{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T03:55:30Z","timestamp":1790826930926,"version":"4.1.0"},"reference-count":69,"publisher":"Oxford University Press (OUP)","issue":"10","license":[{"start":{"date-parts":[[2020,6,26]],"date-time":"2020-06-26T00:00:00Z","timestamp":1593129600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["AI146829"],"award-info":[{"award-number":["AI146829"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["GM128885"],"award-info":[{"award-number":["GM128885"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["AI134673"],"award-info":[{"award-number":["AI134673"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["AI111753"],"award-info":[{"award-number":["AI111753"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["AI141101"],"award-info":[{"award-number":["AI141101"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100004917","name":"Cancer Prevention & Research Institute of Texas","doi-asserted-by":"crossref","award":["RR160053"],"award-info":[{"award-number":["RR160053"]}],"id":[{"id":"10.13039\/100004917","id-type":"DOI","asserted-by":"crossref"}]},{"name":"CPRIT Scholar in Cancer Research"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2020,10,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:sec>\n                  <jats:title>Objectives<\/jats:title>\n                  <jats:p>Metallo-\u03b2-lactamases (MBLs) are an emerging class of antimicrobial resistance enzymes that degrade \u03b2-lactam antibiotics, including last-resort carbapenems. Infections caused by carbapenemase-producing Enterobacteriaceae (CPE) are increasingly prevalent, but treatment options are limited. While several serine-dependent \u03b2-lactamase inhibitors are formulated with commonly prescribed \u03b2-lactams, no MBL inhibitors are currently approved for combinatorial therapies. New compounds that target MBLs to restore carbapenem activity against CPE are therefore urgently needed. Herein we identified and characterized novel synthetic peptide inhibitors that bound to and inhibited NDM-1, which is an emerging \u03b2-lactam resistance mechanism in CPE.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Methods<\/jats:title>\n                  <jats:p>We leveraged Surface Localized Antimicrobial displaY (SLAY) to identify and characterize peptides that inhibit NDM-1, which is a primary carbapenem resistance mechanism in CPE. Lead inhibitor sequences were chemically synthesized and MBCs and MICs were calculated in the presence\/absence of carbapenems. Kinetic analysis with recombinant NDM-1 and select peptides tested direct binding and supported NDM-1 inhibitor mechanisms of action. Inhibitors were also tested for cytotoxicity.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Results<\/jats:title>\n                  <jats:p>We identified approximately 1700 sequences that potentiated carbapenem-dependent killing against NDM-1 Escherichia coli. Several also enhanced meropenem-dependent killing of other CPE. Biochemical characterization of a subset indicated the peptides penetrated the bacterial periplasm and directly bound NDM-1 to inhibit enzymatic activity. Additionally, each demonstrated minimal haemolysis and cytotoxicity against mammalian cell lines.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Conclusions<\/jats:title>\n                  <jats:p>Our approach advances a molecular platform for antimicrobial discovery, which complements the growing need for alternative antimicrobials. We also discovered lead NDM-1 inhibitors, which serve as a starting point for further chemical optimization.<\/jats:p>\n               <\/jats:sec>","DOI":"10.1093\/jac\/dkaa242","type":"journal-article","created":{"date-parts":[[2020,5,20]],"date-time":"2020-05-20T11:11:27Z","timestamp":1589973087000},"page":"2843-2851","source":"Crossref","is-referenced-by-count":17,"title":["Discovery and characterization of New Delhi metallo-\u03b2-lactamase-1 inhibitor peptides that potentiate meropenem-dependent killing of carbapenemase-producing Enterobacteriaceae"],"prefix":"10.1093","volume":"75","author":[{"given":"Misha I","family":"Kazi","sequence":"first","affiliation":[{"name":"Department of Biology, University of Texas at Arlington, Arlington, TX, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Blair W","family":"Perry","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Texas at Arlington, Arlington, TX, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daren