{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,25]],"date-time":"2026-08-25T16:52:50Z","timestamp":1787676770096,"version":"build-2784847793"},"reference-count":113,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100022012","name":"CSIR-Institute of Microbial Technology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100022012","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":[[2026,1]]},"DOI":"10.1016\/j.ejmech.2025.118220","type":"journal-article","created":{"date-parts":[[2025,9,30]],"date-time":"2025-09-30T04:20:47Z","timestamp":1759206047000},"page":"118220","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":4,"special_numbering":"C","title":["Disarming superbugs: New frontiers in inhibiting NDM-1 and other clinically relevant metallo-\u03b2-lactamases"],"prefix":"10.1016","volume":"301","author":[{"given":"Pulkit","family":"Dhiman","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amit","family":"Patwa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arya B.","family":"Narayanan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aayushi","family":"Saini","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ankita","family":"Pundir","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Manoj D.","family":"Dhole","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1785-9287","authenticated-orcid":false,"given":"Vinod D.","family":"Chaudhari","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ejmech.2025.118220_bib1","article-title":"Tackling a crisis for the health and wealth of nations","author":"O'Neill","year":"2024","journal-title":"Afr. J. Lab. Med."},{"issue":"Figure 1","key":"10.1016\/j.ejmech.2025.118220_bib2","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.mib.2019.10.008","article-title":"Antibiotics: past, present and future","volume":"51","author":"Hutchings","year":"2019","journal-title":"Curr. Opin. Microbiol."},{"key":"10.1016\/j.ejmech.2025.118220_bib3","article-title":"Bush and bradford - 2016 - \u03b2-lactams and \u03b2-lactamase inhibitors an Overview.Pdf","volume":"22","author":"Bush","year":"2016","journal-title":"Cold Spring Harb. Perspect. Med."},{"issue":"5","key":"10.1016\/j.ejmech.2025.118220_bib4","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1038\/s41579-022-00820-y","article-title":"Molecular mechanisms of antibiotic resistance revisited","volume":"21","author":"Darby","year":"2023","journal-title":"Nat. Rev. Microbiol."},{"issue":"2","key":"10.1016\/j.ejmech.2025.118220_bib5","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1016\/j.mayocp.2011.12.003","article-title":"Mechanisms of resistance and clinical relevance of resistance to \u03b2-lactams, glycopeptides, and fluoroquinolones","volume":"87","author":"Rice","year":"2012","journal-title":"Mayo Clin. Proc."},{"issue":"March","key":"10.1016\/j.ejmech.2025.118220_bib6","article-title":"Metallo-\u03b2-Lactamase inhibitors: a continuing challenge for combating antibiotic resistance","volume":"309","author":"Kang","year":"2024","journal-title":"Biophys. Chem."},{"issue":"6","key":"10.1016\/j.ejmech.2025.118220_bib7","doi-asserted-by":"crossref","DOI":"10.3390\/biom10060854","article-title":"Metallo\u2010\u03b2\u2010lactamase inhibitors inspired on snapshots from the catalytic mechanism","volume":"10","author":"Palacios","year":"2020","journal-title":"Biomolecules"},{"issue":"5","key":"10.1016\/j.ejmech.2025.118220_bib8","doi-asserted-by":"crossref","first-page":"1558","DOI":"10.1002\/med.21665","article-title":"Principles and current strategies targeting metallo-\u03b2-lactamase mediated antibacterial resistance","volume":"40","author":"Yan","year":"2020","journal-title":"Med. Res. Rev."},{"issue":"31","key":"10.1016\/j.ejmech.2025.118220_bib9","doi-asserted-by":"crossref","first-page":"10013","DOI":"10.1021\/bi990356r","article-title":"On the mechanism of the metallo-\u03b2-lactamase from Bacteroides fragilis","volume":"38","author":"Wang","year":"1999","journal-title":"Biochemistry"},{"issue":"3","key":"10.1016\/j.ejmech.2025.118220_bib10","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1042\/bj3310703","article-title":"The mechanism of catalysis and the inhibition of the Bacillus cereus zinc-dependent \u03b2-lactamase","volume":"331","author":"Bounaga","year":"1998","journal-title":"Biochem. J."},{"issue":"12","key":"10.1016\/j.ejmech.2025.118220_bib11","doi-asserted-by":"crossref","first-page":"1686","DOI":"10.1016\/j.bcp.2007.05.021","article-title":"Metallo-\u03b2-Lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily","volume":"74","author":"Bebrone","year":"2007","journal-title":"Biochem. Pharmacol."