<?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%">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%">Chem. - A Eur. J.</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><pub-dates><date><style  face="normal" font="default" size="100%">jun</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://doi.wiley.com/10.1002/chem.201701591</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><pages><style face="normal" font="default" size="100%">8800–8805</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">© 2017 Wiley-VCH Verlag GmbH &amp;amp; Co. KGaA, Weinheim The design and synthesis of a glucose-based acridone derivative (GLAC), a potent inhibitor of glycogen phosphorylase (GP) are described. GLAC is the first inhibitor of glycogen phosphorylase, the electronic absorption properties of which are clearly distinguishable from those of the enzyme. This allows probing subtle interactions in the catalytic site. The GLAC absorption spectra, associated with X-ray crystallography and quantum chemistry cal culations, reveal that part of the catalytic site of GP behaves as a highly basic environment in which GLAC exists as a bis-anion. This is explained by water-bridged hydrogen-bonding interactions with specific catalytic site residues.</style></abstract></record></records></xml>