C","family":"Card","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Texas at Arlington, Arlington, TX, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard D","family":"Schargel","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Texas at Arlington, Arlington, TX, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hana B","family":"Ali","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Texas at Arlington, Arlington, TX, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Victor C","family":"Obuekwe","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Texas at Arlington, Arlington, TX, USA"},{"name":"Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, TX, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Madhab","family":"Sapkota","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Texas at Arlington, Arlington, TX, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katie N","family":"Kang","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Texas at Arlington, Arlington, TX, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark W","family":"Pellegrino","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Texas at Arlington, Arlington, TX, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David E","family":"Greenberg","sequence":"additional","affiliation":[{"name":"Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, TX, USA"},{"name":"Department of Microbiology, University of Texas Southwestern Medical Center, Dallas, TX, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Todd A","family":"Castoe","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Texas at Arlington, Arlington, TX, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joseph M","family":"Boll","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Texas at Arlington, Arlington, TX, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2020,6,26]]},"reference":[{"key":"2020101416050804400_dkaa242-B1","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1016\/j.tim.2006.07.008","article-title":"The \u03b2-lactamase threat in Enterobacteriaceae, Pseudomonas and Acinetobacter","volume":"14","author":"Livermore","year":"2006","journal-title":"Trends Microbiol"},{"key":"2020101416050804400_dkaa242-B2","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1016\/j.ijantimicag.2011.12.012","article-title":"Fourteen years in resistance","volume":"39","author":"Livermore","year":"2012","journal-title":"Int J Antimicrob Agents"},{"key":"2020101416050804400_dkaa242-B3","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 NY Acad Sci"},{"key":"2020101416050804400_dkaa242-B4","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1111\/j.1574-6976.2008.00105.x","article-title":"The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis","volume":"32","author":"Sauvage","year":"2008","journal-title":"FEMS Microbiol Rev"},{"key":"2020101416050804400_dkaa242-B5","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 Chemother"},{"key":"2020101416050804400_dkaa242-B6","doi-asserted-by":"crossref","first-page":"564","DOI":"10.2174\/092986709787458498","article-title":"Current status of newer carbapenems","volume":"16","author":"Bassetti","year":"2009","journal-title":"Curr Med Chem"},{"key":"2020101416050804400_dkaa242-B7","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1586\/14787210.5.5.833","article-title":"Current concepts in antibiotic-resistant gram-negative bacteria","volume":"5","author":"Torres","year":"2007","journal-title":"Expert Rev Anti Infect Ther"},{"key":"2020101416050804400_dkaa242-B8","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1002\/med.10009","article-title":"Chemical control of phospholipid distribution across bilayer membranes","volume":"22","author":"Boon","year":"2002","journal-title":"Med Res Rev"},{"key":"2020101416050804400_dkaa242-B9","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1046\/j.1469-0691.2000.00107.x","article-title":"Recommendation for treatment of severe infections caused by Enterobacteriaceae producing extended-spectrum \u03b2-lactamases (ESBLs)","volume":"6","author":"Paterson","year":"2000","journal-title":"Clin Microbiol Infect"},{"key":"2020101416050804400_dkaa242-B10","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1053\/srin.2002.36446","article-title":"Serious infections caused by enteric gram-negative bacilli \u2013 mechanisms of antibiotic resistance and implications for therapy