMP(2-)/dAMP(2-) and ADP(3-)/dADP(3-) pairs. In the case of the complexes formed with ATP(4-)/dATP(4-) the 2'-deoxy complexes are somewhat more stable and show also a slightly enhanced tendency for macrochelate formation. This is different for guanine nucleotides: the stabilities of the M(dGMP) complexes are clearly higher, as are the formation degrees of their macrochelates, than is the case with the M(GMP) complexes. This enhanced complex stability and greater tendency to form macrochelates can be attributed to the enhanced basicity (DeltapKaca. 0.2) of N7 in the 2'-deoxy compound. These results allow general conclusions regarding nucleic acids to be made.
Published: 2008
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22. Inosylyl(3'-->5')inosine (IpI-). Acid-base and metal ion-binding properties of a dinucleoside monophosphate in aqueous solution.

Author: Knobloch B, Okruszek A, and Sigel H
Subjects: Chelating Agents chemistry, Ions chemistry, Molecular Structure, Solutions, Acids chemistry, Dinucleoside Phosphates chemistry, Inosine chemistry, Metals chemistry, Nucleotides chemistry
Abstract: The acidity constants of the (N7)H(+) sites of inosylyl(3'-->5')inosine (IpI(-)) were estimated and those of its (N1)H sites were measured by potentiometric pH titrations in aqueous solution (25 degrees C; I = 0.1 M, NaNO3). The same method was used for the determination of the stability constants of the 1:1 complexes formed between Mg(2+), Co(2+), Ni(2+), Zn(2+), or Cd(2+) (= M(2+)) and (IpI - H)(2-) and, in the case of Mg(2+), also of (IpI - 2H)(3-). The stability constants of the M(IpI)(+) complexes were estimated. The acidity constants of H(inosine)(+) and the stability constants of the M(Ino)(2+) and M(Ino - H)(+) complexes were taken from the literature. The comparison of these and related data allows the conclusion that, in the M(IpI - H) species, chelates are formed; most likely they are preferably of an N7/N7 type. For the metal ions Co(2+), Ni(2+), Zn(2+), or Cd(2+), the formation degrees of the chelates are on the order of 60-80%; no chelates could be detected for the Mg(IpI - H) complexes. It is noteworthy that the (N1)H deprotonation, which leads to the M(IpI - H) species, occurs in all M(IpI)(+) complexes in the physiological pH range of about 7.5 or even below.
Published: 2008
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23. Comparison of the acid-base properties of ribose and 2'-deoxyribose nucleotides.

Author: Mucha A, Knobloch B, Jezowska-Bojczuk M, Kozłowski H, and Sigel RK
Subjects: Hydrogen-Ion Concentration, Magnetic Resonance Spectroscopy, Acids chemistry, Alkalies chemistry, Deoxyribose chemistry, Nucleotides chemistry, Ribose chemistry
Abstract: The extent to which the replacement of a ribose unit by a 2'-deoxyribose unit influences the acid-base properties of nucleotides has not hitherto been determined in detail. In this study, by potentiometric pH titrations in aqueous solution, we have measured the acidity constants of the 5'-di- and 5'-triphosphates of 2'-deoxyguanosine [i.e., of H(2)(dGDP)(-) and H(2)(dGTP)(2-)] as well as of the 5'-mono-, 5'-di-, and 5'-triphosphates of 2'-deoxyadenosine [i.e., of H(2)(dAMP)(+/-), H(2)(dADP)(-), and H(2)(dATP)(2-)]. These 12 acidity constants (of the 56 that are listed) are compared with those of the corresponding ribose derivatives (published data) measured under the same experimental conditions. The results show that all protonation sites in the 2'-deoxynucleotides are more basic than those in their ribose counterparts. The influence of the 2'-OH group is dependent on the number of 5'-phosphate groups as well as on the nature of the purine nucleobase. The basicity of N7 in guanine nucleotides is most significantly enhanced (by about 0.2 pK units), while the effect on the phosphate groups and the N1H or N1H(+) sites is less pronounced but clearly present. In addition, (1)H NMR chemical shift change studies in dependence on pD in D(2)O have been carried out for the dAMP, dADP, and dATP systems, which confirmed the results from the potentiometric pH titrations and showed the nucleotides to be in their anti conformations. Overall, our results are not only of relevance for metal ion binding to nucleotides or nucleic acids, but also constitute an exact basis for the calculation, determination, and understanding of perturbed pK(a) values in DNAzymes and ribozymes, as needed for the delineation of acid-base mechanisms in catalysis.
Published: 2008
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24. Discrimination in metal-ion binding to RNA dinucleotides with a non-bridging oxygen or sulfur in the phosphate diester link.

