% 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{Gulys:626511,
      author       = {Gulyás, Kinga Virág and Zhou, Liping and Salamonsen,
                      Daniel and Prester, Andreas and Bartels, Kim and Bosman,
                      Robert and Haffke, Paul and Li, Jintian and Tamási, Viola
                      and Deufel, Fritz and Thoma, Johannes and Andersson
                      Rasmussen, Anna and Csala, Miklós and Schroder Leiros,
                      Hanna-Kirsti and Xu, Zhijian and Widersten, Mikael and
                      Rohde, Holger and Schulz, Eike and Zhu, Weiliang and
                      Erdélyi, Máté},
      title        = {{D}ynamically chiral phosphonic acid-type
                      metallo-β-lactamase inhibitors},
      journal      = {Communications chemistry},
      volume       = {8},
      number       = {1},
      issn         = {2399-3669},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {PUBDB-2025-01464},
      pages        = {119},
      year         = {2025},
      abstract     = {Antibiotic resistance is a growing global health threat
                      that risks the lives of millions. Among the resistance
                      mechanisms, that mediated by metallo-β-lactamases is of
                      particular concern as these bacterial enzymes dismantle most
                      β-lactam antibiotics, which are our widest applied and
                      cheapest to produce antibiotic agents. So far, no clinically
                      applicable metallo-β-lactamase inhibitors are available.
                      Aiming to adapt to structural variations, we introduce the
                      inhibitor concept: dynamically chiral phosphonic acids. We
                      demonstrate that they are straightforward to synthesize,
                      penetrate bacterial membranes, inhibit the
                      metallo-β-lactamase enzymes NDM-1, VIM-2 and GIM-1, and are
                      non-toxic to human cells. Mimicking the transition state of
                      β-lactam hydrolysis, they target the Zn ions of the
                      metallo-β-lactamase active site. As a unique feature, both
                      of their stereoisomers bind metallo-β-lactamases, which
                      provides them unparalleled adaptability to the structural
                      diversity of these enzymes, and may allow them to hamper
                      bacteria’s ability for resistance development.},
      cin          = {EMBL-User},
      ddc          = {540},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3) / DFG project
                      G:(GEPRIS)458246365 - Zeitaufgelöste Strukturanalysde der
                      extended spectrum Beta-Lactamase CTX-M-14 (458246365)},
      pid          = {G:(DE-HGF)POF4-6G3 / G:(GEPRIS)458246365},
      experiment   = {EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40253435},
      UT           = {WOS:001471182500001},
      doi          = {10.1038/s42004-025-01510-5},
      url          = {https://bib-pubdb1.desy.de/record/626511},
}