of gram-negative sepsis in the transplanted patient","volume":"17","author":"Paterson","year":"2002","journal-title":"Semin Respir Infect"},{"key":"2020101416050804400_dkaa242-B11","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1128\/CMR.18.4.657-686.2005","article-title":"Extended-spectrum \u03b2-lactamases: a clinical update","volume":"18","author":"Paterson","year":"2005","journal-title":"Clin Microbiol Rev"},{"key":"2020101416050804400_dkaa242-B12","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1128\/CMR.00001-07","article-title":"Carbapenemases: the versatile \u03b2-lactamases","volume":"20","author":"Queenan","year":"2007","journal-title":"Clin Microbiol Rev"},{"key":"2020101416050804400_dkaa242-B13","first-page":"297","article-title":"Impact of the New Delhi metallo-\u03b2-lactamase on \u03b2-lactam antibiotics","volume":"8","author":"Zmarlicka","year":"2015","journal-title":"Infect Drug Resist"},{"key":"2020101416050804400_dkaa242-B14","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1042\/bj2760269","article-title":"A standard numbering scheme for the class A \u03b2-lactamases","volume":"276","author":"Ambler","year":"1991","journal-title":"Biochem J"},{"key":"2020101416050804400_dkaa242-B15","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1128\/AAC.01009-09","article-title":"Updated functional classification of \u03b2-lactamases","volume":"54","author":"Bush","year":"2010","journal-title":"Antimicrob Agents Chemother"},{"key":"2020101416050804400_dkaa242-B16","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1146\/annurev.mi.45.100191.000345","article-title":"Serine \u03b2-lactamases and penicillin-binding proteins","volume":"45","author":"Ghuysen","year":"1991","journal-title":"Annu Rev Microbiol"},{"key":"2020101416050804400_dkaa242-B17","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"},{"key":"2020101416050804400_dkaa242-B18","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"},{"key":"2020101416050804400_dkaa242-B19","doi-asserted-by":"crossref","first-page":"614","DOI":"10.1016\/S1367-5931(99)00017-4","article-title":"Metallo-\u03b2-lactamase: structure and mechanism","volume":"3","author":"Wang","year":"1999","journal-title":"Curr Opin Chem Biol"},{"key":"2020101416050804400_dkaa242-B20","doi-asserted-by":"crossref","first-page":"890","DOI":"10.1128\/AAC.43.4.890","article-title":"Structure of In31, a blaIMP-containing Pseudomonas aeruginosa integron phyletically related to In5, which carries an unusual array of gene cassettes","volume":"43","author":"Laraki","year":"1999","journal-title":"Antimicrob Agents Chemother"},{"key":"2020101416050804400_dkaa242-B21","doi-asserted-by":"crossref","first-page":"1584","DOI":"10.1128\/AAC.43.7.1584","article-title":"Cloning and characterization of blaVIM, a new integron-borne metallo-\u03b2-lactamase gene from a Pseudomonas aeruginosa clinical isolate","volume":"43","author":"Lauretti","year":"1999","journal-title":"Antimicrob Agents Chemother"},{"key":"2020101416050804400_dkaa242-B22","doi-asserted-by":"crossref","first-page":"5046","DOI":"10.1128\/AAC.00774-09","article-title":"Characterization of a new metallo-\u03b2-lactamase gene, bla(NDM-1), and a novel erythromycin esterase gene carried on a unique genetic structure in Klebsiella pneumoniae sequence type 14 from India","volume":"53","author":"Yong","year":"2009","journal-title":"Antimicrob Agents Chemother"},{"key":"2020101416050804400_dkaa242-B23","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1097\/QCO.0b013e328303670b","article-title":"Clinically significant carbapenemases: an update","volume":"21","author":"Walsh","year":"2008","journal-title":"Curr Opin Infect Dis"},{"key":"2020101416050804400_dkaa242-B24","doi-asserted-by":"crossref","first-page":"S8","DOI":"10.1016\/S0924-8579(10)70004-2","article-title":"Emerging carbapenemases: a global perspective","volume":"36","author":"Walsh","year":"2010","journal-title":"Int J Antimicrob Agents"},{"key":"2020101416050804400_dkaa242-B25","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1128\/AAC.44.4.891-897.2000","article-title":"Characterization of VIM-2, a carbapenem-hydrolyzing metallo-\u03b2-lactamase and its plasmid- and integron-borne gene from a Pseudomonas aeruginosa clinical isolate in France","volume":"44","author":"Poirel","year":"2000","journal-title":"Antimicrob Agents Chemother"},{"key":"2020101416050804400_dkaa242-B26","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 