Author: Knobloch B, Nawrot B, Okruszek A, and Sigel RK
Subjects: Binding Sites, Hydrogen-Ion Concentration, Ions chemistry, Nucleic Acid Conformation, Oligonucleotides chemical synthesis, Organometallic Compounds chemical synthesis, Organometallic Compounds chemistry, Metals chemistry, Oligonucleotides chemistry, Organophosphates chemistry, Oxygen chemistry, RNA chemistry, Sulfur chemistry
Abstract: Replacement of a non-bridging oxygen in the phosphate diester bond by a sulfur has become quite popular in nucleic acid research and is often used as a probe, for example, in ribozymes, where the normally essential Mg(2+) is partly replaced by a thiophilic metal ion to reactivate the system. Despite these widely applied rescue experiments no detailed studies exist quantifying the affinity of metal ions to such terminal sulfur atoms. Therefore, we performed potentiometric pH titrations to determine the binding properties of pUp((S))U(3-) towards Mg(2+), Mn(2+), Zn(2+), Cd(2+), and Pb(2+), and compared these data with those previously obtained for the corresponding pUpU(3-) complexes. The primary binding site in both dinucleotides is the terminal phosphate group. Theoretically, also the formation of 10-membered chelates involving the terminal oxygen or sulfur atoms of the (thio)phosphate bridge is possible with both ligands. The results show that Mg(2+) and Mn(2+) exist as open (op) isomers binding to both dinucleotides only at the terminal phosphate group. Whereas Cd(pUpU)(-) only exists as Cd(pUpU)(-)(op), Cd(pUp((S))U)(-) is present to about 64 % as the S-coordinated macrochelate, Cd(pUp((S))U)(-)(cl/PS). Zn(2+) forms with pUp((S))U(3-) three isomeric species, that is, Zn(pUp((S))U)(-)(op), Zn(pUp((S))U)(-)(cl/PO), and Zn(pUp((S))U)(-)(cl/PS), which occur to about 33, 12 (O-bound), and 55 %, respectively. Pb(2+) forms the 10-membered chelate with both nucleotides involving only the terminal oxygen atoms of the (thio)phosphate bridge, that is, no indication of S binding was discovered in this case. Hence, Zn(2+) and Cd(2+) show pronounced thiophilic properties, whereas Mg(2+), Mn(2+), and Pb(2+) coordinate to the oxygen, macrochelate formation being of relevance with Pb(2+) only.
Published: 2008
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25. Metal-ion-coordinating properties of the dinucleotide 2'-deoxyguanylyl(5'-->3')-2'-deoxy-5'-guanylate (d(pGpG)3-): isomeric equilibria including macrochelated complexes relevant for nucleic acids.

Author: Knobloch B, Sigel H, Okruszek A, and Sigel RK
Subjects: Cations, Divalent, Hydrogen-Ion Concentration, Isomerism, Molecular Structure, Phosphates chemistry, Chelating Agents chemistry, Deoxyguanine Nucleotides chemistry, Metals chemistry, Nucleic Acids chemistry, Organometallic Compounds chemistry
Abstract: The interaction between divalent metal ions and nucleic acids is well known, yet knowledge about the strength of binding of labile metal ions at the various sites is very scarce. We have therefore studied the stabilities of complexes formed between the nucleic acid model d(pGpG) and the essential metal ions Mg2+ and Zn2+ as well as with the generally toxic ions Cd2+ and Pb2+ by potentiometric pH titrations; all four ions are of relevance in ribozyme chemistry. A comparison of the present results with earlier data obtained for M(pUpU)- complexes allows the conclusion that phosphate-bound Mg2+ and Cd2+ form macrochelates by interaction with N7, whereas the also phosphate-coordinated Pb2+ forms a 10-membered chelate with the neighboring phosphate diester bridge. Zn2+ forms both types of chelates with formation degrees of about 91% and 2.4% for Zn[d(pGpG)]cl/N7 and Zn[d(pGpG)]-cl/PO, respectively; the open form with Zn2+ bound only to the terminal phosphate group, Zn[d(pGpG)]-op, amounts to about 6.8 %. The various intramolecular equilibria have also been quantified for the other metal ions. Zn2+, Cu2+, and Cd2+ also form macrochelates in the monoprotonated M[H;d(pGpG)] species (the proton being at the terminal phosphate group), that is, the metal ion at N7 interacts to some extent with the P(O)2(OH)- group. Thus, this study demonstrates that the coordinating properties of the various metal ions toward a pGpG unit in a nucleic acid differ: Mg2+, Zn2+, and Cd2+ have a significant tendency to bridge the distance between N7 and the phosphate group of a (d)GMP unit, although to various extents, whereas Pb2+ (and possibly Ca2+) prefer a pure phosphate coordination.
Published: 2007
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26. Acid-base and metal-ion-binding properties of xanthosine 5'-monophosphate (XMP) in aqueous solution: complex stabilities, isomeric equilibria, and extent of macrochelation.

