{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,23]],"date-time":"2026-04-23T01:35:05Z","timestamp":1776908105805,"version":"3.51.2"},"reference-count":64,"publisher":"FapUNIFESP (SciELO)","license":[{"start":{"date-parts":[[2022,1,1]],"date-time":"2022-01-01T00:00:00Z","timestamp":1640995200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2022,1,1]],"date-time":"2022-01-01T00:00:00Z","timestamp":1640995200000},"content-version":"am","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2022,1,1]],"date-time":"2022-01-01T00:00:00Z","timestamp":1640995200000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Mem. Inst. Oswaldo Cruz"],"DOI":"10.1590\/0074-02760220102","type":"journal-article","created":{"date-parts":[[2022,9,23]],"date-time":"2022-09-23T13:53:56Z","timestamp":1663941236000},"source":"Crossref","is-referenced-by-count":2,"title":["Analysis of a novel class A \u03b2-lactamase OKP-B-6 of Klebsiella quasipneumoniae: structural characterisation and interaction with commercially available drugs"],"prefix":"10.1590","volume":"117","author":[{"given":"Reinaldo","family":"Bellini","sequence":"first","affiliation":[{"name":"Laborat\u00f3rio Nacional de Computa\u00e7\u00e3o Cient\u00edfica,  Brasil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Isabella Alvim","family":"Guedes","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio Nacional de Computa\u00e7\u00e3o Cient\u00edfica,  Brasil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Luciane Prioli","family":"Ciapina","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio Nacional de Computa\u00e7\u00e3o Cient\u00edfica,  Brasil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ana Tereza Ribeiro","family":"de Vasconcelos","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio Nacional de Computa\u00e7\u00e3o Cient\u00edfica,  Brasil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8518-8062","authenticated-orcid":false,"given":"Laurent Emmanuel","family":"Dardenne","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio Nacional de Computa\u00e7\u00e3o Cient\u00edfica,  Brasil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5437-2737","authenticated-orcid":false,"given":"Marisa Fabiana","family":"Nicol\u00e1s","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio Nacional de Computa\u00e7\u00e3o Cient\u00edfica,  Brasil"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"530","published-online":{"date-parts":[[2022]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.drup.2017.11.002","article-title":"An update on \u00df-lactamase inhibitor discovery and development","volume":"36","author":"Docquier JD","year":"2018","journal-title":"Drug Resist Updat"},{"issue":"1036","key":"ref2","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1098\/rstb.1980.0049","article-title":"The structure of beta-lactamases","volume":"289","author":"Ambler RP","year":"1980","journal-title":"Philos Trans R Soc Lond B Biol Sci"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1146\/annurev.mi.45.100191.000345","article-title":"Serine beta-lactamases and penicillin-binding proteins","volume":"45","author":"Ghuysen JM","year":"1991","journal-title":"Annu Rev Microbiol"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/j.coph.2014.09.012","article-title":"Penicillin-binding proteins evergreen drug targets","volume":"18","author":"Fr\u00e8re JM","year":"2014","journal-title":"Curr Opin Pharmacol"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1080\/02648725.1994.10647912","article-title":"The structures and catalytic mechanisms of active-site serine beta-lactamases","volume":"12","author":"Lamotte-Brasseur J","year":"1994","journal-title":"Biotechnol Genet Eng Rev"},{"issue":"3","key":"ref6","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1128\/AAC.01009-09","article-title":"Updated functional classification of beta-lactamases","volume":"54","author":"Bush K","year":"2010","journal-title":"Antimicrob Agents Chemother"},{"issue":"19","key":"ref7","doi-asserted-by":"crossref","first-page":"5732","DOI":"10.1021\/bi700300u","article-title":"Crystal structure of KPC-2 insights into carbapenemase activity in class A beta-lactamases","volume":"46","author":"Ke W","year":"2007","journal-title":"Biochemistry"},{"issue":"4","key":"ref8","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1016\/S1473-3099(09)70054-4","article-title":"The real threat of Klebsiella pneumoniae carbapenemase-producing bacteria","volume":"9","author":"Nordmann