Infect Dis"},{"key":"2020101416050804400_dkaa242-B27","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":"2020101416050804400_dkaa242-B28","author":"Tacconelli","year":"2017"},{"key":"2020101416050804400_dkaa242-B29","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1016\/S1473-3099(17)30753-3","article-title":"Discovery, research, and development of new antibiotics: the WHO priority list of antibiotic-resistant bacteria and tuberculosis","volume":"18","author":"Tacconelli","year":"2018","journal-title":"Lancet Infect Dis"},{"key":"2020101416050804400_dkaa242-B30","doi-asserted-by":"crossref","first-page":"852","DOI":"10.1128\/AAC.11.5.852","article-title":"Clavulanic acid: a \u03b2-lactamase-inhibiting \u03b2-lactam from Streptomyces clavuligerus","volume":"11","author":"Reading","year":"1977","journal-title":"Antimicrob Agents Chemother"},{"key":"2020101416050804400_dkaa242-B31","doi-asserted-by":"crossref","first-page":"414","DOI":"10.1128\/AAC.14.3.414","article-title":"CP-45,899, a \u03b2-lactamase inhibitor that extends the antibacterial spectrum of \u03b2-lactams: initial bacteriological characterization","volume":"14","author":"English","year":"1978","journal-title":"Antimicrob Agents Chemother"},{"key":"2020101416050804400_dkaa242-B32","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1098\/rstb.1980.0048","article-title":"\u03b2-Lactamase inactivation by mechanism-based reagents","volume":"289","author":"Fisher","year":"1980","journal-title":"Philos Trans R Soc Lond B Biol Sci"},{"key":"2020101416050804400_dkaa242-B33","doi-asserted-by":"crossref","first-page":"11663","DOI":"10.1073\/pnas.1205073109","article-title":"Avibactam is a covalent, reversible, non-\u03b2-lactam \u03b2-lactamase inhibitor","volume":"109","author":"Ehmann","year":"2012","journal-title":"Proc Natl Acad Sci USA"},{"key":"2020101416050804400_dkaa242-B34","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1038\/s41579-019-0159-8","article-title":"Interplay between \u03b2-lactamases and new \u03b2-lactamase inhibitors","volume":"17","author":"Bush","year":"2019","journal-title":"Nat Rev Microbiol"},{"key":"2020101416050804400_dkaa242-B35","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1093\/jac\/dkh550","article-title":"A specific peptide inhibitor of the class B metallo-\u03b2-lactamase L-1 from Stenotrophomonas maltophilia identified using phage display","volume":"55","author":"Sanschagrin","year":"2005","journal-title":"J Antimicrob Chemother"},{"key":"2020101416050804400_dkaa242-B36","doi-asserted-by":"crossref","first-page":"5169","DOI":"10.1016\/j.bmcl.2006.07.001","article-title":"Homo-cysteinyl peptide inhibitors of the L1 metallo-\u03b2-lactamase, and SAR as determined by combinatorial library synthesis","volume":"16","author":"Sun","year":"2006","journal-title":"Bioorg Med Chem Lett"},{"key":"2020101416050804400_dkaa242-B37","doi-asserted-by":"crossref","first-page":"2455","DOI":"10.1016\/0960-894X(96)00453-2","article-title":"Trifluoromethyl alcohol and ketone inhibitors of metallo-\u03b2-lactamases","volume":"6","author":"Walter","year":"1996","journal-title":"Bioorg Med Chem Lett"},{"key":"2020101416050804400_dkaa242-B38","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":"2020101416050804400_dkaa242-B39","doi-asserted-by":"crossref","first-page":"4698","DOI":"10.1016\/j.bmcl.2016.08.048","article-title":"Optimization of amino acid thioesters as inhibitors of metallo-\u03b2-lactamase L1","volume":"26","author":"Liu","year":"2016","journal-title":"Bioorg Med Chem Lett"},{"key":"2020101416050804400_dkaa242-B40","doi-asserted-by":"crossref","first-page":"618","DOI":"10.1016\/j.cell.2017.12.009","article-title":"Discovery of next-generation antimicrobials through bacterial self-screening of surface-displayed peptide libraries","volume":"172","author":"Tucker","year":"2018","journal-title":"Cell"},{"key":"2020101416050804400_dkaa242-B41","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1093\/bioinformatics\/btp616","article-title":"edgeR: a Bioconductor package for differential expression analysis of digital gene expression data","volume":"26","author":"Robinson","year":"2010","journal-title":"Bioinformatics"},{"key":"2020101416050804400_dkaa242-B42","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1038\/nmeth.3885","article-title":"Data-driven hypothesis weighting increases detection power in genome-scale multiple