},{"issue":"12","key":"10.1016\/j.ejmech.2025.118220_bib12","doi-asserted-by":"crossref","first-page":"5952","DOI":"10.1128\/AAC.05108-11","article-title":"A novel variant, NDM-5, of the New Delhi metallo-\u03b2-lactamase in a multidrug-resistant Escherichia coli ST648 isolate recovered from a patient in the United Kingdom","volume":"55","author":"Hornsey","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.ejmech.2025.118220_bib13","doi-asserted-by":"crossref","DOI":"10.1186\/s44280-024-00050-2","article-title":"Transmission patterns of multiple strains producing New Delhi metallo-\u03b2-lactamase variants among animals and the environment in live poultry markets","author":"Yin","year":"2024","journal-title":"One Heal. Adv"},{"key":"10.1016\/j.ejmech.2025.118220_bib14","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2021.113747","article-title":"Efforts towards the inhibitor design for New Delhi metallo-beta-lactamase (NDM-1)","volume":"225","author":"Nagulapalli Venkata","year":"2021","journal-title":"Eur. J. Med. Chem."},{"issue":"8","key":"10.1016\/j.ejmech.2025.118220_bib15","doi-asserted-by":"crossref","first-page":"2574","DOI":"10.1096\/fj.11-184036","article-title":"Crystal structure of NDM-1 reveals a common \u03b2-lactam hydrolysis mechanism","volume":"25","author":"Zhang","year":"2011","journal-title":"FASEB J."},{"issue":"9","key":"10.1016\/j.ejmech.2025.118220_bib16","doi-asserted-by":"crossref","first-page":"1484","DOI":"10.1002\/pro.697","article-title":"Crystal structure of New Delhi metallo-\u03b2-lactamase reveals molecular basis for antibiotic resistance","volume":"20","author":"King","year":"2011","journal-title":"Protein Sci."},{"issue":"9","key":"10.1016\/j.ejmech.2025.118220_bib17","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1371\/journal.pone.0024621","article-title":"Structure of apo- and monometalated forms of NDM-1-A highly potent carbapenem-hydrolyzing metallo-\u03b2-lactamase","volume":"6","author":"Kim","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.ejmech.2025.118220_bib18","first-page":"993","article-title":"New Delhi metallo-\u03b2-lactamase-1: structure, inhibitors and detection of producer","author":"Paul","year":"2016","journal-title":"Future Med. Chem."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118220_bib19","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1021\/acsinfecdis.8b00247","article-title":"Ten years with New Delhi metallo-\u03b2-lactamase-1 (NDM-1): from structural insights to inhibitor design","volume":"5","author":"Linciano","year":"2019","journal-title":"ACS Infect. Dis."},{"key":"10.1016\/j.ejmech.2025.118220_bib20","doi-asserted-by":"crossref","first-page":"1029","DOI":"10.2174\/1389450116666151001105622","article-title":"B1-Metallo- -lactamases : where do we stand","volume":"17","author":"Mojica","year":"2016","journal-title":"Curr. Drug Targets"},{"issue":"10","key":"10.1016\/j.ejmech.2025.118220_bib21","doi-asserted-by":"crossref","first-page":"1160","DOI":"10.1107\/S1744309111029654","article-title":"Structure of New Delhi metallo-\u03b2-lactamase 1 (NDM-1)","volume":"67","author":"Green","year":"2011","journal-title":"Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun."},{"issue":"18","key":"10.1016\/j.ejmech.2025.118220_bib22","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. Med. Chem."},{"issue":"6","key":"10.1016\/j.ejmech.2025.118220_bib23","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1128\/AAC.00212-20","article-title":"Spectrum of beta-lactamase inhibition by the cyclic boronate QPX7728, an ultrabroad-spectrum beta-lactamase inhibitor of serine and metallo-beta-lactamases: enhancement of activity of multiple antibiotics against isogenic strains expressing single beta-La","volume":"64","author":"Lomovskaya","year":"2020","journal-title":"Antimicrob. Agents Chemother."},{"issue":"6","key":"10.1016\/j.ejmech.2025.118220_bib24","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. Med. Chem."},{"issue":"2","key":"10.1016\/j.ejmech.2025.118220_bib25","doi-asserted-by":"crossref","DOI":"10.1128\/aac.02168-21","article-title":"The ultrabroad-spectrum beta-lactamase inhibitor QPX7728 restores the potency of multiple oral beta-lactam antibiotics against beta-lactamase-producing strains of resistant Enterobacterales","volume":"66","author":"Lomovskaya","year":"2022","journal-title":"Antimicrob. Agents Chemother."},{"issue":"23","key":"10.1016\/j.ejmech.2025.118220_bib26","doi-asserted-by":"crossref","first-page":"17523","DOI":"10.1021\/acs.jmedchem.1c01722","article-title":"Selection of QPX7831, an orally bioavailable prodrug of boronic acid \u03b2-lactamase inhibitor QPX7728","volume":"64","author":"Reddy","year":"2021","journal-title":"J. Med. Chem."},{"issue":"6","key":"10.1016\/j.ejmech.2025.118220_bib27","article-title":"In vitro and in vivo activities of KSP-1007, a broad spectrum inhibitor of serine- and metallo-\u03b2-lactamases, in combination with meropenem against carbapenem-resistant gram-negative bacteria","volume":"68","author":"Takemoto","year":"2024","journal-title":"Antimicrob. Agents Chemother."