{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T03:55:37Z","timestamp":1790826937337,"version":"4.1.0"},"reference-count":46,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Bioorganic Chemistry"],"published-print":{"date-parts":[[2022,10]]},"DOI":"10.1016\/j.bioorg.2022.105928","type":"journal-article","created":{"date-parts":[[2022,6,13]],"date-time":"2022-06-13T11:18:48Z","timestamp":1655119128000},"page":"105928","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":11,"special_numbering":"C","title":["Dihydroxyphenyl-substituted thiosemicarbazone: A potent scaffold for the development of metallo-\u03b2-lactamases inhibitors and antimicrobial"],"prefix":"10.1016","volume":"127","author":[{"given":"Lu","family":"Liu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yin-Sui","family":"Xu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jia-Zhu","family":"Chigan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Le","family":"Zhai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Huan-Huan","family":"Ding","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiao-Rong","family":"Wu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wei-Ya","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ke-Wu","family":"Yang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bioorg.2022.105928_b0005","doi-asserted-by":"crossref","first-page":"3861","DOI":"10.1002\/anie.200500835","article-title":"Irreversible inhibition of metallo-beta-lactamase (IMP-1) by 3-(3-mercaptopropionylsulfanyl) propionic acid pentafluorophenyl ester","volume":"44","author":"Kurosaki","year":"2005","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.bioorg.2022.105928_b0010","doi-asserted-by":"crossref","first-page":"1022","DOI":"10.1002\/anie.200502984","article-title":"A new approach to the inhibition of metallo-beta-lactamases","volume":"45","author":"Spencer","year":"2006","journal-title":"Angew. Chem. Int. Ed. Engl."},{"issue":"10","key":"10.1016\/j.bioorg.2022.105928_b0015","doi-asserted-by":"crossref","DOI":"10.1128\/AAC.01076-18","article-title":"Past and present perspectives on beta-Lactamases","volume":"62","author":"Bush","year":"2018","journal-title":"Antimicrob Agents Ch."},{"issue":"10","key":"10.1016\/j.bioorg.2022.105928_b0020","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1021\/ar0400241","article-title":"Metallo-\u03b2-lactamases: novel weaponry for antibiotic resistance in bacteria","volume":"39","author":"Crowder","year":"2006","journal-title":"Acc. Chem. Res."},{"issue":"11","key":"10.1016\/j.bioorg.2022.105928_b0025","doi-asserted-by":"crossref","first-page":"4943","DOI":"10.1128\/AAC.00296-11","article-title":"Carbapenems: past, present, and future","volume":"55","author":"Papp-Wallace","year":"2011","journal-title":"Antimicrob Agents Ch."},{"issue":"2","key":"10.1016\/j.bioorg.2022.105928_b0030","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1089\/mdr.1996.2.245","article-title":"The aeromonas metallo-beta-lactamases: genetics, enzymology, and contribution to drug resistance","volume":"2","author":"Rossolini","year":"1996","journal-title":"Microb Drug Resist."},{"issue":"12","key":"10.1016\/j.bioorg.2022.105928_b0035","doi-asserted-by":"crossref","first-page":"1699","DOI":"10.1111\/j.1469-0691.2010.03385.x","article-title":"New Delhi metallo-beta-lactamase (NDM-1): towards a new pandemia?","volume":"16","author":"Rolain","year":"2010","journal-title":"Clin. Microbiol. Infect."},{"issue":"4","key":"10.1016\/j.bioorg.2022.105928_b0040","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1007\/s10096-016-2578-z","article-title":"Outbreak of NDM-1-producing Klebsiella pneumoniae ST76 and ST37 isolates in neonates","volume":"35","author":"Zhu","year":"2016","journal-title":"Eur. J. Clin. Microbiol. Infect. Dis."},{"issue":"6","key":"10.1016\/j.bioorg.2022.105928_b0045","doi-asserted-by":"crossref","first-page":"651","DOI":"10.2165\/11318430-000000000-00000","article-title":"Current challenges in antimicrobial chemotherapy","volume":"70","author":"Bebrone","year":"2010","journal-title":"Drugs."