testing","volume":"13","author":"Ignatiadis","year":"2016","journal-title":"Nat Methods"},{"key":"2020101416050804400_dkaa242-B43","doi-asserted-by":"crossref","first-page":"4","DOI":"10.32614\/RJ-2015-001","article-title":"Peptides: a package for data mining of antimicrobial peptides","volume":"7","author":"Osorio","year":"2015","journal-title":"R J"},{"key":"2020101416050804400_dkaa242-B44","volume-title":"R: A Language and Environment for Statistical Computing","year":"2019"},{"key":"2020101416050804400_dkaa242-B45","doi-asserted-by":"crossref","first-page":"3645","DOI":"10.1093\/bioinformatics\/btx469","article-title":"ggseqlogo: a versatile R package for drawing sequence logos","volume":"33","author":"Wagih","year":"2017","journal-title":"Bioinformatics"},{"key":"2020101416050804400_dkaa242-B46","first-page":"e50854","article-title":"Establishing the minimal bactericidal concentration of an antimicrobial agent for planktonic cells (MBC-P) and biofilm cells (MBC-B)","author":"Mah","year":"2014","journal-title":"J Vis Exp"},{"key":"2020101416050804400_dkaa242-B47","first-page":"75","volume-title":"Antimicrobial Susceptibility Testing Protocols. CRC Press","author":"Qaiyumi"},{"key":"2020101416050804400_dkaa242-B48","doi-asserted-by":"crossref","first-page":"1604","DOI":"10.1111\/mmi.14240","article-title":"Colistin heteroresistance in Enterobacter cloacae is regulated by PhoPQ-dependent 4-amino-4-deoxy-l-arabinose addition to lipid A","volume":"111","author":"Kang","year":"2019","journal-title":"Mol Microbiol"},{"key":"2020101416050804400_dkaa242-B49","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.40171","article-title":"The Acinetobacter baumannii Mla system and glycerophospholipid transport to the outer membrane","volume":"8","author":"Kamischke","year":"2019","journal-title":"Elife"},{"key":"2020101416050804400_dkaa242-B50","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 Antimicrob Chemother"},{"key":"2020101416050804400_dkaa242-B51","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1002\/cmdc.201700240","article-title":"Synthesis, DNA cleavage activity, cytotoxicity, acetylcholinesterase inhibition, and acute murine toxicity of redox-active ruthenium(ii) polypyridyl complexes","volume":"12","author":"Alatrash","year":"2017","journal-title":"ChemMedChem"},{"key":"2020101416050804400_dkaa242-B52","doi-asserted-by":"crossref","first-page":"27394","DOI":"10.1038\/srep27394","article-title":"Design of an \u03b1-helical antimicrobial peptide with improved cell-selective and potent anti-biofilm activity","volume":"6","author":"Zhang","year":"2016","journal-title":"Sci Rep"},{"key":"2020101416050804400_dkaa242-B53","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1093\/jac\/dkl354","article-title":"Two decades of imipenem therapy","volume":"58","author":"Rodloff","year":"2006","journal-title":"J Antimicrob Chemother"},{"key":"2020101416050804400_dkaa242-B54","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1038\/nrmicro1994","article-title":"The porin and the permeating antibiotic: a selective diffusion barrier in Gram-negative bacteria","volume":"6","author":"Pag\u00e8s","year":"2008","journal-title":"Nat Rev Microbiol"},{"key":"2020101416050804400_dkaa242-B55","doi-asserted-by":"crossref","first-page":"E6228","DOI":"10.1073\/pnas.1611594113","article-title":"A penicillin-binding protein inhibits selection of colistin-resistant, lipooligosaccharide-deficient Acinetobacter baumannii","volume":"113","author":"Boll","year":"2016","journal-title":"Proc Natl Acad Sci USA"},{"key":"2020101416050804400_dkaa242-B56","doi-asserted-by":"crossref","first-page":"e00478","DOI":"10.1128\/mBio.00478-15","article-title":"Reinforcing lipid A acylation on the cell surface of Acinetobacter baumannii promotes cationic antimicrobial peptide resistance and desiccation survival","volume":"6","author":"Boll","year":"2015","journal-title":"MBio"},{"key":"2020101416050804400_dkaa242-B57","doi-asserted-by":"crossref","first-page":"3138","DOI":"10.1016\/j.bmc.2013.03.031","article-title":"An altered zinc-binding site confers resistance to a covalent inactivator of New Delhi metallo-\u03b2-lactamase-1 (NDM-1) discovered by high-throughput screening","volume":"21","author":"Thomas","year":"2013","journal-title":"Bioorg Med Chem"},{"key":"2020101416050804400_dkaa242-B58","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1093\/jac\/dku403","article-title":"Biochemical