},{"issue":"17","key":"10.1016\/j.ejmech.2025.118220_bib28","doi-asserted-by":"crossref","first-page":"7267","DOI":"10.1021\/acs.jmedchem.7b00407","article-title":"Dipicolinic acid derivatives as inhibitors of New Delhi metallo-\u03b2-lactamase-1","volume":"60","author":"Chen","year":"2017","journal-title":"J. Med. Chem."},{"issue":"6","key":"10.1016\/j.ejmech.2025.118220_bib29","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1080\/08927022.2018.1559311","article-title":"Insight into the inhibition mechanism and structure\u2013activity relationship of 2,6-dipicolinic acid and its analogue to New Delhi metallo-\u03b2-lactamase-1","volume":"45","author":"Niu","year":"2019","journal-title":"Mol. Simul."},{"issue":"14","key":"10.1016\/j.ejmech.2025.118220_bib30","doi-asserted-by":"crossref","first-page":"1272","DOI":"10.1002\/cmdc.202000123","article-title":"Iminodiacetic acid as a novel metal-binding pharmacophore for New Delhi metallo-\u03b2-lactamase inhibitor development","volume":"15","author":"Chen","year":"2020","journal-title":"ChemMedChem"},{"issue":"4","key":"10.1016\/j.ejmech.2025.118220_bib31","doi-asserted-by":"crossref","first-page":"654","DOI":"10.1002\/cmdc.202000607","article-title":"Benzimidazole and benzoxazole zinc chelators as inhibitors of metallo-\u03b2-lactamase NDM-1","volume":"16","author":"Jackson","year":"2021","journal-title":"ChemMedChem"},{"issue":"1","key":"10.1016\/j.ejmech.2025.118220_bib32","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1038\/s41557-021-00831-x","article-title":"Imitation of \u03b2-lactam binding enables broad-spectrum metallo-\u03b2-lactamase inhibitors","volume":"14","author":"Brem","year":"2022","journal-title":"Nat. Chem."},{"issue":"9","key":"10.1016\/j.ejmech.2025.118220_bib33","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2023.105135","article-title":"Characterization of a novel inhibitor for the New Delhi metallo-\u03b2-lactamase-4: implications for drug design and combating bacterial drug resistance","volume":"299","author":"Thoden","year":"2023","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ejmech.2025.118220_bib34","doi-asserted-by":"crossref","first-page":"7062","DOI":"10.1021\/acs.jmedchem.4c02207","article-title":"Discovery of conformationally constrained dihydro benzo-indole derivatives as metallo-\u03b2-lactamase inhibitors to tackle multidrug-resistant bacterial infections","volume":"68","author":"Dhiman","year":"2025","journal-title":"J. Med. Chem."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118220_bib35","doi-asserted-by":"crossref","first-page":"386","DOI":"10.1016\/j.bmcl.2013.10.068","article-title":"Simplified captopril analogues as NDM-1 inhibitors","volume":"24","author":"Li","year":"2014","journal-title":"Bioorg. Med. Chem. Lett"},{"issue":"November 2020","key":"10.1016\/j.ejmech.2025.118220_bib36","article-title":"Structure-guided optimization of D-captopril for discovery of potent NDM-1 inhibitors","volume":"29","author":"Ma","year":"2021","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.118220_bib37","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2024.116140","article-title":"Fluorinated captopril analogues inhibit metallo-\u03b2-lactamases and facilitate structure determination of NDM-1 binding pose","volume":"266","author":"Kondratieva","year":"2024","journal-title":"Eur. J. Med. Chem."},{"issue":"7","key":"10.1016\/j.ejmech.2025.118220_bib38","doi-asserted-by":"crossref","first-page":"1931","DOI":"10.1016\/j.apsb.2021.01.018","article-title":"AncPhore: a versatile tool for anchor pharmacophore steered drug discovery with applications in discovery of new inhibitors targeting metallo-\u03b2-lactamases and indoleamine\/tryptophan 2,3-dioxygenases","volume":"11","author":"Dai","year":"2021","journal-title":"Acta Pharm. Sin. B"},{"issue":"19","key":"10.1016\/j.ejmech.2025.118220_bib39","doi-asserted-by":"crossref","first-page":"13746","DOI":"10.1021\/acs.jmedchem.3c01189","article-title":"Discovery of 2-aminothiazole-4-carboxylic acids as broad-spectrum metallo-\u03b2-lactamase inhibitors by mimicking carbapenem hydrolysate binding","volume":"66","author":"Yan","year":"2023","journal-title":"J. Med. Chem."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118220_bib40","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."},{"issue":"9","key":"10.1016\/j.ejmech.2025.118220_bib41","doi-asserted-by":"crossref","first-page":"2419","DOI":"10.1021\/acsinfecdis.0c00207","article-title":"ANT2681: SAR studies leading to the identification of a metallo-\u03b2-lactamase inhibitor with potential for clinical use in combination with meropenem for the treatment of infections caused by NDM-producing Enterobacteriaceae","volume":"6","author":"Davies","year":"2020","journal-title":"ACS Infect. Dis."},{"key":"10.1016\/j.ejmech.2025.118220_bib42","doi-asserted-by":"crossref","DOI":"10.1128\/AAC.00203-21","article-title":"Novel speci fi c metallo- b -lactamase inhibitor ANT2681 restores meropenem activity to clinically effective levels against NDM-","volume":"65","author":"Zalacain","year":"2021","journal-title":"Antimicrob. Agents Chemother."