@article{EdgecockCarettaDavenneetal.2013,
  author    = {Edgecock, T. R. and Caretta, O. and Davenne, T. and Densam, C. and Fitton, M. and Kelliher, D. and Loveridge, P. and Machida, S. and Prior, C. and Rogers, C. and Rooney, M. and Thomason, J. and Wilcox, D. and Wildner, E. and Efthymiopoulos, I. and Garoby, R. and Gilardoni, S. and Hansen, C. and Benedetto, E. and Jensen, E. and Kosmicki, A. and Martini, M. and Osborne, J. and Prior, G. and Stora, T. and Melo Mendonca, T. and Vlachoudis, V. and Waaijer, C. and Cupial, P. and Chanc{\´e}, A. and Longhin, A. and Payet, J. and Zito, M. and Baussan, E. and Bobeth, C. and Bouquerel, E. and Dracos, M. and Gaudiot, G. and Lepers, B. and Osswald, F. and Poussot, P. and Vassilopoulos, N. and Wurtz, J. and Zeter, V. and Bielski, J. and Kozien, M. and Lacny, L. and Skoczen, B. and Szybinski, B. and Ustrycka, A. and Wroblewski, A. and Marie-Jeanne, M. and Balint, P. and Fourel, C. and Giraud, J. and Jacob, J. and Lamy, T. and Latrasse, L. and Sortais, P. and Thuillier, T. and Mitrofanov, S. and Loiselet, M. and Keutgen, Th. and Delbar, Th. and Debray, F. and Trophine, C. and Veys, S. and Daversin, C. and Zorin, V. and Izotov, I. and Skalyga, V. and Burt, G. and Dexter, A. C. and Kravchuk, V. L. and Marchi, T. and Cinausero, M. and Gramegna, F. and De Angelis, G. and Prete, G. and Collazuol, G. and Laveder, M. and Mazzocco, M. and Mezzetto, M. and Signorini, C. and Vardaci, E. and Di Nitto, A. and Brondi, A. and La Rana, G. and Migliozzi, P. and Moro, R. and Palladino, V. and Gelli, N. and Berkovits, D. and Hass, M. and Hirsh, T. Y. and Schuhmann, M. and Stahl, A. and Wehner, J. and Bross, A. and Kopp, J. and Neuffer, D. and Wands, R. and Bayes, R. and Laing, A. and Soler, P. and Agarwalla, S. K. and Cervera Villanueva, A. and Donini, A. and Ghosh, T. and G{\´o}mez Cadenas, J. J. and Hern{\´a}ndez, P. and Mart{\´i}n-Albo, J. and Mena, O. and Burguet-Castell, J. and Agostino, L. and Buizza-Avanzini, M. and Marafini, M. and Patzak, T. and Tonazzo, A. and Duchesneau, D. and Mosca, L. and Bogomilov, M. and Karadzhov, Y. and Matev, R. and Tsenov, R. and Akhmedov, E. and Blennow, M. and Lindner, M. and Schwetz, T. and Fern{\´a}ndez Martinez, E. and Maltoni, M. and Men{\´e}ndez, J. and Giunti, C. and Gonz{\´a}lez Garc{\´i}a, M. C. and Salvado, J. and Coloma, P. and Huber, P. and Li, T. and L{\´o}pez Pav{\´o}n, J. and Orme, C. and Pascoli, S. and Meloni, D. and Tang, J. and Winter, W. and Ohlsson, T. and Zhang, H. and Scotto-Lavina, L. and Terranova, F. and Bonesini, M. and Tortora, L. and Alekou, A. and Aslaninejad, M. and Bontoiu, C. and Kurup, A. and Jenner, L. J. and Long, K. and Pasternak, J. and Pozimski, J. and Back, J. J. and Harrison, P. and Beard, K. and Bogacz, A. and Berg, J. S. and Stratakis, D. and Witte, H. and Snopok, P. and Bliss, N. and Cordwell, M. and Moss, A. and Pattalwar, S. and Apollonio, M.},
  title     = {High intensity neutrino oscillation facilities in Europe},
  series = {Physical Review Special Topics-Accelerators and Beams},
  volume    = {16},
  journal   = {Physical Review Special Topics-Accelerators and Beams},
  number    = {2},
  doi       = {10.1103/PhysRevSTAB.16.021002},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-126611},
  pages     = {21002},
  year      = {2013},
  abstract  = {The EUROnu project has studied three possible options for future, high intensity neutrino oscillation facilities in Europe. The first is a Super Beam, in which the neutrinos come from the decay of pions created by bombarding targets with a 4 MW proton beam from the CERN High Power Superconducting Proton Linac. The far detector for this facility is the 500 kt MEMPHYS water Cherenkov, located in the Frejus tunnel. The second facility is the Neutrino Factory, in which the neutrinos come from the decay of mu(+) and mu(-) beams in a storage ring. The far detector in this case is a 100 kt magnetized iron neutrino detector at a baseline of 2000 km. The third option is a Beta Beam, in which the neutrinos come from the decay of beta emitting isotopes, in particular He-6 and Ne-18, also stored in a ring. The far detector is also the MEMPHYS detector in the Frejus tunnel. EUROnu has undertaken conceptual designs of these facilities and studied the performance of the detectors. Based on this, it has determined the physics reach of each facility, in particular for the measurement of CP violation in the lepton sector, and estimated the cost of construction. These have demonstrated that the best facility to build is the Neutrino Factory. However, if a powerful proton driver is constructed for another purpose or if the MEMPHYS detector is built for astroparticle physics, the Super Beam also becomes very attractive.},
