{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T14:58:39Z","timestamp":1790261919503,"version":"4.1.0"},"reference-count":52,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2020,12,1]],"date-time":"2020-12-01T00:00:00Z","timestamp":1606780800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,12,1]],"date-time":"2020-12-01T00:00:00Z","timestamp":1606780800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2021,9,13]],"date-time":"2021-09-13T00:00:00Z","timestamp":1631491200000},"content-version":"am","delay-in-days":286,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100001671","name":"European Synchrotron Radiation Facility","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001671","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001407","name":"Department of Biotechnology, Ministry of Science and Technology, India","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001407","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100012990","name":"Universit\u00e0 degli Studi di Siena","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100012990","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100007856","name":"Baylor College of Medicine","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100007856","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003407","name":"Ministero dell\u2019Istruzione, dell\u2019Universit\u00e0 e della Ricerca","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003407","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["BE1540\/15-2"],"award-info":[{"award-number":["BE1540\/15-2"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["SPP 1710"],"award-info":[{"award-number":["SPP 1710"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["European Journal of Medicinal Chemistry"],"published-print":{"date-parts":[[2020,12]]},"DOI":"10.1016\/j.ejmech.2020.112720","type":"journal-article","created":{"date-parts":[[2020,8,20]],"date-time":"2020-08-20T11:33:54Z","timestamp":1597923234000},"page":"112720","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":42,"special_numbering":"C","title":["4-Amino-1,2,4-triazole-3-thione-derived Schiff bases as metallo-\u03b2-lactamase inhibitors"],"prefix":"10.1016","volume":"208","author":[{"given":"Laurent","family":"Gavara","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laurent","family":"Sevaille","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Filomena","family":"De Luca","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paola","family":"Mercuri","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8706-9232","authenticated-orcid":false,"given":"Carine","family":"Bebrone","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Georges","family":"Feller","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alice","family":"Legru","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Giulia","family":"Cerboni","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Silvia","family":"Tanfoni","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Damien","family":"Baud","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7922-0289","authenticated-orcid":false,"given":"Giuliano","family":"Cutolo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Beno\u00eet","family":"Bestgen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Giulia","family":"Chelini","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Federica","family":"Verdirosa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Filomena","family":"Sannio","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2574-3911","authenticated-orcid":false,"given":"Cecilia","family":"Pozzi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0709-2537","authenticated-orcid":false,"given":"Manuela","family":"Benvenuti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karolina","family":"Kwapien","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marina","family":"Fischer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katja","family":"Becker","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Marie","family":"Fr\u00e8re","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefano","family":"Mangani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nohad","family":"Gresh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Doroth\u00e9e","family":"Berthomieu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Moreno","family":"Galleni","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9483-4476","authenticated-orcid":false,"given":"Jean-Denis","family":"Docquier","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Fran\u00e7ois","family":"Hernandez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ejmech.2020.112720_bib1","doi-asserted-by":"crossref","first-page":"1791","DOI":"10.3201\/eid1710.110655","article-title":"Global spread of carbapenemase-producing Enterobacteriaceae","volume":"17","author":"Nordmann","year":"2011","journal-title":"Emerg. Infect. Dis."