},{"issue":"9","key":"10.1016\/j.ejmech.2025.118220_bib43","doi-asserted-by":"crossref","DOI":"10.1016\/j.bmc.2020.115437","article-title":"A novel potent metal-binding NDM-1 inhibitor was identified by fragment virtual, SPR and NMR screening","volume":"28","author":"Guo","year":"2020","journal-title":"Bioorg. Med. Chem."},{"issue":"3","key":"10.1016\/j.ejmech.2025.118220_bib44","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1021\/acsinfecdis.2c00485","article-title":"In vitro and in vivo development of a \u03b2-Lactam-Metallo-\u03b2-Lactamase inhibitor: targeting carbapenem-resistant Enterobacterales","volume":"9","author":"Peters","year":"2023","journal-title":"ACS Infect. Dis."},{"issue":"13","key":"10.1016\/j.ejmech.2025.118220_bib45","doi-asserted-by":"crossref","first-page":"9141","DOI":"10.1021\/acs.jmedchem.1c00362","article-title":"Novel cephalosporin conjugates display potent and selective inhibition of imipenemase-type metallo-\u03b2-lactamases","volume":"64","author":"Tehrani","year":"2021","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.118220_bib46","first-page":"1","article-title":"Synthesis and evaluation of carbapenem\/metallo-\u03b2-lactamase inhibitor conjugates","volume":"202400302","author":"Gao","year":"2024","journal-title":"ChemMedChem"},{"issue":"11","key":"10.1016\/j.ejmech.2025.118220_bib47","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1021\/acsinfecdis.5b00046","article-title":"A substrate-mimicking scaffold as an inhibitor of the NDM-1 carbapenemase","volume":"1","author":"Gonz\u00e1lez","year":"2016","journal-title":"ACS Infect. Dis."},{"issue":"5","key":"10.1016\/j.ejmech.2025.118220_bib48","doi-asserted-by":"crossref","first-page":"3795","DOI":"10.1021\/acs.jmedchem.3c02209","article-title":"Rational design of benzobisheterocycle metallo-\u03b2-lactamase inhibitors: a tricyclic scaffold enhances potency against target enzymes","volume":"67","author":"Villamil","year":"2024","journal-title":"J. Med. Chem."},{"issue":"18","key":"10.1016\/j.ejmech.2025.118220_bib49","doi-asserted-by":"crossref","first-page":"8480","DOI":"10.1021\/acs.jmedchem.9b00728","article-title":"Heteroaryl phosphonates as noncovalent inhibitors of both serine- and metallocarbapenemases","volume":"62","author":"Pemberton","year":"2019","journal-title":"J. Med. Chem."},{"issue":"6","key":"10.1016\/j.ejmech.2025.118220_bib50","doi-asserted-by":"crossref","first-page":"1366","DOI":"10.1021\/acsinfecdis.9b00459","article-title":"Small molecule carboxylates inhibit metallo-\u03b2-lactamases and resensitize carbapenem-resistant bacteria to meropenem","volume":"6","author":"Tehrani","year":"2020","journal-title":"ACS Infect. Dis."},{"issue":"4","key":"10.1016\/j.ejmech.2025.118220_bib51","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/molecules27041283","article-title":"Risedronate and methotrexate are high-affinity inhibitors of New Delhi metallo-\u03b2-lactamase-1 (NDM-1): a drug repurposing approach","volume":"27","author":"Muteeb","year":"2022","journal-title":"Molecules"},{"issue":"1","key":"10.1016\/j.ejmech.2025.118220_bib52","doi-asserted-by":"crossref","DOI":"10.1038\/s42004-025-01510-5","article-title":"Dynamically chiral phosphonic acid-type metallo-\u03b2-lactamase inhibitors","volume":"8","author":"Guly\u00e1s","year":"2025","journal-title":"Commun. Chem."},{"issue":"2","key":"10.1016\/j.ejmech.2025.118220_bib53","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/j.bmcl.2017.10.074","article-title":"NOTA analogue: a first dithiocarbamate inhibitor of metallo-\u03b2-lactamases","volume":"28","author":"Zhang","year":"2018","journal-title":"Bioorg. Med. Chem. Lett"},{"issue":"21","key":"10.1016\/j.ejmech.2025.118220_bib54","doi-asserted-by":"crossref","first-page":"3436","DOI":"10.1016\/j.bmcl.2018.09.028","article-title":"Dithiocarbamates: efficient metallo-\u03b2-lactamase inhibitors with good antibacterial activity when combined with meropenem","volume":"28","author":"Wang","year":"2018","journal-title":"Bioorg. Med. Chem. Lett"},{"issue":"11","key":"10.1016\/j.ejmech.2025.118220_bib55","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/biom9110699","article-title":"Dithiocarbamate as a valuable scaffold for the inhibition of metallo-\u03b2-lactmases","volume":"9","author":"Ge","year":"2019","journal-title":"Biomolecules"},{"issue":"December 2020","key":"10.1016\/j.ejmech.2025.118220_bib56","first-page":"107","article-title":"Diaryl-substituted thiosemicarbazone: a potent scaffold for the development of New Delhi metallo-\u03b2-lactamase-1 inhibitors","author":"Li","year":"2021","journal-title":"Bioorg. Chem."