<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Mamais, Michael</style></author><author><style face="normal" font="default" size="100%">Degli Esposti, Alessandra</style></author><author><style face="normal" font="default" size="100%">Kouloumoundra, Virginia</style></author><author><style face="normal" font="default" size="100%">Gustavsson, Thomas</style></author><author><style face="normal" font="default" size="100%">Monti, Filippo</style></author><author><style face="normal" font="default" size="100%">Venturini, Alessandro</style></author><author><style face="normal" font="default" size="100%">Chrysina, Evangelia D.</style></author><author><style face="normal" font="default" size="100%">Markovitsi, Dimitra</style></author><author><style face="normal" font="default" size="100%">Gimisis, Thanasis</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Frontispiece: A New Potent Inhibitor of Glycogen Phosphorylase Reveals the Basicity of the Catalytic Site</style></title><secondary-title><style face="normal" font="default" size="100%">Chemistry – A European Journal</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">acridone based inhibitors</style></keyword><keyword><style  face="normal" font="default" size="100%">glycogen phosphorylase</style></keyword><keyword><style  face="normal" font="default" size="100%">optical spectra</style></keyword><keyword><style  face="normal" font="default" size="100%">quantum chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">X-ray crystallography</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2017</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://onlinelibrary.wiley.com/doi/abs/10.1002/chem.201783763</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">37</style></number><volume><style face="normal" font="default" size="100%">23</style></volume><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Glycogen phosphorylase (GP) plays a key role in glucose regulation. The design and synthesis of a new potent inhibitor of GP is described. By exploiting its optical properties, it is shown that, due to an extended hydrogen bonding network, the local pH in the GP catalytic site is higher than 12. For the full story, see the Communication by A. Venturini, E. D. Chrysina, D. Markovitsi, T. Gimisis et al. on page 8800 ff.</style></abstract></record></records></xml>