},{"issue":"5","key":"10.1016\/j.bioorg.2022.105928_b0050","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/S1473-3099(11)70056-1","article-title":"Metallo-\u03b2-lactamases: a last frontier for \u03b2-lactams?","volume":"11","author":"Cornaglia","year":"2011","journal-title":"Lancet"},{"issue":"39","key":"10.1016\/j.bioorg.2022.105928_b0055","doi-asserted-by":"crossref","first-page":"27960","DOI":"10.1074\/jbc.M113.485979","article-title":"Kinetics of avibactam inhibition against class A, C, and D \u03b2-lactamases","volume":"288","author":"Ehmann","year":"2013","journal-title":"J. Biol. Chem."},{"issue":"26","key":"10.1016\/j.bioorg.2022.105928_b0060","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.1601368113","article-title":"Cross-class metallo-\u03b2-lactamase inhibition by bisthiazolidines reveals multiple binding modes","volume":"113","author":"Hinchliffe","year":"2016","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.bioorg.2022.105928_b0065","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1016\/j.ejmech.2017.05.061","article-title":"Structure-activity relationship study and optimisation of 2-aminopyrrole-1-benzyl-4,5-diphenyl-1H-pyrrole-3-carbonitrile as a broad spectrum metallo-\u03b2-lactamase inhibitor","volume":"137","author":"McGeary","year":"2017","journal-title":"Eur. J. Med. Chem."},{"issue":"62","key":"10.1016\/j.bioorg.2022.105928_b0070","doi-asserted-by":"crossref","first-page":"8544","DOI":"10.1021\/acs.jmedchem.9b00911","article-title":"Bicyclic Boronate VNRX-5133 inhibits metallo- and serine-beta-lactamases","volume":"18","author":"Krajnc","year":"2019","journal-title":"J. Med. Chem."},{"issue":"23","key":"10.1016\/j.bioorg.2022.105928_b0075","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-beta-lactamase inhibitors","volume":"27","author":"Xiang","year":"2017","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.bioorg.2022.105928_b0080","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2020.104436","article-title":"Hydroxamic acid with benzenesulfonamide: an effective scaffold for the development of broad-spectrum metallo-\u03b2-lactamase inhibitors","volume":"105","author":"Li","year":"2020","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.bioorg.2022.105928_b0085","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-beta-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.bioorg.2022.105928_b0090","doi-asserted-by":"crossref","first-page":"2419","DOI":"10.1021\/acsinfecdis.0c00207","article-title":"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."},{"issue":"14","key":"10.1016\/j.bioorg.2022.105928_b0095","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-beta-lactamase inhibitor development","volume":"15","author":"Chen","year":"2020","journal-title":"ChemMedChem"},{"issue":"1","key":"10.1016\/j.bioorg.2022.105928_b0100","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1128\/AAC.01335-15","article-title":"Structural basis of Metallo-beta-Lactamase inhibition by captopril stereoisomers","volume":"60","author":"Brem","year":"2016","journal-title":"Antimicrob Agents Ch."},{"issue":"9","key":"10.1016\/j.bioorg.2022.105928_b0105","doi-asserted-by":"crossref","first-page":"965","DOI":"10.1016\/j.chembiol.2006.08.005","article-title":"Small-molecule screening identifies the selanazal drug ebselen as a potent inhibitor of DMT1-mediated iron uptake","volume":"13","author":"Wetli","year":"2006","journal-title":"Chem. Biol."},{"issue":"11","key":"10.1016\/j.bioorg.2022.105928_b0110","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1021\/acsinfecdis.5b00046","article-title":"Bisthiazolidines: a substrate-mimicking scaffold as an inhibitor of the NDM-1 Carbapenemase","volume":"1","author":"Gonzalez","year":"2015","journal-title":"ACS Infect Dis."},{"issue":"11","key":"10.1016\/j.bioorg.2022.105928_b0115","doi-asserted-by":"crossref","first-page":"699","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":"7506","key":"10.1016\/j.bioorg.2022.105928_b0120","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1038\/nature13445","article-title":"Aspergillomarasmine a overcomes metallo-beta-lactamase antibiotic resistance","volume":"510","author":"King","year":"2014","journal-title":"Nature"},{"issue":"2","key":"10.1016\/j.bioorg.2022.105928_b0125","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1093\/jac\/dkx403","article-title":"Bacterial zincophore [S, S]-ethylenediamine-N, N'-disuccinic acid is an effective inhibitor of MBLs","volume":"73","author":"Proschak","year":"2018","journal-title":"J. Antimicrob. Chemother."