Author: Sigel H, Massoud SS, Song B, Griesser R, Knobloch B, and Operschall BP
Subjects: Acids chemistry, Alkalies chemistry, Hydrogen-Ion Concentration, Ions chemistry, Potentiometry, Solubility, Solutions chemistry, Stereoisomerism, Water chemistry, Xanthine, Chelating Agents chemistry, Metals chemistry, Ribonucleotides chemistry
Abstract: The four acidity constants of threefold protonated xanthosine 5'-monophosphate, H3(XMP)+, reveal that at the physiological pH of 7.5 (XMP-H)(3-) strongly dominates (and not XMP(2-) as given in textbooks); this is in contrast to the related inosine (IMP(2-)) and guanosine 5'-monophosphate (GMP(2-)) and it means that XMP should better be named as xanthosinate 5'-monophosphate. In addition, evidence is provided for a tautomeric (XMP-HN1)(3-)/(XMP-HN3)(3-) equilibrium. The stability constants of the M(H;XMP)+ species were estimated and those of the M(XMP) and M(XMP-H)- complexes (M2+=Mg2+, Ca2+, Sr2+, Ba2+, Mn2+, Co2+, Ni2+, Cu2+, Zn2+, Cd2+) measured potentiometrically in aqueous solution. The primary M2+ binding site in M(XMP) is (mostly) N7 of the monodeprotonated xanthine residue, the proton being at the phosphate group. The corresponding macrochelates involving P(O)2(OH)- (most likely outer-sphere) are formed to approximately 65% for nearly all M2+. In M(XMP-H)- the primary M2+ binding site is (mostly) the phosphate group; here the formation degree of the N7 macrochelates varies widely from close to zero for the alkaline earth ions, to approximately 50% for Mn2+, and approximately 90% or more for Co2+, Ni2+, Cu2+, Zn2+, and Cd2+. Because for (XMP-H)(3-) the micro stability constants quantifying the M2+ affinity of the xanthosinate and PO3(2-) residues are known, one may apply a recently developed quantification method for the chelate effect to the corresponding macrochelates; this chelate effect is close to zero for the alkaline earth ions and it amounts to about one log unit for Co2+, Ni2+, Cu2+. This method also allows calculation of the formation degrees of the monodentatally coordinated isomers; this information is of relevance for biological systems because it demonstrates how metal ions can switch from one site to another through macrochelate formation. These insights are meaningful for metal-ion-dependent reactions of XMP in metabolic pathways; previous mechanistic proposals based on XMP(2-) need revision.
Published: 2006
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27. Acid-base properties of the nucleic-acid model 2'-deoxyguanylyl(5'-->3')-2'-deoxy-5'-guanylate, d(pGpG)3-, and of related guanine derivatives.

