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@ARTICLE{Chatziefthymiou:602646,
      author       = {Chatziefthymiou, S. and Kuzikov, M. and Afandi, S. and
                      Crosas, E. and Pompidor, G. and Taberman, H. and
                      Windschügel, B. and Labahn, Joerg and Kolbe, M. and
                      Hakanpää, J.},
      title        = {{I}nhibitor screening and structural characterization of
                      virulence factors from {SARS}-{C}o{V}-2},
      journal      = {Acta crystallographica / Section A},
      volume       = {78},
      number       = {a2},
      issn         = {0108-7673},
      address      = {Oxford [u.a.]},
      publisher    = {Blackwell},
      reportid     = {PUBDB-2024-00707},
      pages        = {e333},
      year         = {2022},
      abstract     = {Coronavirus induced zoonotic diseases can cause pandemics
                      with unforeseeable consequences to human health and global
                      economy. Our project aims to screen and develop effective
                      therapeutics against SARS-CoV-2, targeting its
                      replication-transcription complex (RTC). Following an
                      interdisciplinary research approach, compound libraries of
                      approved drugs are used for the discovery of potent
                      inhibitors for proteins of the RTC and the binding mode of
                      these enzymeinhibitor complexes is studied by X-ray
                      crystallography. Our workflow includes the production of
                      proteins involved in the coronavirus RTC, the
                      high-throughput inhibitor screening with fluorescence-based
                      assays using drug repurposing libraries and the
                      structure/function analysis of the identified
                      enzyme-inhibitor complexes. The advantages of this approach
                      is that it is cost efficient, high-throughput, allows the
                      direct identification of potent inhibitors and ensures
                      optimal beamtime usage. Furthermore, such a platform can be
                      successfully used in future viral outbreaks. In this
                      presentation we will give an overview of this project and
                      the results achieved to date. We will focus on one of the
                      target proteins, namely the uridine-specific
                      endoribonuclease nsp15, and apart from the results from its
                      inhibitor screening we will also present findings that
                      allowed us to shed light on important activity determinants
                      of this enzyme.},
      cin          = {FS-PETRA-D / ITT / DOOR ; HAS-User / CSSB-HZI-MK},
      ddc          = {530},
      cid          = {I:(DE-H253)FS-PETRA-D-20210408 / I:(DE-H253)ITT-20160816 /
                      I:(DE-H253)HAS-User-20120731 /
                      I:(DE-H253)CSSB-HZI-MK-20210520},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633) / 6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-633 / G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P11-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:001048207700273},
      doi          = {10.1107/S2053273322093986},
      url          = {https://bib-pubdb1.desy.de/record/602646},
}