},{"issue":"9","key":"10.1016\/j.bioorg.2022.105928_b0130","doi-asserted-by":"crossref","first-page":"1407","DOI":"10.1021\/acsinfecdis.8b00137","article-title":"Synthesis and preclinical evaluation of TPA-Based zinc chelators as metallo-beta-lactamase inhibitors","volume":"4","author":"Schnaars","year":"2018","journal-title":"ACS Infect Dis."},{"issue":"4","key":"10.1016\/j.bioorg.2022.105928_b0135","doi-asserted-by":"crossref","first-page":"528","DOI":"10.1039\/C8MD00578H","article-title":"Synthesis and biological evaluation of zinc chelating compounds as metallo-beta-lactamase inhibitors","volume":"10","author":"Kildahl-Andersen","year":"2019","journal-title":"Medchemcomm."},{"issue":"11","key":"10.1016\/j.bioorg.2022.105928_b0140","doi-asserted-by":"crossref","first-page":"1525","DOI":"10.1016\/j.tet.2019.02.004","article-title":"Synthesis and biological evaluation of new dipicolylamine zinc chelators as metallo-\u03b2-lactamase inhibitors","volume":"75","author":"Prandina","year":"2019","journal-title":"Tetrahedron"},{"issue":"6","key":"10.1016\/j.bioorg.2022.105928_b0145","doi-asserted-by":"crossref","DOI":"10.1128\/AAC.02415-19","article-title":"ZN148 is a modular synthetic metallo-beta-lactamase inhibitor that reverses carbapenem resistance in Gram-negative pathogens in vivo","volume":"64","author":"Samuelsen","year":"2020","journal-title":"Antimicrob Agents Ch."},{"issue":"38","key":"10.1016\/j.bioorg.2022.105928_b0150","doi-asserted-by":"crossref","first-page":"4802","DOI":"10.1039\/C8CC01067F","article-title":"A protein structure-guided covalent scaffold selectively targets the B1 and B2 subclass metallo-beta-lactamases","volume":"54","author":"Chen","year":"2018","journal-title":"Chem. Commun. (Camb.)"},{"key":"10.1016\/j.bioorg.2022.105928_b0155","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."},{"key":"10.1016\/j.bioorg.2022.105928_b0160","doi-asserted-by":"crossref","first-page":"105161","DOI":"10.1016\/j.ejps.2019.105161","article-title":"3-Bromopyruvate as a potent covalently reversible inhibitor of New Delhi metallo-\u03b2-lactamase-1 (NDM-1)","volume":"142","author":"Kang","year":"2020","journal-title":"Eur J Pharm Sci."},{"issue":"1","key":"10.1016\/j.bioorg.2022.105928_b0165","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1038\/s41467-018-02828-6","article-title":"Bismuth antimicrobial drugs serve as broad-spectrum metallo-\u03b2-lactamase inhibitors","volume":"9","author":"Wang","year":"2018","journal-title":"Nat Commun."},{"key":"10.1016\/j.bioorg.2022.105928_b0170","doi-asserted-by":"crossref","DOI":"10.1021\/acsinfecdis.9b00385","article-title":"Identification of cisplatin and palladium (II) complexes as potent metallo-beta-lactamases inhibitors for targeting carbapenem-resistant enterobacteriaceae (CRE)","author":"Chen","year":"2020","journal-title":"ACS Infect Dis."},{"key":"10.1016\/j.bioorg.2022.105928_b0175","article-title":"Ruthenium complex as prospective inhibitor of metallo-\u03b2-lactamases to reverse carbapenem resistance","author":"Cheng","year":"2020","journal-title":"Dalton Trans"},{"issue":"7","key":"10.1016\/j.bioorg.2022.105928_b0180","doi-asserted-by":"crossref","first-page":"569","DOI":"10.2174\/1389557518666181015152657","article-title":"A structural chemistry perspective on the antimalarial properties of thiosemicarbazone metal complexes","volume":"19","author":"Summers","year":"2019","journal-title":"Mini-Rev. Med. Chem."},{"key":"10.1016\/j.bioorg.2022.105928_b0185","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1186\/s13045-016-0330-x","article-title":"The novel thiosemicarbazone, di-2-pyridylketone 4-cyclohexyl-4-methyl-3-thiosemicarbazone (DpC), inhibits neuroblastoma growth in vitro and in vivo via multiple mechanisms","volume":"9","author":"Guo","year":"2016","journal-title":"J. Hematol. Oncol."