Author: Knobloch B, Sigel H, Okruszek A, and Sigel RK
Subjects: Guanosine Monophosphate chemistry, Kinetics, Molecular Conformation, Uridine Monophosphate chemistry, Deoxyguanine Nucleotides chemistry, Dideoxynucleosides chemistry, Guanine analogs & derivatives, Guanine chemistry, Hydrogen-Ion Concentration
Abstract: The dinucleotide d(pGpG) is an often employed DNA model to study various kinds of interactions between DNA and metal ions, but its acid-base properties were not yet described in detail. In this study the six deprotonation reactions of H4[d(pGpG)]+ are quantified. The acidity constants for the release of the first proton from the terminal P(O)(OH)2 group (pKa = 0.65) and for one of the (N7)H+ sites (pKa = 2.4) are estimated. The acidity constants of the remaining four deprotonation reactions were measured by potentiometric pH titrations in aqueous solution (25 degrees C; I = 0.1 M, NaNO3): The pKa values for the deprotonations of the second (N7)H+, the P(O)2(OH)-, and the two (N1)H sites are 2.98, 6.56, 9.54 and 10.11, respectively. Based on these results we show how to estimate acidity constants for related systems that have not been studied, e.g. pGpG, which is involved in the initiation step of a rotavirus RNA polymerase. The relevance of our results for nucleic acids in general is briefly indicated.
Published: 2006
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28. Acid-base and metal-ion binding properties of the RNA dinucleotide uridylyl-(5'-->3')-[5']uridylate (pUpU3-).

Author: Knobloch B, Suliga D, Okruszek A, and Sigel RK
Subjects: Hydrogen-Ion Concentration, Ions chemistry, Molecular Structure, Metals chemistry, Nucleotides chemistry, RNA chemistry, Uridine Monophosphate analogs & derivatives, Uridine Monophosphate chemistry
Abstract: It is well known that Mg2+ and other divalent metal ions bind to the phosphate groups of nucleic acids. Subtle differences in the coordination properties of these metal ions to RNA, especially to ribozymes, determine whether they either promote or inhibit catalytic activity. The ability of metal ions to coordinate simultaneously with two neighboring phosphate groups is important for ribozyme structure and activity. However, such an interaction has not yet been quantified. Here, we have performed potentiometric pH titrations to determine the acidity constants of the protonated dinucleotide H2(pUpU)-, as well as the binding properties of pUpU3- towards Mg2+, Mn2+, Cd2+, Zn2+, and Pb2+. Whereas Mg2+, Mn2+, and Cd2+ only bind to the more basic 5'-terminal phosphate group, Pb2+, and to a certain extent also Zn2+, show a remarkably enhanced stability of the [M(pUpU)]- complex. This can be attributed to the formation of a macrochelate by bridging the two phosphate groups within this dinucleotide by these metal ions. Such a macrochelate is also possible in an oligonucleotide, because the basic structural units are the same, despite the difference in charge. The formation degrees of the macrochelated species of [Zn(pUpU)]- and [Pb(pUpU)]- amount to around 25 and 90 %, respectively. These findings are important in the context of ribozyme and DNAzyme catalysis, and explain, for example, why the leadzyme could be selected in the first place, and why this artificial ribozyme is inhibited by other divalent metal ions, such as Mg2+.
Published: 2005
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29. Metal ion-binding properties of (N3)-deprotonated uridine, thymidine, and related pyrimidine nucleosides in aqueous solution.

Author: Knobloch B, Linert W, and Sigel H
Subjects: Acid-Base Equilibrium, Hydrogen-Ion Concentration, Ligands, Magnetic Resonance Spectroscopy, Potentiometry, Water chemistry, Cations chemistry, Chelating Agents chemistry, Metals chemistry, Pyrimidine Nucleosides chemistry
Abstract: The acidity constants for (N3)H of the uridine-type ligands (U) 5-fluorouridine, 5-chloro-2'-deoxyuridine, uridine, and thymidine (2'-deoxy-5-methyluridine) and the stability constants of the M(U-H)(+) complexes for M(2+) = Mg(2+), Ca(2+), Sr(2+), Ba(2+), Mn(2+), Co(2+), Ni(2+), Cu(2+), Zn(2+), Cd(2+), and Pb(2+) were measured (potentiometric pH titrations; aqueous solution; 25 degrees C; I = 0.1 M, NaNO(3)). Plots of logK(M(U-H))(M) vs. pK(U)(H) result in straight lines that are compared with previous plots for simple pyridine-type and o-amino(methyl)pyridine-type ligands as well as with the stabilities of the corresponding M(cytidine)(2+) complexes. The results indicate monodentate coordination to (N3)(-) in M(U-H)(+) for Co(2+) and Ni(2+). For the M(U-H)(+) species of Cd(2+), Zn(2+), or Cu(2+), increased stabilities imply that semichelates form, i.e., M(2+) is (N3)(-)-bound and coordinated water molecules form hydrogen bonds to (C2)O and (C4)O; these "double" semichelates are in equilibrium with "single" semichelates involving either (C2)O or (C4)O and possibly also with four-membered chelates for which M(2+) is innersphere-coordinated to (N3)(-) and a carbonyl oxygen. For the alkaline earth ions, semichelates dominate with the M(2+) outersphere bound to (N3)(-) and innersphere to one of the carbonyl oxygens. Mn(U-H)(+) is with its properties between those of Cd(2+) (which probably also hold for Pb(2+)) and the alkaline earth ions. In nucleic acids, M(2+)-C(O) interactions are expected, if support is provided by other primary binding sites. (N3)H may possibly be acidified via carbonyl-coordinated M(2+) to become a proton donor in the physiological pH range, at which direct (N3)(-) binding of M(2+) also seems possible.
Published: 2005
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30. Two metal ions coordinated to a purine residue tolerate each other well.