},{"key":"10.1016\/j.ejmech.2020.112720_bib2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1093\/jac\/dkr378","article-title":"The emergence of pan-resistant Gram-negative pathogens merits a rapid global political response","volume":"67","author":"Walsh","year":"2012","journal-title":"J.\u00a0Antimicrob. Chemother."},{"key":"10.1016\/j.ejmech.2020.112720_bib3","doi-asserted-by":"crossref","first-page":"482","DOI":"10.3934\/microbiol.2018.3.482","article-title":"An overview of the antimicrobial resistance mechanisms of bacteria","volume":"4","author":"Reygaert","year":"2018","journal-title":"AIMS Microbiol."},{"key":"10.1016\/j.ejmech.2020.112720_bib4","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/S1473-3099(18)30605-4","article-title":"Burden of AMR Collaborative Group. Attributable deaths and disability-adjusted life-years caused by infections with antibiotic-resistant bacteria in the EU and the European Economic Area in 2015: a population-level modelling analysis","volume":"19","author":"Cassini","year":"2019","journal-title":"Lancet Infect. Dis."},{"key":"10.1016\/j.ejmech.2020.112720_bib5","doi-asserted-by":"crossref","DOI":"10.1128\/AAC.01076-18","article-title":"Past and present perspectives on \u03b2-lactamases","volume":"62","author":"Bush","year":"2018","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.ejmech.2020.112720_bib6","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1111\/j.1749-6632.2012.06796.x","article-title":"Metallo-\u03b2-lactamase structure and function","volume":"1277","author":"Palzkill","year":"2013","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"10.1016\/j.ejmech.2020.112720_bib7","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1016\/j.jgar.2018.05.004","article-title":"Escherichia coli encoding blaNDM-5 associated with community-acquired urinary tract infections with unusual MIC creep-like phenomenon against imipenem","volume":"14","author":"Gajamer","year":"2018","journal-title":"J.\u00a0Glob. Antimicrob. Resist."},{"key":"10.1016\/j.ejmech.2020.112720_bib8","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.drup.2017.11.002","article-title":"An update on \u03b2-lactamase inhibitor discovery and development","volume":"36","author":"Docquier","year":"2018","journal-title":"Drug Resist. Updates"},{"key":"10.1016\/j.ejmech.2020.112720_bib9","unstructured":"C. J. Burns, D. Daigle, B. Liu, D. McGarry, D. C. Pevear, R. E. Trout, \u03b2-Lactamase inhibitors. WO Patent WO 2014\/089365 A1."},{"key":"10.1016\/j.ejmech.2020.112720_bib10","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.cbpa.2019.03.001","article-title":"Will morphing boron-based inhibitors beat the \u03b2-lactamases?","volume":"50","author":"Krajnc","year":"2019","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.ejmech.2020.112720_bib11","doi-asserted-by":"crossref","first-page":"8544","DOI":"10.1021\/acs.jmedchem.9b00911","article-title":"Bicyclic boronate VNRX-5133 inhibits metallo- and serine \u03b2-lactamases","volume":"62","author":"Krajnc","year":"2019","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112720_bib12","doi-asserted-by":"crossref","DOI":"10.1128\/AAC.01963-19","article-title":"VNRX-5133 (Taniborbactam), a broad-spectrum inhibitor of serine- and metallo-\u03b2-lactamase, restores activity of cefepime in Enterobacterales and Pseudomonas aeruginosa","volume":"64","author":"Hamrick","year":"2020","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.ejmech.2020.112720_bib13","doi-asserted-by":"crossref","first-page":"2789","DOI":"10.1021\/acs.jmedchem.9b01518","article-title":"Discovery of Taniborbactam (VNRX-5133): a broad spectrum serine- and metallo-\u03b2-lactamase inhibitor for carbapenem-resistant bacterial infections","volume":"63","author":"Liu","year":"2020","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112720_bib14","doi-asserted-by":"crossref","DOI":"10.1128\/AAC.00074-18","article-title":"Discovery of a novel metallo-\u03b2-lactamase inhibitor that potentiates meropenem activity against carbapenem-resistant Enterobacteriaceae","volume":"62","author":"Everett","year":"2018","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.ejmech.2020.112720_bib15","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1021\/acsinfecdis.8b00246","article-title":"SAR studies leading to the identification of a novel series of metallo-\u03b2-lactamase inhibitors for the treatment of carbapenem-resistant Enterobacteriaceae infections that display efficacy in an animal infection model","volume":"5","author":"Leiris","year":"2019","journal-title":"ACS Infect. Dis."