},{"issue":"4","key":"10.1016\/j.bioorg.2022.105928_b0190","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1007\/s10637-008-9123-6","article-title":"A phase 2 consortium (P2C) trial of 3-aminopyridine-2-carboxaldehyde thiosemicarbazone (3-AP) for advanced adenocarcinoma of the pancreas","volume":"26","author":"Attia","year":"2008","journal-title":"Invest. New Drugs."},{"key":"10.1016\/j.bioorg.2022.105928_b0195","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1016\/j.molliq.2018.01.083","article-title":"Synthesis, tyrosinase inhibition and transportation behavior of novel beta-enamino thiosemicarbazide derivatives by human serum albumin","volume":"254","author":"Chaves","year":"2018","journal-title":"J. Mol. Liq."},{"key":"10.1016\/j.bioorg.2022.105928_b0200","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2020.104576","article-title":"Diaryl-substituted thiosemicarbazone: a potent scaffold for the development of New Delhi metallo-\u03b2-lactamase-1 inhibitors","volume":"107","author":"Li","year":"2021","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.bioorg.2022.105928_b0205","doi-asserted-by":"crossref","first-page":"574","DOI":"10.1038\/s41429-021-00440-3","article-title":"Thiosemicarbazones exhibit potent inhibitory efficacy against New Delhi metallo-\u03b2-lactamase-1 in vitro and in vivo","volume":"74","author":"Ge","year":"2021","journal-title":"J. Antibiot."},{"key":"10.1016\/j.bioorg.2022.105928_b0210","doi-asserted-by":"crossref","first-page":"1671","DOI":"10.1021\/acsinfecdis.8b00147","article-title":"Real-time monitoring of NDM-1 activity in live bacterial cells by isothermal titration calorimetry: a new approach to measure inhibition of antibiotic-resistant bacteria","volume":"4","author":"Zhang","year":"2018","journal-title":"ACS Infect. Dis."},{"issue":"6","key":"10.1016\/j.bioorg.2022.105928_b0215","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1177\/108705710100600609","article-title":"High-density miniaturized thermal shift assays as a general strategy for drug discovery","volume":"6","author":"Pantoliano","year":"2001","journal-title":"J. Biomol. Screen."},{"key":"10.1016\/j.bioorg.2022.105928_b0220","doi-asserted-by":"crossref","first-page":"3626","DOI":"10.1021\/jm501844d","article-title":"Approved drugs containing thiols as inhibitors of metallo-\u03b2-lactamases: strategy to combat multidrug-resistant Ba","volume":"58","author":"Klingler","year":"2015","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bioorg.2022.105928_b0225","doi-asserted-by":"crossref","first-page":"4142","DOI":"10.1039\/C9BM01050E","article-title":"Construction, mechanism and antibacterial resistance insight of the polypeptide-based nanoparticles","volume":"7","author":"Zhen","year":"2019","journal-title":"Biomater. Sci."},{"key":"10.1016\/j.bioorg.2022.105928_b0230","doi-asserted-by":"crossref","first-page":"105138","DOI":"10.1016\/j.bioorg.2021.105138","article-title":"N-acylhydrazones confer inhibitory efficacy against New Delhi metallo-\u03b2-lactamase-1","volume":"114","author":"Gao","year":"2021","journal-title":"Bioorg. Chem."}],"container-title":["Bioorganic Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0045206822003339?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0045206822003339?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,23]],"date-time":"2025-09-23T08:34:07Z","timestamp":1758616447000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0045206822003339"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,10]]},"references-count":46,"alternative-id":["S0045206822003339"],"URL":"https:\/\/doi.org\/10.1016\/j.bioorg.2022.105928","relation":{},"ISSN":["0045-2068"],"issn-type":[{"value":"0045-2068","type":"print"}],"subject":[],"published":{"date-parts":[[2022,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Dihydroxyphenyl-substituted thiosemicarbazone: A potent scaffold for the development of metallo-\u03b2-lactamases inhibitors and antimicrobial","name":"articletitle","label":"Article Title"},{"value":"Bioorganic Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bioorg.2022.105928","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"105928"}}