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118220_bib57","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/j.apsb.2020.07.005","article-title":"Discovery of thiosemicarbazone derivatives as effective New Delhi metallo-\u03b2-lactamase-1 (NDM-1) inhibitors against NDM-1 producing clinical isolates","volume":"11","author":"Zhao","year":"2021","journal-title":"Acta Pharm. Sin. B"},{"issue":"May","key":"10.1016\/j.ejmech.2025.118220_bib58","article-title":"Dihydroxyphenyl-substituted thiosemicarbazone: a potent scaffold for the development of metallo-\u03b2-lactamases inhibitors and antimicrobial","volume":"127","author":"Liu","year":"2022","journal-title":"Bioorg. Chem."},{"issue":"September","key":"10.1016\/j.ejmech.2025.118220_bib59","article-title":"Discovery of isatin-\u03b2-methyldithiocarbazate derivatives as New Delhi metallo- \u03b2-lactamase-1 (NDM-1) inhibitors against NDM-1 producing clinical isolates","volume":"166","author":"Lv","year":"2023","journal-title":"Biomed. Pharmacother."},{"issue":"November 2024","key":"10.1016\/j.ejmech.2025.118220_bib60","article-title":"Novel methyldithiocarbazate derivatives as NDM-1 inhibitors to combat multidrug-resistant bacterial infection with \u03b2-lactams","volume":"154","author":"Wang","year":"2025","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.ejmech.2025.118220_bib61","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/S0378-1097(97)00472-2","article-title":"Inhibition of metallo-beta-lactamases by a series of thiol ester derivatives of mercaptophenylacetic acid","volume":"157","author":"Payne","year":"1997","journal-title":"FEMS Microbiol. Lett."},{"key":"10.1016\/j.ejmech.2025.118220_bib62","doi-asserted-by":"crossref","first-page":"3626","DOI":"10.1021\/jm501844d","article-title":"Drugs containing thiols as inhibitors of metallo-\u03b2 lactamases: strategy to combat multidrug-resistant bacteria","volume":"58","author":"Klingler","year":"2015","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.118220_bib63","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1021\/acsinfecdis.8b00366","article-title":"Novel mercapto propionamide derivatives with potent New Delhi metallo-\u03b2-lactamase-1 inhibitory activity and low toxicity","volume":"5","author":"Meng","year":"2019","journal-title":"ACS Infect. Dis."},{"issue":"4","key":"10.1016\/j.ejmech.2025.118220_bib64","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1021\/acsmedchemlett.5b00495","article-title":"Triazolylthioacetamide: a valid scaffold for the development of New Delhi metallo-\u03b2-lactmase-1 (NDM-1) inhibitors","volume":"7","author":"Zhai","year":"2016","journal-title":"ACS Med. Chem. Lett."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118220_bib65","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/j.jmb.2007.10.036","article-title":"Structural insights into the design of inhibitors for the L1 metallo-\u03b2-lactamase from Stenotrophomonas maltophilia","volume":"375","author":"Nauton","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ejmech.2025.118220_bib66","first-page":"972","article-title":"J. F. H. 1,2,4-Triazole-3-Thione compounds as inhibitors of dizinc metallo-b-lactamases","volume":"12","author":"Laurent","year":"2017","journal-title":"Chem. Commun."},{"key":"10.1016\/j.ejmech.2025.118220_bib67","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2020.112720","article-title":"4-Amino-1,2,4-Triazole-3-Thione-Derived Schiff bases as metallo-\u03b2-lactamase inhibitors","volume":"208","author":"Gavara","year":"2020","journal-title":"Eur. J. Med. Chem."},{"issue":"8","key":"10.1016\/j.ejmech.2025.118220_bib68","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/biom10081094","article-title":"4-(N-Alkyl-and-Acyl-Amino)-1,2,4-Triazole-3-Thione analogs as metallo-\u03b2-lactamase inhibitors: impact of 4-linker on potency and spectrum of inhibition","volume":"10","author":"Gavara","year":"2020","journal-title":"Biomolecules"},{"issue":"March","key":"10.1016\/j.ejmech.2025.118220_bib69","article-title":"1,2,4-Triazole-3-Thione analogues with an arylakyl group at position 4 as metallo-\u03b2-lactamase inhibitors","volume":"72","author":"Gavara","year":"2022","journal-title":"Bioorg. Med. Chem."},{"issue":"24","key":"10.1016\/j.ejmech.2025.118220_bib70","doi-asserted-by":"crossref","first-page":"16392","DOI":"10.1021\/acs.jmedchem.2c01257","article-title":"Optimization of 1,2,4-triazole-3-thiones toward broad-spectrum metallo-\u03b2-lactamase inhibitors showing potent synergistic activity on VIM- and NDM-1-producing clinical isolates","volume":"65","author":"Legru","year":"2022","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.118220_bib71","doi-asserted-by":"crossref","DOI":"10.1021\/acs.jmedchem.2c00766","article-title":"Rapid evolution of a fragment-like molecule to pan-metallo-beta-lactamase inhibitors: initial leads toward clinical candidates","author":"Mandal","year":"2022","journal-title":"J. Med. Chem."