},{"key":"10.1016\/j.ejmech.2020.112720_bib16","doi-asserted-by":"crossref","first-page":"673","DOI":"10.4155\/fmc-2017-0007","article-title":"Progress toward inhibitors of metallo-\u03b2-lactamases","volume":"9","author":"McGeary","year":"2017","journal-title":"Future Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112720_bib17","doi-asserted-by":"crossref","first-page":"2282","DOI":"10.1039\/b802311e","article-title":"Structural basis for the broad-spectrum inhibition of metallo-\u03b2-lactamases by thiols","volume":"6","author":"Li\u00e9nard","year":"2008","journal-title":"Org. Biomol. Chem."},{"key":"10.1016\/j.ejmech.2020.112720_bib18","doi-asserted-by":"crossref","first-page":"4862","DOI":"10.1021\/jm100213c","article-title":"Mercaptophosphonate compounds as broad-spectrum inhibitors of the metallo-\u03b2-lactamases","volume":"53","author":"Lassaux","year":"2010","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112720_bib19","doi-asserted-by":"crossref","first-page":"31913","DOI":"10.1074\/jbc.M104742200","article-title":"Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-\u03b2-lactamase","volume":"276","author":"Toney","year":"2001","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.ejmech.2020.112720_bib20","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1038\/nature13445","article-title":"Aspergillomarasmine A overcomes metallo-\u03b2-lactamase antibiotic resistance","volume":"510","author":"King","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.ejmech.2020.112720_bib21","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1021\/acsinfecdis.7b00106","article-title":"Probing the interaction of aspergillomarasmine A with metallo-\u03b2-lactamase NDM-1, VIM-2, and IMP-7","volume":"4","author":"Bergstrom","year":"2018","journal-title":"ACS Infect. Dis."},{"key":"10.1016\/j.ejmech.2020.112720_bib22","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1254\/jjp.63.187","article-title":"Pharmacological profiles of aspergillomarasmines as endothelin converting enzyme inhibitors","volume":"63","author":"Matsuura","year":"1993","journal-title":"Jpn. J. Pharmacol."},{"key":"10.1016\/j.ejmech.2020.112720_bib23","doi-asserted-by":"crossref","DOI":"10.1128\/AAC.02415-19","article-title":"ZN148 \u2013 a modular synthetic metallo-\u03b2-lactamase inhibitor reverses carbapenem-resistance in Gram-negative pathogens in\u00a0vivo","author":"Samuelsen","year":"2020","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.ejmech.2020.112720_bib24","doi-asserted-by":"crossref","first-page":"12406","DOI":"10.1038\/ncomms12406","article-title":"Structural basis of metallo-\u03b2-lactamase, serine-\u03b2-lactamase and penicillin-binding protein inhibition by cyclic boronates","volume":"7","author":"Brem","year":"2016","journal-title":"Nat. Commun."},{"key":"10.1016\/j.ejmech.2020.112720_bib25","doi-asserted-by":"crossref","DOI":"10.1021\/acs.jmedchem.9b01976","article-title":"Discovery of cyclic boronic acid QPX7728, an ultra-broad-spectrum inhibitor of serine and metallo-\u03b2-lactamases","author":"Hecker","year":"2020","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112720_bib26","doi-asserted-by":"crossref","first-page":"2627","DOI":"10.1016\/j.bmc.2005.11.046","article-title":"New leads of metallo-\u03b2-lactamase inhibitors from structure-based pharmacophore design","volume":"14","author":"Olsen","year":"2006","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112720_bib27","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/j.jmb.2007.10.036","article-title":"Structural insights into the design of inhibitors of the L1 metallo-\u03b2-lactamase from Stenotrophomonas maltophilia","volume":"375","author":"Nauton","year":"2008","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.ejmech.2020.112720_bib28","doi-asserted-by":"crossref","first-page":"972","DOI":"10.1002\/cmdc.201700186","article-title":"1,2,4-Triazole-3-thione compounds as inhibitors of dizinc metallo-\u03b2-lactamase","volume":"12","author":"Sevaille","year":"2017","journal-title":"ChemMedChem"},{"key":"10.1016\/j.ejmech.2020.112720_bib29","doi-asserted-by":"crossref","first-page":"6295","DOI":"10.1021\/acs.jpcb.7b01053","article-title":"Calibration of 1,2,4-triazole-3-thione, an original Zn-binding group of metallo-\u03b2-lactamase inhibitors. Validation of a polarizable MM\/MD potential by quantum chemistry","volume":"121","author":"Kwapien","year":"2017","journal-title":"J.