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@ARTICLE{Lis:614237,
      author       = {Lis, Kinga and Plewka, Jacek and Menezes, Filipe and
                      Bielecka, Ewa and Chykunova, Yuliya and Pustelny, Katarzyna
                      and Niebling, Stephan and Garcia, Angelica Struve and
                      Garcia-Alai, Maria and Popowicz, Grzegorz M. and Czarna,
                      Anna and Kantyka, Tomasz and Pyrc, Krzysztof},
      title        = {{SARS}-{C}o{V}-2 {M}pro oligomerization as a potential
                      target for therapy},
      journal      = {International journal of biological macromolecules},
      volume       = {267},
      issn         = {0141-8130},
      address      = {New York, NY [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PUBDB-2024-05777},
      pages        = {131392},
      year         = {2024},
      abstract     = {The main protease (Mpro) of SARS-CoV-2 is critical in the
                      virus's replication cycle, facilitating the maturation of
                      polyproteins into functional units. Due to its conservation
                      across taxa, Mpro is a promising target for broad-spectrum
                      antiviral drugs. Targeting Mpro with small molecule
                      inhibitors, such as nirmatrelvir combined with ritonavir
                      (Paxlovid™), which the FDA has approved for post-exposure
                      treatment and prophylaxis, can effectively interrupt the
                      replication process of the virus. A key aspect of Mpro's
                      function is its ability to form a functional dimer. However,
                      the mechanics of dimerization and its influence on
                      proteolytic activity remain less understood. In this study,
                      we utilized biochemical, structural, and molecular modelling
                      approaches to explore Mpro dimerization. We evaluated
                      critical residues, specifically Arg4 and Arg298, that are
                      essential for dimerization. Our results show that changes in
                      the oligomerization state of Mpro directly affect its
                      enzymatic activity and dimerization propensity. We
                      discovered a synergistic relationship influencing dimer
                      formation, involving both intra- and intermolecular
                      interactions. These findings highlight the potential for
                      developing allosteric inhibitors targeting Mpro, offering
                      promising new directions for therapeutic strategies.},
      cin          = {CSSB-CF-SPC},
      ddc          = {570},
      cid          = {I:(DE-H253)CSSB-CF-SPC-20210520},
      pnm          = {899 - ohne Topic (POF4-899) / CARE - Corona Accelerated
                      $R\&D$ in Europe (101005077)},
      pid          = {G:(DE-HGF)POF4-899 / G:(EU-Grant)101005077},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:38582483},
      UT           = {WOS:001242446400001},
      doi          = {10.1016/j.ijbiomac.2024.131392},
      url          = {https://bib-pubdb1.desy.de/record/614237},
}