characterization of New Delhi metallo-\u03b2-lactamase variants reveals differences in protein stability","volume":"70","author":"Makena","year":"2015","journal-title":"J Antimicrob Chemother"},{"key":"2020101416050804400_dkaa242-B59","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1021\/acsinfecdis.6b00045","article-title":"Contribution of amphipathicity and hydrophobicity to the antimicrobial activity and cytotoxicity of \u03b2-hairpin peptides","volume":"2","author":"Edwards","year":"2016","journal-title":"ACS Infect Dis"},{"key":"2020101416050804400_dkaa242-B60","doi-asserted-by":"crossref","first-page":"43122","DOI":"10.1074\/jbc.M106961200","article-title":"An inner membrane enzyme in Salmonella and Escherichia coli that transfers 4-amino-4-deoxy-L-arabinose to lipid A: induction on polymyxin-resistant mutants and role of a novel lipid-linked donor","volume":"276","author":"Trent","year":"2001","journal-title":"J Biol Chem"},{"key":"2020101416050804400_dkaa242-B61","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1146\/annurev.biochem.76.010307.145803","article-title":"Lipid A modification systems in gram-negative bacteria","volume":"76","author":"Raetz","year":"2007","journal-title":"Annu Rev Biochem"},{"key":"2020101416050804400_dkaa242-B62","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1128\/AAC.31.2.230","article-title":"Decreased binding of antibiotics to lipopolysaccharides from polymyxin-resistant strains of Escherichia coli and Salmonella typhimurium","volume":"31","author":"Peterson","year":"1987","journal-title":"Antimicrob Agents Chemother"},{"key":"2020101416050804400_dkaa242-B63","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1172\/JCI114198","article-title":"Interaction of human defensins with Escherichia coli. Mechanism of bactericidal activity","volume":"84","author":"Lehrer","year":"1989","journal-title":"J Clin Invest"},{"key":"2020101416050804400_dkaa242-B64","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 bacteria","volume":"58","author":"Klingler","year":"2015","journal-title":"J Med Chem"},{"key":"2020101416050804400_dkaa242-B65","doi-asserted-by":"crossref","first-page":"1589","DOI":"10.1016\/j.bmcl.2016.02.007","article-title":"Captopril analogues as metallo-\u03b2-lactamase inhibitors","volume":"26","author":"Yusof","year":"2016","journal-title":"Bioorg Med Chem Lett"},{"key":"2020101416050804400_dkaa242-B66","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1016\/j.ejmech.2016.03.017","article-title":"Design, synthesis, and in vitro and biological evaluation of potent amino acid-derived thiol inhibitors of the metallo-\u03b2-lactamase IMP-1","volume":"114","author":"Arjomandi","year":"2016","journal-title":"Eur J Med Chem"},{"key":"2020101416050804400_dkaa242-B67","doi-asserted-by":"crossref","first-page":"1084","DOI":"10.1038\/nchem.2110","article-title":"Rhodanine hydrolysis leads to potent thioenolate mediated metallo-\u03b2-lactamase inhibition","volume":"6","author":"Brem","year":"2014","journal-title":"Nat Chem"},{"key":"2020101416050804400_dkaa242-B68","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":"2020101416050804400_dkaa242-B69","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1021\/ml500534c","article-title":"Azolylthioacetamide: a highly promising scaffold for the development of metallo-\u03b2-lactamase inhibitors","volume":"6","author":"Yang","year":"2015","journal-title":"ACS Med Chem Lett"}],"container-title":["Journal of Antimicrobial Chemotherapy"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/academic.oup.com\/jac\/article-pdf\/75\/10\/2843\/33885386\/dkaa242.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"http:\/\/academic.oup.com\/jac\/article-pdf\/75\/10\/2843\/33885386\/dkaa242.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,10,14]],"date-time":"2020-10-14T20:06:29Z","timestamp":1602705989000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/jac\/article\/75\/10\/2843\/5863537"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,6,26]]},"references-count":69,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2020,6,26]]},"published-print":{"date-parts":[[2020,10,1]]}},"URL":"https:\/\/doi.org\/10.1093\/jac\/dkaa242","relation":{},"ISSN":["0305-7453","1460-2091"],"issn-type":[{"value":"0305-7453","type":"print"},{"value":"1460-2091","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2020,10]]},"published":{"date-parts":[[2020,6,26]]}}}