},{"issue":"52","key":"10.1016\/j.ejmech.2025.118220_bib72","first-page":"1","article-title":"Sca Ff old for the inhibition of serine and metallo- \u03b2 -lactamases","volume":"13","author":"Linciano","year":"2020","journal-title":"Pharmaceuticals"},{"issue":"12","key":"10.1016\/j.ejmech.2025.118220_bib73","doi-asserted-by":"crossref","first-page":"1682","DOI":"10.3390\/ph16121682","article-title":"Structure-based optimization of 1,2,4-triazole-3-thione derivatives: improving inhibition of NDM-\/VIM-Type metallo-\u03b2-lactamases and synergistic activity on resistant bacteria","volume":"16","author":"Bersani","year":"2023","journal-title":"Pharmaceuticals"},{"issue":"23","key":"10.1016\/j.ejmech.2025.118220_bib74","doi-asserted-by":"crossref","first-page":"5225","DOI":"10.1016\/j.bmcl.2017.10.038","article-title":"Azolylthioacetamides as a potent scaffold for the development of metallo-\u03b2-lactamase inhibitors","volume":"27","author":"Xiang","year":"2017","journal-title":"Bioorg. Med. Chem. Lett"},{"issue":"6","key":"10.1016\/j.ejmech.2025.118220_bib75","first-page":"1","article-title":"ZN148 is a modular synthetic metallo--lactamase inhibitor that reverses carbapenem resistance in gram-negative pathogens in vivo","volume":"64","author":"\u00d8rjan","year":"2020","journal-title":"Antimicrob. Agents Chemother."},{"issue":"April","key":"10.1016\/j.ejmech.2025.118220_bib76","article-title":"Bioisosteric investigation of ebselen: synthesis and in vitro characterization of 1,2-benzisothiazol-3(2H)-One derivatives as potent New Delhi metallo-\u03b2-lactamase inhibitors","volume":"100","author":"Jin","year":"2020","journal-title":"Bioorg. Chem."},{"issue":"8","key":"10.1016\/j.ejmech.2025.118220_bib77","doi-asserted-by":"crossref","DOI":"10.1016\/j.arabjc.2021.103270","article-title":"Facile synthesis of 4-aryl-N-(5-Methyl-1H-Pyrazol-3-Yl)Benzamides via Suzuki Miyaura reaction: antibacterial activity against clinically isolated NDM-1-positive bacteria and their docking studies","volume":"14","author":"Ahmad","year":"2021","journal-title":"Arab. J. Chem."},{"key":"10.1016\/j.ejmech.2025.118220_bib78","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1021\/acsinfecdis.1c00577","article-title":"Discovery of an effective small-moleculeallostericinhibitor of new Delhi Metallo-\u03b2-Lactamase(NDM","volume":"8","author":"Thomas","year":"2022","journal-title":"ACS Infect. Dis."},{"issue":"November 2023","key":"10.1016\/j.ejmech.2025.118220_bib79","article-title":"Discovery of hydroxamate as a promising scaffold dually inhibiting metallo- and serine-\u03b2-lactamases","volume":"265","author":"Wu","year":"2024","journal-title":"Eur. J. Med. Chem."},{"issue":"5","key":"10.1016\/j.ejmech.2025.118220_bib80","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1021\/ml200290p","article-title":"Small molecule suppression of carbapenem resistance in Ndm-1 producing Klebsiella pneumoniae","volume":"3","author":"Worthington","year":"2012","journal-title":"ACS Med. Chem. Lett."},{"issue":"7","key":"10.1016\/j.ejmech.2025.118220_bib81","doi-asserted-by":"crossref","first-page":"3515","DOI":"10.1039\/D0NJ06090A","article-title":"Synthesis of 1,3,4-trisubstituted pyrrolidines as meropenem adjuvants targeting New Delhi metallo-\u03b2-lactamase","volume":"45","author":"Jin","year":"2021","journal-title":"New J. Chem."},{"issue":"July","key":"10.1016\/j.ejmech.2025.118220_bib82","article-title":"A fragment-based drug discovery strategy applied to the identification of NDM-1 \u03b2-lactamase inhibitors","volume":"240","author":"Caburet","year":"2022","journal-title":"Eur. J. Med. Chem."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118220_bib83","doi-asserted-by":"crossref","DOI":"10.1080\/22221751.2023.2294854","article-title":"Novel nitroxoline derivative combating resistant bacterial infections through outer membrane disruption and competitive NDM-1 inhibition","volume":"13","author":"He","year":"2024","journal-title":"Emerg. Microb. Infect."},{"issue":"November 2018","key":"10.1016\/j.ejmech.2025.118220_bib84","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1016\/j.bioorg.2018.11.035","article-title":"Ebsulfur as a potent scaffold for inhibition and labelling of New Delhi metallo-\u03b2-lactamase-1 in vitro and in vivo","volume":"84","author":"Su","year":"2019","journal-title":"Bioorg. Chem."},{"issue":"12","key":"10.1016\/j.ejmech.2025.118220_bib85","doi-asserted-by":"crossref","first-page":"1084","DOI":"10.1038\/nchem.2110","article-title":"Rhodanine hydrolysis leads to potent thioenolate mediated metallo-\u03b2 2-lactamase inhibition","volume":"6","author":"Brem","year":"2014","journal-title":"Nat. Chem."},{"issue":"February","key":"10.1016\/j.ejmech.2025.118220_bib86","article-title":"Novel partially reversible NDM-1 inhibitors based on the naturally occurring houttuynin","volume":"147","author":"Wang","year":"2024","journal-title":"Bioorg. Chem."},{"issue":"April","key":"10.1016\/j.ejmech.2025.118220_bib87","first-page":"1","article-title":"PHT427 as an effective New Delhi metallo-\u03b2-lactamase-1 (NDM-1) inhibitor restored the susceptibility of meropenem against Enterobacteriaceae producing NDM-1","volume":"14","author":"Li","year":"2023","journal-title":"Front. Microbiol."