Author: Knobloch B, Sigel RK, Lippert B, and Sigel H
Published: 2004
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31. A quantitative appraisal of the ambivalent metal ion binding properties of cytidine in aqueous solution and an estimation of the anti-syn energy barrier of cytidine derivatives.

Author: Knobloch B and Sigel H
Subjects: Binding Sites, Calcium chemistry, Calcium metabolism, Isomerism, Magnesium chemistry, Magnesium metabolism, Manganese chemistry, Manganese metabolism, Solubility, Water chemistry, Cytidine chemistry, Cytidine metabolism, Metals chemistry, Metals metabolism
Abstract: The recently defined log K (M)(M)(L) versus pK(H)(H)(L) straight-line plots for L = pyridine-type (PyN) and ortho-aminopyridine-type (oPyN) ligands now allow the evaluation in a quantitative manner of the stability of the 1:1 complexes formed between cytidine (Cyd) and Ca(2+), Mg(2+), Mn(2+), Co(2+), Ni(2+), Cu(2+), Zn(2+) or Cd(2+) (M(2+)); the corresponding stability constants, K(M)(M)(Cyd) including the acidity constant, K(H)(H)(Cyd) for the deprotonation of the (N3)H(+) site had been determined previously under exactly the same conditions as the mentioned plots. Since the stabilities of the M(PyN)(2+) and M(oPyN)(2+) complexes of Ca(2+) and Mg(2+) are practically identical, it is concluded that complex formation occurs in an outer-sphere manner, and this is in accord with the fact that in the p K(a) range 3-7 metal ion binding is independent of K(H)(H)(Pyn) or K(H)(H)(oPyN). Ca(Cyd)(2+) and Mg(Cyd)(2+) are more stable than the corresponding (outer-sphere) M(PyN)(2+) complexes and this means that the C2 carbonyl group of Cyd must participate, next to N3 which is most likely outer-sphere, in metal ion binding, leading thus to chelates; these have formation degrees of about 50% and 35%, respectively. Co(Cyd)(2+) and Ni(Cyd)(2+) show no increased stability based on the log K(M)(M)(oPyN) versus pK(H)(H)(oPyN) hence, the (C2)O group does not participate in metal ion binding, but the inner-sphere coordination to N3 is strongly inhibited by the (C4)NH(2) group. In the M(Cyd)(2+) complexes of Mn(2+), Cu(2+), Zn(2+) and Cd(2+), this inhibiting effect on M(2+) binding at N3 is partially compensated by participation of the (C2)O group in complex formation and the corresponding chelates have formation degrees between about 30% (Zn(2+)) and 83% (Cu(2+)). The different structures of the mentioned chelates are discussed in relation to available crystal structure analyses. (1). There is evidence (crystal structure studies: Cu(2+), Zn(2+), Cd(2+)) that four-membered rings form, i.e. there is a strong M(2+) bond to N3 and a weak one to (C2)O. (2). By hydrogen bond formation to (C2)O of a metal ion-bound water molecule, six-membered rings, so-called semichelates, may form. (3). For Ca(2+) and Mg(2+), and possibly Mn(2+), and their Cyd complexes, six-membered chelates are also likely with (C2)O being inner-sphere (crystal structure) and N3 outer-sphere. (4). Finally, for these metal ions also complexes with a sole outer-sphere interaction may occur. All these types of chelates are expected to be in equilibrium with each other in solution, but, depending on the metal ion, either the one or the other form will dominate. Clearly, the cytidine residue is an ambivalent binding site which adjusts well to the requirements of the metal ion to be bound and this observation is of relevance for single-stranded nucleic acids and their interactions with metal ions. In addition, the anti- syn energy barrier has been estimated as being in the order of 6-7.5 kJ/mol for cytidine derivatives in aqueous solution at 25 degrees C.
Published: 2004
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32. [Effect of glucocorticosteroids on the liver function of fasting sheep].