  language  = {en}
}
@article{RudelPrustySiegletal.2013,
  author    = {Rudel, Thomas and Prusty, Bhupesh K. and Siegl, Christine and Hauck, Petra and Hain, Johannes and Korhonen, Suvi J. and Hiltunen-Back, Eija and Poulakkainen, Mirja},
  title     = {Chlamydia trachomatis Infection Induces Replication of Latent HHV-6},
  series = {PLoS ONE},
  journal   = {PLoS ONE},
  doi       = {10.1371/journal.pone.0061400},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-96731},
  year      = {2013},
  abstract  = {Human herpesvirus-6 (HHV-6) exists in latent form either as a nuclear episome or integrated into human chromosomes in more than 90\% of healthy individuals without causing clinical symptoms. Immunosuppression and stress conditions can reactivate HHV-6 replication, associated with clinical complications and even death. We have previously shown that co-infection of Chlamydia trachomatis and HHV-6 promotes chlamydial persistence and increases viral uptake in an in vitro cell culture model. Here we investigated C. trachomatis-induced HHV-6 activation in cell lines and fresh blood samples from patients having Chromosomally integrated HHV-6 (CiHHV-6). We observed activation of latent HHV-6 DNA replication in CiHHV-6 cell lines and fresh blood cells without formation of viral particles. Interestingly, we detected HHV-6 DNA in blood as well as cervical swabs from C. trachomatis-infected women. Low virus titers correlated with high C. trachomatis load and vice versa, demonstrating a potentially significant interaction of these pathogens in blood cells and in the cervix of infected patients. Our data suggest a thus far underestimated interference of HHV-6 and C. trachomatis with a likely impact on the disease outcome as consequence of co-infection.},
  language  = {en}
}
@article{BoschertFrischBacketal.2016,
  author    = {Boschert, V. and Frisch, C. and Back, J. W. and van Pee,, K. and Weidauer, S. E. and Muth, E.-M. and Schmieder, P. and Beerbaum, M. and Knappik, A. and Timmerman, P. and Mueller, T. D.},
  title     = {The sclerostin-neutralizing antibody AbD09097 recognizes an epitope adjacent to sclerostin's binding site for the Wnt co-receptor LRP6},
  series = {Open Biology},
  volume    = {6},
  journal   = {Open Biology},
  doi       = {10.1098/rsob.160120},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-177925},
  year      = {2016},
  abstract  = {The glycoprotein sclerostin has been identified as a negative regulator of bone growth. It exerts its function by interacting with the Wnt co-receptor LRP5/6, blocks the binding of Wnt factors and thereby inhibits Wnt signalling. Neutralizing anti-sclerostin antibodies are able to restore Wnt activity and enhance bone growth thereby presenting a new osteoanabolic therapy approach for diseases such as osteoporosis. We have generated various Fab antibodies against human and murine sclerostin using a phage display set-up. Biochemical analyses have identified one Fab developed against murine sclerostin, AbD09097 that efficiently neutralizes sclerostin's Wnt inhibitory activity. In vitro interaction analysis using sclerostin variants revealed that this neutralizing Fab binds to sclerostin's flexible second loop, which has been shown to harbour the LRP5/6 binding motif. Affinity maturation was then applied to AbD09097, providing a set of improved neutralizing Fab antibodies which particularly bind human sclerostin with enhanced affinity. Determining the crystal structure of AbD09097 provides first insights into how this antibody might recognize and neutralize sclerostin. Together with the structure-function relationship derived from affinity maturation these new data will foster the rational design of new and highly efficient anti-sclerostin antibodies for the therapy of bone loss diseases such as osteoporosis.},
  language  = {en}
}