},{"issue":"5","key":"10.1016\/j.ejmech.2025.118220_bib88","doi-asserted-by":"crossref","first-page":"3400","DOI":"10.1021\/acs.jmedchem.3c01614","article-title":"Structure guided discovery of novel Pan metallo-\u03b2-lactamase inhibitors with improved Gram-negative bacterial cell penetration","volume":"67","author":"Dong","year":"2024","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.118220_bib89","doi-asserted-by":"crossref","first-page":"1809","DOI":"10.1021\/acsinfecdis.1c00104","article-title":"StructuralBasisofMetallo-\u03b2-LactamaseInhibitionby N-Sulfamoylpyrrole-2-Carboxylates","volume":"7","author":"Farley","year":"2021","journal-title":"ACS Infect. Dis."},{"issue":"46","key":"10.1016\/j.ejmech.2025.118220_bib90","doi-asserted-by":"crossref","first-page":"9543","DOI":"10.1039\/C5CC02594J","article-title":"Ebselen as a potent covalent inhibitor of New Delhi metallo-\u03b2-lactamase (NDM-1)","volume":"51","author":"Chiou","year":"2015","journal-title":"Chem. Commun."},{"issue":"September","key":"10.1016\/j.ejmech.2025.118220_bib91","article-title":"1,2-Isoselenazol-3(2H)-One derivatives as NDM-1 inhibitors displaying synergistic antimicrobial effects with meropenem on NDM-1 producing clinical isolates","volume":"129","author":"Yue","year":"2022","journal-title":"Bioorg. Chem."},{"issue":"13","key":"10.1016\/j.ejmech.2025.118220_bib92","doi-asserted-by":"crossref","first-page":"2947","DOI":"10.1016\/j.bmc.2016.04.064","article-title":"Discovery of a novel covalent non-\u03b2-lactam inhibitor of the metallo-\u03b2-lactamase NDM-1","volume":"24","author":"Christopeit","year":"2016","journal-title":"Bioorg. Med. Chem."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118220_bib93","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41598-020-71025-7","article-title":"Strain-specific anti-biofilm and antibiotic-potentiating activity of 3\u2032,4\u2032-difluoroquercetin","volume":"10","author":"Kho","year":"2020","journal-title":"Sci. Rep."},{"issue":"5","key":"10.1016\/j.ejmech.2025.118220_bib94","doi-asserted-by":"crossref","first-page":"1624","DOI":"10.1021\/acsinfecdis.3c00715","article-title":"3-O-Substituted quercetin: an antibiotic-potentiating agent against multidrug-resistant gram-negative Enterobacteriaceae through simultaneous inhibition of efflux pump and broad-spectrum carbapenemases","volume":"10","author":"Lee","year":"2024","journal-title":"ACS Infect. Dis."},{"issue":"19","key":"10.1016\/j.ejmech.2025.118220_bib95","doi-asserted-by":"crossref","first-page":"5133","DOI":"10.1016\/j.bmc.2017.07.025","article-title":"Synthesis and biological evaluation of aspergillomarasmine A derivatives as novel NDM-1 inhibitor to overcome antibiotics resistance","volume":"25","author":"Zhang","year":"2017","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.118220_bib96","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/j.jgar.2019.02.003","article-title":"Discovery of NDM-1 inhibitors from natural products","volume":"18","author":"Shi","year":"2019","journal-title":"J. Glob. Antimicrob. Resist."},{"issue":"February","key":"10.1016\/j.ejmech.2025.118220_bib97","article-title":"Discovery of baicalin as NDM-1 inhibitor: virtual screening, biological evaluation and molecular simulation","volume":"88","author":"Shi","year":"2019","journal-title":"Bioorg. Chem."},{"issue":"10","key":"10.1016\/j.ejmech.2025.118220_bib98","doi-asserted-by":"crossref","first-page":"6955","DOI":"10.1111\/jcmm.14580","article-title":"Theaflavin-3,3\u2032-Digallate increases the antibacterial activity of \u03b2-lactam antibiotics by inhibiting metallo-\u03b2-lactamase activity","volume":"23","author":"Teng","year":"2019","journal-title":"J. Cell Mol. Med."},{"issue":"17","key":"10.1016\/j.ejmech.2025.118220_bib99","doi-asserted-by":"crossref","DOI":"10.3390\/ijms241713399","article-title":"Betaxolol as a potent inhibitor of NDM-1-positive E. Coli that synergistically enhances the anti-inflammatory effect in combination with meropenem","volume":"24","author":"Sun","year":"2023","journal-title":"Int. J. Mol. Sci."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118220_bib100","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1111\/bph.16210","article-title":"Novel metallo-\u03b2-lactamases inhibitors restore the susceptibility of carbapenems to New Delhi metallo-lactamase-1 (NDM-1)-Harbouring bacteria","volume":"181","author":"Guo","year":"2024","journal-title":"Br. J. Pharmacol."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118220_bib101","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12866-024-03214-7","article-title":"Phenotypic, molecular, and in silico characterization of coumarin as carbapenemase inhibitor to fight carbapenem-resistant Klebsiella pneumoniae","volume":"24","author":"Abdel-Halim","year":"2024","journal-title":"BMC Microbiol."