\u00a0Phys. Chem. B"},{"key":"10.1016\/j.ejmech.2020.112720_bib30","doi-asserted-by":"crossref","first-page":"3282","DOI":"10.1016\/j.bmcl.2011.04.027","article-title":"The identification of new metallo-\u03b2-lactamase inhibitor leads from fragment-based screening","volume":"21","author":"Vella","year":"2011","journal-title":"Bioorg. Med. Chem. Lett"},{"key":"10.1016\/j.ejmech.2020.112720_bib31","doi-asserted-by":"crossref","first-page":"8671","DOI":"10.1021\/acs.jmedchem.5b01289","article-title":"Discovery of novel inhibitor scaffolds against the metallo-\u03b2-lactamase VIM-2 by surface plasmon resonance (SPR) based fragment screening","volume":"58","author":"Christopeit","year":"2015","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112720_bib32","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1021\/acsmedchemlett.7b00428","article-title":"Structure-based virtual screening for the discovery of novel inhibitors of New Delhi Metallo-\u03b2-lactamase-1","volume":"9","author":"Spyrakis","year":"2018","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2020.112720_bib33","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1016\/j.drudis.2008.07.005","article-title":"Do enthalpy and entropy distinguish first class from best in class?","volume":"13","author":"Freire","year":"2008","journal-title":"Drug Discov. Today"},{"key":"10.1016\/j.ejmech.2020.112720_bib34","doi-asserted-by":"crossref","first-page":"888","DOI":"10.1042\/BST0380888","article-title":"Calorimetry as a tool for understanding biomolecular interactions and an aid to drug design","volume":"38","author":"Ladbury","year":"2010","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.ejmech.2020.112720_bib35","doi-asserted-by":"crossref","first-page":"3197","DOI":"10.1128\/AAC.01336-09","article-title":"Mutational analysis of VIM-2 reveals an essential determinant for metallo-\u03b2-lactamase stability and folding","volume":"54","author":"Borgianni","year":"2010","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.ejmech.2020.112720_bib36","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1021\/acsmedchemlett.9b00674","article-title":"Screen of unfocused libraries identifies compounds with direct or synergistic antibacterial activity","volume":"11","author":"Mugnaini","year":"2020","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2020.112720_bib37","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/j.pep.2005.01.016","article-title":"Protein production by auto-induction in high density shaking cultures","volume":"41","author":"Studier","year":"2005","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.ejmech.2020.112720_bib38","doi-asserted-by":"crossref","first-page":"902","DOI":"10.1128\/AAC.43.4.902","article-title":"Biochemical characterization of the Pseudomonas aeruginosa 101\/1477 metallo-\u03b2-lactamase IMP-1 produced by Escherichia coli","volume":"43","author":"Laraki","year":"1999","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.ejmech.2020.112720_bib39","doi-asserted-by":"crossref","first-page":"1823","DOI":"10.1128\/AAC.46.6.1823-1830.2002","article-title":"CAU-1, a subclass B3 metallo-\u03b2-lactamase of low substrate affinity encoded by an ortholog present in the Caulobacter crescentus chromosome","volume":"46","author":"Docquier","year":"2002","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.ejmech.2020.112720_bib40","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1093\/jac\/dkg067","article-title":"On functional and structural heterogeneity of VIM-type metallo-\u03b2-lactamases","volume":"51","author":"Docquier","year":"2003","journal-title":"J.\u00a0Antimicrob. Chemother."