P","year":"2009","journal-title":"Lancet Infect Dis"},{"issue":"4","key":"ref9","first-page":"e00290","article-title":"Whole-genome sequencing of human clinical Klebsiella pneumoniae isolates reveals misidentification and misunderstandings of Klebsiella pneumoniae, Klebsiella variicola, and","volume":"2","author":"Long SW","year":"2017","journal-title":"Klebsiella quasipneumoniae. mSphere"},{"key":"ref10","article-title":"\u00df-lactam\/\u00df-lactamase inhibitor combinations: an update","volume":"9","author":"Tehrani KHME","year":"2018","journal-title":"MedChemComm"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.jbiotec.2018.05.005","article-title":"Class A \u00df-lactamases and inhibitors In silico analysis of the binding mode and the relationship with resistance","volume":"279","author":"Pereira R","year":"2018","journal-title":"J Biotechnol"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"622","DOI":"10.3389\/fmicb.2018.00622","article-title":"Exploring additional dimensions of complexity in inhibitor design for serine \u00df-lactamases mechanistic and intra- and inter-molecular chemistry approaches","volume":"9","year":"2018","journal-title":"Front Microbiol"},{"issue":"4","key":"ref13","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1021\/bi035985m","article-title":"Tazobactam forms a stoichiometric trans-enamine intermediate in the E166A variant of SHV-1 beta-lactamase 1.63 A crystal structure","volume":"43","author":"Padayatti PS","year":"2004","journal-title":"Biochemistry"},{"issue":"44","key":"ref14","doi-asserted-by":"crossref","first-page":"14111","DOI":"10.1021\/bi0487903","article-title":"Inhibitor-resistant class A beta-lactamases consequences of the Ser130-to-Gly mutation seen in Apo and tazobactam structures of the SHV-1 variant","volume":"43","author":"Sun T","year":"2004","journal-title":"Biochemistry"},{"issue":"39","key":"ref15","doi-asserted-by":"crossref","first-page":"11895","DOI":"10.1021\/bi060990m","article-title":"Effect of the inhibitor-resistant M69V substitution on the structures and populations of trans-enamine \u00df-lactamase intermediates","volume":"45","author":"Totir MA","year":"2006","journal-title":"Biochemistry"},{"issue":"9","key":"ref16","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0136813","article-title":"Inhibition of Klebsiella \u00df-lactamases (SHV-1 and KPC-2) by avibactam a dtructural study","volume":"10","author":"Krishnan NP","year":"2015","journal-title":"PLoS One"},{"issue":"29","key":"ref17","doi-asserted-by":"crossref","first-page":"11663","DOI":"10.1073\/pnas.1205073109","article-title":"Avibactam is a covalent, reversible, non- -lactam -lactamase inhibitor","volume":"109","author":"Ehmann DE","year":"2012","journal-title":"Proc Natl Acad Sci"},{"issue":"4","key":"ref18","doi-asserted-by":"crossref","first-page":"e01936","DOI":"10.1128\/AAC.01936-19","article-title":"Potency of vaborbactam is less affected than that of avibactam in strains producing KPC-2 mutations that confer resistance to ceftazidime-avibactam","volume":"64","author":"Tsivkovski R","year":"2020","journal-title":"Antimicrob Agents Chemother"},{"issue":"8","key":"ref19","first-page":"a025247","article-title":"Cold Spring Harb Perspect","volume":"6","author":"Bush K","year":"2016","journal-title":"Med"},{"issue":"39","key":"ref20","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 \u00df-lactamases","volume":"288","author":"Ehmann DE","year":"2013","journal-title":"J Biol Chem"},{"issue":"1","key":"ref21","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1186\/1471-2164-15-54","article-title":"Comparative analysis of the complete genome of KPC-2-producing Klebsiella pneumoniae Kp13 reveals remarkable genome plasticity and a wide repertoire of virulence and resistance mechanisms","volume":"15","author":"Ramos PIP","year":"2014","journal-title":"BMC Genomics"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.plasmid.2018.08.001","article-title":"Evolution and typing of IncC plasmids contributing to antibiotic resistance in Gram-negative bacteria","volume":"99","author":"Ambrose SJ","year":"2018","journal-title":"Plasmid"},{"issue":"4","key":"ref23","article-title":"Rapid phenotypic evolution in multidrug-resistant Klebsiella pneumoniae hospital outbreak strains","volume":"5","author":"van Dorp L","year":"2019","journal-title":"Microb Genom"},{"issue":"7","key":"ref24","doi-asserted-by":"crossref","first-page":"2400","DOI":"10.1128\/AAC.48.7.2400-2408.2004","article-title":"Diversity