% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Mamais:397870,
      author       = {Mamais, Michael and DegliEsposti, Alessandra and
                      Kouloumoundra, Virginia and Gustavsson, Thomas and Monti,
                      Filippo and Venturini, Alessandro and Chrysina, Evangelia D.
                      and Markovitsi, Dimitra and Gimisis, Thanasis},
      title        = {{A} {N}ew {P}otent {I}nhibitor of {G}lycogen
                      {P}hosphorylase {R}eveals the {B}asicity of the {C}atalytic
                      {S}ite},
      journal      = {Chemistry - a European journal},
      volume       = {23},
      number       = {37},
      issn         = {0947-6539},
      address      = {Weinheim},
      publisher    = {Wiley-VCH},
      reportid     = {PUBDB-2017-13502},
      pages        = {8800 - 8805},
      year         = {2017},
      note         = {© Wiley-VCH Verlag GmbH $\&$ Co. KGaA, Weinheim ; Post
                      referee fulltext in progress; Embargo 12 months from
                      publication},
      abstract     = {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 calculations, 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.},
      cin          = {EMBL-User},
      ddc          = {540},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (POF3-622) / BIOSTRUCT-X - Transnational
                      access and enhancement of integrated Biological Structure
                      determination at synchrotron X-ray radiation facilities
                      (283570) / LASERLAB-EUROPE - The Integrated Initiative of
                      European Laser Research Infrastructures III (284464)},
      pid          = {G:(DE-HGF)POF3-6G3 / G:(EU-Grant)283570 /
                      G:(EU-Grant)284464},
      experiment   = {EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:28493496},
      UT           = {WOS:000404550000003},
      doi          = {10.1002/chem.201701591},
      url          = {https://bib-pubdb1.desy.de/record/397870},
}