Author: Fürll M and Knobloch B
Subjects: Animals, Bilirubin blood, Blood Glucose metabolism, Fatty Acids, Nonesterified blood, Female, Insulin blood, Liver physiology, Fasting physiology, Liver drug effects, Prednisolone pharmacology, Sheep physiology
Abstract: During a five-day fasting period prednisolone (30 mg/d) reduced strongly as a result of induced hyperglycemia and hyperinsulinaemia the rise of FFA and bilirubin in six nonpregnant ewes in contrast to six control animals. The liver fat content remained in treated ewes within the physiological range, but in control animals the fat concentration increased to 300 g/kg. beta-OH-butyrate was only a little influenced. Harmful effects on the liver function in prednisolone treated ewes could not be observed. Plasma cortisol concentration contradicted a depression of endogenous cortisol secretion.
Published: 1994

33. [Effects of glucocorticosteroids on the fat metabolism and liver function in nonpregnant, nonlactating cows].

Author: Fürll M and Knobloch B
Subjects: 3-Hydroxybutyric Acid, Animals, Aspartate Aminotransferases blood, Bilirubin blood, Blood Glucose analysis, Fatty Acids, Nonesterified blood, Female, Glycerol blood, Hydroxybutyrates blood, Insulin blood, Lipolysis drug effects, Liver physiology, Liver Glycogen metabolism, Urea blood, Cattle physiology, Lipid Metabolism, Liver drug effects, Prednisolone pharmacology
Abstract: Following a five-day course of prednisolone (200 mg/d) the glucose, urea and insulin concentrations in the blood plasma as well as the glycogen content in the liver increased significantly in five nonpregnant, nonlactating cows compared with five control animals. In both groups the FFA, bilirubin and beta-OH-butyrate concentrations, the ASAT activities as well as the liver lipid concentration did not change. Under these conditions prednisolone does not stimulate lipolysis, nor does it disturb liver function in cows.
Published: 1993

34. [The effects of glucocorticosteroids on lipolysis stimulated by fasting and liver function in cows].

Author: Fürll M, Kirbach H, and Knobloch B
Subjects: 3-Hydroxybutyric Acid, Animals, Aspartate Aminotransferases blood, Bilirubin blood, Blood Glucose analysis, Cattle blood, Cattle metabolism, Energy Metabolism drug effects, Fasting physiology, Fatty Acids, Nonesterified blood, Female, Glutamate Dehydrogenase blood, Hydrocortisone blood, Hydroxybutyrates blood, Insulin blood, Lipids analysis, Liver chemistry, Liver physiology, Liver Glycogen analysis, Urea blood, Cattle physiology, Lipolysis drug effects, Liver drug effects, Prednisolone pharmacology
Abstract: During a five-day period prednisolone (200 mg/d) reduced the rise of FFA, beta-hydroxybutyrate and bilirubin concentrations in the blood plasma of three cows compared with three control animals. The liver fat content remained within the physiological range. The reduced lipolysis in the experimental group was the result of a reactive hyperinsulinaemia, a more effective energy metabolism and a diminished metabolic activity. Harmful effects on the liver function could not be observed. Plasma cortisol concentration was reduced for only a short time.
Published: 1993

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34 results on '"Knobloch, B"'

1. Arc-to-pocket transition and quantitative understanding of transport properties in cuprate superconductors

2. Transport properties and doping evolution of the Fermi surface in cuprates

3. Characterization of two electronic subsystems in cuprates through optical conductivity

4. NOT RESOURCE CURSE NOR RESOURCE BENEFIT, BUT 'RESOURCE NEGATION'? COMMUNITIES AGAINST COAL SEAM GAS ON THE FOSSIL FRONTIER