and evolution of the class A chromosomal beta-lactamase gene in Klebsiella pneumoniae","volume":"48","author":"Haeggman S","year":"2004","journal-title":"Antimicrob Agents Chemother"},{"issue":"7","key":"ref25","doi-asserted-by":"crossref","first-page":"3097","DOI":"10.1128\/AAC.49.7.3097-3098.2005","article-title":"One new LEN enzyme and two new OKP enzymes in Klebsiella pneumoniae clinical isolates and proposed nomenclature for chromosomal \u00df-lactamases of this species","volume":"49","author":"Siebor E","year":"2005","journal-title":"Antimicrob Agents Chemother"},{"issue":"9","key":"ref26","doi-asserted-by":"crossref","first-page":"3146","DOI":"10.1099\/ijs.0.062737-0","article-title":"Description of Klebsiella quasipneumoniae sp nov., isolated from human infections, with two subspecies, Klebsiella quasipneumoniae subsp. quasipneumoniae subsp. nov. and Klebsiella quasipneumoniae subsp. similipneumoniae subsp. nov., and demonstration that Klebsiella singaporensis is a junior heterotypic synonym of Klebsiella variicola","volume":"64","author":"Brisse S","year":"2014","journal-title":"Int J Syst Evol Microbiol"},{"issue":"12","key":"ref27","doi-asserted-by":"crossref","first-page":"5149","DOI":"10.1128\/AAC.49.12.5149-5152.2005","article-title":"Variants of the Klebsiella pneumoniae OKP chromosomal beta-lactamase are divided into two main groups, OKP-A and OKP-B","volume":"49","author":"Fevre C","year":"2005","journal-title":"Antimicrob Agents Chemother"},{"issue":"1","key":"ref28","doi-asserted-by":"crossref","first-page":"29","DOI":"10.21149\/8156","article-title":"Klebsiella variicola and Klebsiella quasipneumoniae with capacity to adapt to clinical and plant settings","volume":"60","author":"Mart\u00ednez-Romero E","year":"2018","journal-title":"Salud Publica Mex"},{"issue":"1","key":"ref29","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1038\/s41598-018-36554-2","article-title":"Molecular characterization of carbapenem resistant Klebsiella pneumoniae and Klebsiella quasipneumoniae isolated from Lebanon","volume":"9","author":"Arabaghian H","year":"2019","journal-title":"Sci Rep"},{"issue":"6","key":"ref30","doi-asserted-by":"crossref","first-page":"e02513","DOI":"10.1128\/AAC.02513-18","article-title":"Klebsiella quasipneumoniae provides a window into carbapenemase gene transfer, plasmid rearrangements, and patient interactions with the hospital environment","volume":"63","author":"Mathers AJ","year":"2019","journal-title":"Antimicrob Agents Chemother"},{"issue":"11","key":"ref31","doi-asserted-by":"crossref","first-page":"3205","DOI":"10.1093\/jac\/dkz332","article-title":"Klebsiella pneumoniae and Klebsiella quasipneumoniae define the population structure of blaKPC-2Klebsiella a 5 year retrospective genomic study in Singapore","volume":"74","author":"Octavia S","year":"2019","journal-title":"J Antimicrob Chemother"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"220","DOI":"10.3389\/fmicb.2018.00220","article-title":"Comparative genomic analysis of a clinical isolate of Klebsiella quasipneumoniae subsp similipneumoniae, a KPC-2 and OKP-B-6 beta-lactamases producer harboring two drug-resistance plasmids from southeast Brazil","volume":"9","author":"Nicol\u00e1s MF","year":"2018","journal-title":"Front Microbiol"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1007\/978-3-030-18768-2_7","article-title":"Bacterial signal peptidases","volume":"92","author":"Paetzel M","year":"2019","journal-title":"Subcell Biochem"},{"issue":"W1","key":"ref34","doi-asserted-by":"crossref","first-page":"W296","DOI":"10.1093\/nar\/gky427","article-title":"SWISS-MODEL homology modelling of protein structures and complexes","volume":"46","author":"Waterhouse A","year":"2018","journal-title":"Nucleic Acids Res"},{"issue":"1","key":"ref35","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1002\/pro.3330","article-title":"MolProbity more and better reference data for improved all-atom structure validation","volume":"27","author":"Williams CJ","year":"2018","journal-title":"Protein Sci"},{"issue":"1","key":"ref36","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity all-atom structure validation for macromolecular crystallography","volume":"66","author":"Chen VB","year":"2010","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"issue":"2","key":"ref37","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1107\/S0021889892009944","article-title":"PROCHECK a program to check the