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@ARTICLE{Guenther:437962,
      author       = {Guenther, Sebastian and Reinke, Patrick and Oberthuer,
                      Dominik and Yefanov, Oleksandr and Ginn, Helen and Meier,
                      Susanne and Lane, Thomas and Lorenzen, Kristina and Gelisio,
                      Luca and Brehm, Wolfgang and Dunkel, Ilona and Domaracky,
                      Martin and Saouane, Sofiane and Lieske, Julia and Ehrt,
                      Christiane and Koua, Faisal and Tolstikova, Alexandra and
                      White, Thomas and Groessler, Michael and Fleckenstein,
                      Holger and Trost, Fabian and Galchenkova, Marina and
                      Gevorkov, Yaroslav and Li, Chufeng and Awel, Salah and Peck,
                      Ariana and Xavier, P. Lourdu and Barthelmess, Miriam and
                      Schlünzen, Frank and Werner, Nadine and Andaleeb, Hina and
                      Ullah, Najeeb and Falke, Sven and Franca, Bruno Alves and
                      Schwinzer, Martin and Brognaro, Hevila and Seychell, Brandon
                      and Gieseler, Henry and Melo, Diogo and Zaitsev-Doyle, Jo J.
                      and Norton-Baker, Brenna and Knoska, Juraj and Pena Murillo,
                      Gisel Esperanza and Mashhour, Aida Rahmani and Guicking,
                      Filip and Hennicke, Vincent and Fischer, Pontus and Rogers,
                      Cromarte and Monteiro, Diana C. F. and Hakanpää, Johanna
                      and Meyer, Jan and Noei, Heshmat and Gribbon, Phil and
                      Ellinger, Bernhard and Kuzikov, Maria and Wolf, Markus and
                      Zhang, Linlin and Sun, Xinyuanyuan and Pletzer-Zelgert,
                      Jonathan and Wollenhaupt, Jan and Feiler, Christian and
                      Weiss, Manfred and Schulz, Eike-Christian and Mehrabi,
                      Pedram and Schmidt, Christina and Schubert, Robin and Han,
                      Huijong and Krichel, Boris and Fernández-García, Yaiza and
                      Escudero-Pérez, Beatriz and Günther, Stephan and Turk,
                      Dusan and Uetrecht, Charlotte and Beck, Tobias and Tidow,
                      Henning and Chari, Aschwin and Zaliani, Andrea and Rarey,
                      Matthias and Cox, Russel and Hilgenfeld, Rolf and Chapman,
                      Henry N and Pearson, Arwen R. and Betzel, Christian and
                      Meents, Alke},
      title        = {{C}atalytic cleavage of {HEAT} and subsequent covalent
                      binding of the tetralone moiety by the {SARS}-{C}o{V}-2 main
                      protease},
      publisher    = {Zenodo},
      reportid     = {PUBDB-2020-01727},
      year         = {2020},
      note         = {PrePrint:
                      https://www.biorxiv.org/content/10.1101/2020.05.02.043554},
      abstract     = {Here we present the crystal structure of SARS-CoV-2 main
                      protease (Mpro) covalently bound to 2-methyl-1-tetralone.
                      This complex was obtained by co-crystallization of Mpro with
                      HEAT
                      (2-(((4-hydroxyphenethyl)amino)methyl)-3,4-dihydronaphthalen-1(2H)-one)
                      in the framework of a large X-ray crystallographic screening
                      project of Mpro against a drug repurposing library,
                      consisting of 5632 approved drugs or compounds in clinical
                      phase trials. Further investigations showed that HEAT is
                      cleaved by Mpro in an E1cB-like reaction mechanism into
                      2-methylene-1-tetralone and tyramine. The catalytic Cys145
                      subsequently binds covalently in a Michael addition to the
                      methylene carbon atom of 2-methylene-1-tetralone. According
                      to this postulated model HEAT is acting in a pro-drug-like
                      fashion. It is metabolized by Mpro, followed by covalent
                      binding of one metabolite to the active site. The structure
                      of the covalent adduct elucidated in this study opens up a
                      new path for developing non-peptidic inhibitors.},
      cin          = {FS-CFEL-1 / CFEL-I / CFEL-TRSB / FS-PET-D / IT / CFEL-ARD /
                      FS-NL / EMBL / UNI/CUI / UNI/PHY},
      cid          = {I:(DE-H253)FS-CFEL-1-20120731 / I:(DE-H253)CFEL-I-20161114
                      / I:(DE-H253)CFEL-TRSB-20161025 /
                      I:(DE-H253)FS-PET-D-20190712 / I:(DE-H253)IT-20120731 /
                      I:(DE-H253)CFEL-ARD-20160914 / I:(DE-H253)FS-NL-20120731 /
                      I:(DE-H253)EMBL-20120731 / $I:(DE-H253)UNI_CUI-20121230$ /
                      $I:(DE-H253)UNI_PHY-20170505$},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621) /
                      HIDSS-0002 - DASHH: Data Science in Hamburg - Helmholtz
                      Graduate School for the Structure of Matter
                      $(2019_IVF-HIDSS-0002)$},
      pid          = {G:(DE-HGF)POF3-6215 / $G:(DE-HGF)2019_IVF-HIDSS-0002$},
      experiment   = {EXP:(DE-H253)P-P11-20150101 /
                      EXP:(DE-H253)CFEL-Exp-20150101},
      typ          = {PUB:(DE-HGF)25},
      doi          = {10.1101/2020.05.02.043554},
      url          = {https://bib-pubdb1.desy.de/record/437962},
}