5. Anisotropy of electronic correlations: On the applicability of local theories to layered materials

6. Rolle von Omentin als kardioprotektives Adipokin: V 38

7. Effects of Glucocorticoids on Immunological Parameters and on Fat Metabolism During Short Time Treatment

8. Effects of Glucocorticoids on Immunological Parameters and on Fat Metabolism During Short Time Treatment

9. Accurate analysis of Mg2+ binding to RNA: From classical methods to a novel iterative calculation procedure

10. Stability and Structure of Mixed-Ligand Metal Ion Complexes That Contain Ni(2+), Cu(2+), or Zn(2+), and Histamine, as well as Adenosine 5 '-Triphosphate (ATP(4-)) or Uridine 5 '-Triphosphate (UTP(4-)): An Intricate Network of Equilibria

11. Comparison of the acid-base properties of ribose and 2'-deoxyribose nucleotides

12. Metal-Ion-Coordinating Properties of the Dinucleotide 2′-Deoxyguanylyl(5′→3′)-2′-deoxy-5′-guanylate (d(pGpG)3−): Isomeric Equilibria Including Macrochelated Complexes Relevant for Nucleic Acids

13. Precision electroweak measurements on the Z resonance

14. Acid–base properties of the nucleic-acid model 2′-deoxyguanylyl(5′→3′)-2′-deoxy-5′-guanylate, d(pGpG)3–, and of related guanine derivatives

15. Two metal ions coordinated to a purine residue tolerate each other well

16. Effect of the ribose versus 2'-deoxyribose residue on the metal ion-binding properties of purine nucleotides

17. NMR solution structure of the kappa-zeta region of S.cerevisiae group II intron ai5(gamma)

18. Sekretionsfaktoren von humanem epikardialem Fett können zu Insulinresistenz führen und die Funktion von Kardiomyozyten beeinträchtigen

19. The structural stabilization of the κ three-way junction by Mg(II) represents the first step in the folding of a group II intron.

20. Stability and structure of mixed-ligand metal ion complexes that contain Ni2+, Cu2+, or Zn2+, and Histamine, as well as adenosine 5'-triphosphate (ATP4-) or uridine 5'-triphosphate (UTP(4-): an intricate network of equilibria.

21. Effect of the ribose versus 2'-deoxyribose residue on the metal ion-binding properties of purine nucleotides.

22. Inosylyl(3'-->5')inosine (IpI-). Acid-base and metal ion-binding properties of a dinucleoside monophosphate in aqueous solution.

23. Comparison of the acid-base properties of ribose and 2'-deoxyribose nucleotides.

24. Discrimination in metal-ion binding to RNA dinucleotides with a non-bridging oxygen or sulfur in the phosphate diester link.

25. Metal-ion-coordinating properties of the dinucleotide 2'-deoxyguanylyl(5'-->3')-2'-deoxy-5'-guanylate (d(pGpG)3-): isomeric equilibria including macrochelated complexes relevant for nucleic acids.

26. Acid-base and metal-ion-binding properties of xanthosine 5'-monophosphate (XMP) in aqueous solution: complex stabilities, isomeric equilibria, and extent of macrochelation.

27. Acid-base properties of the nucleic-acid model 2'-deoxyguanylyl(5'-->3')-2'-deoxy-5'-guanylate, d(pGpG)3-, and of related guanine derivatives.

28. Acid-base and metal-ion binding properties of the RNA dinucleotide uridylyl-(5'-->3')-[5']uridylate (pUpU3-).

29. Metal ion-binding properties of (N3)-deprotonated uridine, thymidine, and related pyrimidine nucleosides in aqueous solution.

30. Two metal ions coordinated to a purine residue tolerate each other well.

31. A quantitative appraisal of the ambivalent metal ion binding properties of cytidine in aqueous solution and an estimation of the anti-syn energy barrier of cytidine derivatives.

32. [Effect of glucocorticosteroids on the liver function of fasting sheep].

33. [Effects of glucocorticosteroids on the fat metabolism and liver function in nonpregnant, nonlactating cows].

34. [The effects of glucocorticosteroids on lipolysis stimulated by fasting and liver function in cows].

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