},{"key":"10.1016\/j.ejmech.2020.112720_bib41","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1089\/mdr.1996.2.253","article-title":"Overproduction and purification of the Aeromonas hydrophila CphA metallo-\u03b2-lactamse expressed in Escherichia coli","volume":"2","author":"Hernandez-Villadares","year":"1996","journal-title":"Microb. Drug Resist."},{"key":"10.1016\/j.ejmech.2020.112720_bib42","doi-asserted-by":"crossref","first-page":"28195","DOI":"10.1074\/jbc.M414052200","article-title":"Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-\u03b2-lactamase by site-directed mutagenesis","volume":"280","author":"Bebrone","year":"2005","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.ejmech.2020.112720_bib43","series-title":"Performance Standards for Antimicrobial Disk Susceptibility Tests; Approved Standard, Document M02-A12","author":"Clinical Laboratory Standard Institute","year":"2015"},{"key":"10.1016\/j.ejmech.2020.112720_bib44","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1093\/jac\/dkg126","article-title":"Relative contributions of the AcrAB, MdfA and NorE efflux pumps to quinolone resistance in Escherichia coli","volume":"51","author":"Yang","year":"2003","journal-title":"J.\u00a0Antimicrob. Chemother."},{"key":"10.1016\/j.ejmech.2020.112720_bib45","series-title":"Methods for Dilution Antimicrobial Susceptibility Tests for Bacteria that Grow Aerobically, Document M07-A10","author":"Clinical Laboratory Standard Institute","year":"2015"},{"key":"10.1016\/j.ejmech.2020.112720_bib46","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1515\/BC.2005.006","article-title":"Characterization of the glyoxalases of the malarial parasite Plasmodium falciparum and comparison with their human counterparts","volume":"386","author":"Akoachere","year":"2005","journal-title":"Biol. Chem."},{"key":"10.1016\/j.ejmech.2020.112720_bib47","doi-asserted-by":"crossref","first-page":"4343","DOI":"10.1128\/AAC.00409-10","article-title":"High-resolution crystal structure of the subclass B3 metallo-\u03b2-lactamase BJP-1: rational basis for substrate specificity and interaction with sulfonamides","volume":"54","author":"Docquier","year":"2010","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.ejmech.2020.112720_bib48","doi-asserted-by":"crossref","first-page":"1437","DOI":"10.1002\/cmdc.201800213","article-title":"Atomic-resolution structure of a class C \u03b2-lactamase and its complex with avibactam","volume":"13","author":"Pozzi","year":"2018","journal-title":"ChemMedChem"},{"issue":"Pt4","key":"10.1016\/j.ejmech.2020.112720_bib49","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1107\/S0907444911001314","article-title":"REFMAC5 for the refinement of macromolecular crystal structures","volume":"67","author":"Murshudov","year":"2011","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"issue":"Pt4","key":"10.1016\/j.ejmech.2020.112720_bib50","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1107\/S0907444910045749","article-title":"Overview of the CCP4 suite and current developments","volume":"67","author":"Wynn","year":"2011","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"issue":"Pt4","key":"10.1016\/j.ejmech.2020.112720_bib51","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.ejmech.2020.112720_bib52","doi-asserted-by":"crossref","first-page":"1171","DOI":"10.1038\/nprot.2008.91","article-title":"Automated macromolecular model building for X-ray crystallography using ARP\/wARP version 7","volume":"3","author":"Langer","year":"2008","journal-title":"Nat. Protoc."}],"container-title":["European Journal of Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523420306929?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523420306929?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T06:00:06Z","timestamp":1777528806000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0223523420306929"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,12]]},"references-count":52,"alternative-id":["S0223523420306929"],"URL":"https:\/\/doi.org\/10.1016\/j.ejmech.2020.112720","relation":{},"ISSN":["0223-5234"],"issn-type":[{"value":"0223-5234","type":"print"}],"subject":[],"published":{"date-parts":[[2020,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"4-Amino-1,2,4-triazole-3-thione-derived Schiff bases as metallo-\u03b2-lactamase inhibitors","name":"articletitle","label":"Article Title"},{"value":"European Journal of Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ejmech.2020.112720","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier Masson SAS. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"112720"}}