},{"issue":"6","key":"10.1016\/j.ejmech.2025.118220_bib102","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/md18060295","article-title":"Pyridine-2,6-Dithiocarboxylic acid and its metal complexes: new inhibitors of New Delhi metallo \u03b2-lactamase-1","volume":"18","author":"Thomas","year":"2020","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ejmech.2025.118220_bib103","doi-asserted-by":"crossref","first-page":"975","DOI":"10.1021\/acsinfecdis.9b00385","article-title":"Identification of cisplatin and palladium(II) complexes as potent metallo-\u03b2-lactamase inhibitors for targeting carbapenem-resistant Enterobacteriaceae","volume":"6","author":"Chen","year":"2020","journal-title":"ACS Infect. Dis."},{"issue":"40","key":"10.1016\/j.ejmech.2025.118220_bib104","doi-asserted-by":"crossref","first-page":"14099","DOI":"10.1039\/D0DT02430A","article-title":"Ruthenium complexes as prospective inhibitors of metallo-\u03b2-lactamases to reverse carbapenem resistance","volume":"49","author":"Chen","year":"2020","journal-title":"Dalt. Trans."},{"issue":"Iii","key":"10.1016\/j.ejmech.2025.118220_bib105","first-page":"1","article-title":"Cobalt (III) Schiff base complexes as irreversible inhibitors of the metallo-\u03b2-","volume":"5133","author":"Ndm","year":"2025"},{"issue":"1","key":"10.1016\/j.ejmech.2025.118220_bib106","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41598-017-09588-1","article-title":"Potential inhibitors designed against NDM-1 type metallo-\u03b2-lactamases: an attempt to enhance efficacies of antibiotics against multi-drug-resistant bacteria","volume":"7","author":"Khan","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ejmech.2025.118220_bib107","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2021.113418","article-title":"Azetidinimines as a novel series of non-covalent broad-spectrum inhibitors of \u03b2-lactamases with submicromolar activities against carbapenemases KPC-2 (class A), NDM-1 (class B) and OXA-48 (class D)","volume":"219","author":"Romero","year":"2021","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.118220_bib108","doi-asserted-by":"crossref","DOI":"10.1016\/j.bmc.2023.117559","article-title":"Aurones and derivatives as promising New Delhi metallo-\u03b2-lactamase (NDM-1) inhibitors","volume":"97","author":"Caburet","year":"2024","journal-title":"Bioorg. Med. Chem."},{"issue":"14","key":"10.1016\/j.ejmech.2025.118220_bib109","doi-asserted-by":"crossref","first-page":"7491","DOI":"10.1021\/acs.jmedchem.9b01976","article-title":"Discovery of cyclic boronic acid QPX7728, an ultrabroad-spectrum inhibitor of serine and metallo-\u03b2-lactamases","volume":"63","author":"Hecker","year":"2020","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.118220_bib110","series-title":"Metallo-Beta-Lactamase Ihhibitors and Methods of Use There of","author":"Pasternak","year":"2018"},{"issue":"2","key":"10.1016\/j.ejmech.2025.118220_bib111","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/ph18020206","article-title":"Breakthrough advances in beta-lactamase inhibitors: new synthesized compounds and mechanisms of action against drug-resistant bacteria","volume":"18","author":"Huang","year":"2025","journal-title":"Pharmaceuticals"},{"key":"10.1016\/j.ejmech.2025.118220_bib112","doi-asserted-by":"crossref","first-page":"10556","DOI":"10.1021\/acs.jmedchem.5c00553","article-title":"Harder than metal: challenging antimicrobial resistance with metallo-\u03b2-lactamase inhibitors","volume":"68","author":"De Falco","year":"2025","journal-title":"J. Med. Chem."},{"issue":"6","key":"10.1016\/j.ejmech.2025.118220_bib113","doi-asserted-by":"crossref","DOI":"10.3390\/antibiotics13060502","article-title":"Implications of artificial intelligence in addressing antimicrobial resistance: innovations, global challenges, and healthcare's future","volume":"13","author":"Branda","year":"2024","journal-title":"Antibiotics"}],"container-title":["European Journal of Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523425009857?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523425009857?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,9]],"date-time":"2025-11-09T07:57:31Z","timestamp":1762675051000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0223523425009857"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,1]]},"references-count":113,"alternative-id":["S0223523425009857"],"URL":"https:\/\/doi.org\/10.1016\/j.ejmech.2025.118220","relation":{},"ISSN":["0223-5234"],"issn-type":[{"value":"0223-5234","type":"print"}],"subject":[],"published":{"date-parts":[[2026,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Disarming superbugs: New frontiers in inhibiting NDM-1 and other clinically relevant metallo-\u03b2-lactamases","name":"articletitle","label":"Article Title"},{"value":"European Journal of Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ejmech.2025.118220","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Elsevier Masson SAS. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"118220"}}