stereochemical quality of protein structures","volume":"26","author":"Laskowski RA","year":"1993","journal-title":"J Appl Crystallogr"},{"issue":"4","key":"ref38","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1007\/BF00228148","article-title":"AQUA and PROCHECK-NMR programs for checking the quality of protein structures solved by NMR","volume":"8","author":"Laskowski RA","year":"1996","journal-title":"J Biomol NMR"},{"issue":"9","key":"ref39","doi-asserted-by":"crossref","first-page":"1511","DOI":"10.1002\/pro.5560020916","article-title":"Verification of protein structures patterns of nonbonded atomic interactions","volume":"2","author":"Colovos C","year":"1993","journal-title":"Protein Sci"},{"issue":"6","key":"ref40","doi-asserted-by":"crossref","first-page":"1861","DOI":"10.1021\/bi0022745","article-title":"Inhibition of the SHV-1 \u00df-lactamase by sulfones crystallographic observation of two reaction intermediates with tazobactam","volume":"40","author":"Kuzin AP","year":"2001","journal-title":"Biochemistry"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"W665","DOI":"10.1093\/nar\/gkh381","article-title":"PDB2PQR an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations","volume":"32","author":"Dolinsky TJ","year":"2004","journal-title":"Nucleic Acids Res"},{"key":"ref42"},{"issue":"15","key":"ref43","doi-asserted-by":"crossref","first-page":"2074","DOI":"10.1093\/bioinformatics\/bts310","article-title":"DoGSiteScorer a web server for automatic binding site prediction, analysis and druggability assessment","volume":"28","author":"Volkamer A","year":"2012","journal-title":"Bioinformatics"},{"issue":"2","key":"ref44","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1021\/ct100578z","article-title":"PROPKA3 consistent treatment of internal and surface residues in empirical pKa predictions","volume":"7","author":"Olsson MHM","year":"2011","journal-title":"J Chem Theory Comput"},{"issue":"11","key":"ref45","doi-asserted-by":"crossref","first-page":"5818","DOI":"10.1073\/pnas.1922203117","article-title":"Mechanism of proton transfer in class A \u00df-lactamase catalysis and inhibition by avibactam","volume":"117","author":"Pemberton OA","year":"2020","journal-title":"Proc Natl Acad Sci"},{"issue":"6","key":"ref46","doi-asserted-by":"crossref","first-page":"2496","DOI":"10.1128\/AAC.02247-12","article-title":"Structural insight into potent broad-spectrum inhibition with reversible recyclization mechanism avibactam in complex with CTX-M-15 and Pseudomonas aeruginosa AmpC \u00df-lactamases","volume":"57","author":"Lahiri SD","year":"2013","journal-title":"Antimicrob Agents Chemother"},{"issue":"31","key":"ref47","doi-asserted-by":"crossref","first-page":"5174","DOI":"10.1021\/bi500589x","article-title":"Inactivation of TEM-1 by avibactam (NXL-104) insights from quantum mechanics\/molecular mechanics metadynamics simulations","volume":"53","author":"Sgrignani J","year":"2014","journal-title":"Biochemistry"},{"key":"ref48","article-title":"PubChem in 2021: new data content and improved web interfaces","volume":"49","author":"Kim S","year":"2021","journal-title":"Nucleic Acids Res"},{"issue":"12","key":"ref49","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1007\/s10822-007-9133-z","article-title":"Epik a software program for pKa prediction and protonation state generation for drug-like molecules","volume":"21","author":"Shelley JC","year":"2007","journal-title":"J Comput Aided Mol Des"},{"issue":"3","key":"ref50","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1021\/bi501197t","article-title":"Detecting a quasi-stable imine species on the reaction pathway of SHV-1 \u00df-lactamase and 6\u00df-(hydroxymethyl)penicillanic acid sulfone","volume":"54","author":"Che T","year":"2015","journal-title":"Biochemistry"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fphar.2018.01089","article-title":"Empirical scoring functions for structure-based virtual screening applications, critical aspects, and challenges","volume":"9","author":"Guedes IA","year":"2018","journal-title":"Front Pharmacol"},{"issue":"1","key":"ref52","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1007\/s12551-013-0130-2","article-title":"Receptor-ligand molecular docking","volume":"6","author":"Guedes IA","year":"2014","journal-title":"Biophys Rev"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.jmgm.2014.11.002","article-title":"Structural modeling and docking studies of ribose 5-phosphate isomerase from Leishmania major and Homo sapiens a comparative analysis for Leishmaniasis treatment","volume":"55","author":"Capriles PVSZ","year":"2015","journal-title":"J Mol Graph Model"},{"issue":"1","key":"ref54","doi-asserted-by":"crossref","first-page":"5543","DOI":"10.1038\/s41598-021-84700-0","article-title":"Drug design and repurposing with DockThor-VS web server focusing on SARS-CoV-2 therapeutic targets and their non-synonym variants","volume":"11","author":"Guedes IA","year":"2021","journal-title":"Sci Rep"},{"issue":"2","key":"ref55","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1021\/acs.jcim.9b00905","article-title":"Highly flexible ligand docking benchmarking of the DockThor Program on the LEADS-PEP Protein-peptide Dataset","volume":"60","author":"dos Santos KB","year":"2020","journal-title":"J Chem Inf Model"},{"key":"ref56","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1016\/j.ins.2014.08.002","article-title":"A dynamic niching genetic algorithm strategy for docking highly flexible ligands","volume":"289","author":"de Magalh\u00e3es CS","year":"2014","journal-title":"Inf Sci"},{"issue":"40","key":"ref57","doi-asserted-by":"crossref","first-page":"16798","DOI":"10.1021\/ja3073676","article-title":"Crystal structure of a preacylation complex of the \u00df-lactamase inhibitor sulbactam bound to a sulfenamide bond-containing thiol-\u00df-lactamase","volume":"134","author":"Rodkey EA","year":"2012","journal-title":"J Am Chem Soc"},{"issue":"5-6","key":"ref58","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1002\/(SICI)1096-987X(199604)17:5\/6<490::AID-JCC1>3.0.CO;2-P","article-title":"Merck molecular force field I. Basis, form, scope, parameterization, and performance of MMFF94","volume":"17","author":"Halgren TA","year":"1996","journal-title":"J Comput Chem"},{"issue":"1","key":"ref59","doi-asserted-by":"crossref","first-page":"3198","DOI":"10.1038\/s41598-021-82410-1","article-title":"New machine learning and physics-based scoring functions for drug discovery","volume":"11","author":"Guedes IA","year":"2021","journal-title":"Sci Rep"},{"issue":"7","key":"ref60","doi-asserted-by":"crossref","first-page":"3700","DOI":"10.1128\/AAC.04405-14","article-title":"Avibactam and inhibitor-resistant SHV \u00df-lactamases","volume":"59","author":"Winkler ML","year":"2015","journal-title":"Antimicrob Agents Chemother"},{"issue":"3","key":"ref61","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1016\/S0969-2126(02)00725-6","article-title":"Structural milestones in the reaction pathway of an amide hydrolase substrate, acyl, and product complexes of cephalothin with AmpC beta-lactamase","volume":"10","author":"Beadle BM","year":"2002","journal-title":"Structure"},{"issue":"22","key":"ref62","doi-asserted-by":"crossref","first-page":"4551","DOI":"10.1021\/bi300508r","article-title":"NXL104 irreversibly inhibits the \u00df-lactamase from Mycobacterium tuberculosis","volume":"51","author":"Xu H","year":"2012","journal-title":"Biochemistry"},{"issue":"4","key":"ref63","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1021\/acsinfecdis.5b00007","article-title":"Molecular mechanism of avibactam-mediated \u00df-lactamase inhibition","volume":"1","author":"King DT","year":"2015","journal-title":"ACS Infect Dis"},{"issue":"6","key":"ref64","doi-asserted-by":"crossref","first-page":"1765","DOI":"10.1021\/acsinfecdis.1c00094","article-title":"In crystallo time-resolved interaction of the clostridioides difficile CDD-1 enzyme with avibactam provides new insights into the catalytic mechanism of class D \u00df-lactamases","volume":"7","author":"Stewart NK","year":"2021","journal-title":"ACS Infect Dis"}],"container-title":["Mem\u00f3rias do Instituto Oswaldo Cruz"],"original-title":[],"link":[{"URL":"http:\/\/www.scielo.br\/scielo.php?script=sci_pdf&pid=S0074-02762022000101124&tlng=en","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,9,23]],"date-time":"2022-09-23T13:55:05Z","timestamp":1663941305000},"score":1,"resource":{"primary":{"URL":"http:\/\/www.scielo.br\/scielo.php?script=sci_arttext&pid=S0074-02762022000101124&tlng=en"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022]]},"references-count":64,"alternative-id":["S0074-02762022000101124"],"URL":"https:\/\/doi.org\/10.1590\/0074-02760220102","relation":{},"ISSN":["1678-8060","0074-0276"],"issn-type":[{"value":"1678-8060","type":"electronic"},{"value":"0074-0276","type":"print"}],"subject":[],"published":{"date-parts":[[2022]]},"article-number":"e220102"}}