{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,25]],"date-time":"2026-08-25T18:02:40Z","timestamp":1787680960652,"version":"build-2784847793"},"reference-count":68,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,6,1]],"date-time":"2026-06-01T00:00:00Z","timestamp":1780272000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,6,1]],"date-time":"2026-06-01T00:00:00Z","timestamp":1780272000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,2,25]],"date-time":"2026-02-25T00:00:00Z","timestamp":1771977600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100005969","name":"Alma Mater Studiorum University of Bologna","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100005969","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100024370","name":"Ministero dell'Istruzione dell'Universita e della Ricerca","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100024370","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Inorganic Biochemistry"],"published-print":{"date-parts":[[2026,6]]},"DOI":"10.1016\/j.jinorgbio.2026.113272","type":"journal-article","created":{"date-parts":[[2026,2,21]],"date-time":"2026-02-21T07:15:45Z","timestamp":1771658145000},"page":"113272","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"special_numbering":"C","title":["Structure-activity studies reveal efficient inactivation of urease by Ebsulfur-based compounds"],"prefix":"10.1016","volume":"279","author":[{"given":"Luca","family":"Mazzei","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arundhati","family":"Paul","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michele","family":"Cianci","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrea","family":"Pizzi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Giuseppe","family":"Resnati","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefano","family":"Ciurli","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jinorgbio.2026.113272_bb0005","doi-asserted-by":"crossref","unstructured":"C.J.L. Murray, K.S. Ikuta, F. Sharara, L. Swetschinski, G. Robles Aguilar, A. Gray, C. Han, C. Bisignano, P. Rao, E. Wool, et al. Global burden of bacterial antimicrobial resistance in 2019: a systematic analysis, Lancet (2022), 399 (10325), 629\u2013655. doi:https:\/\/doi.org\/10.1016\/S0140-6736(21)02724-0.","DOI":"10.1016\/S0140-6736(21)02724-0"},{"issue":"10369","key":"10.1016\/j.jinorgbio.2026.113272_bb0010","doi-asserted-by":"crossref","first-page":"2221","DOI":"10.1016\/S0140-6736(22)02185-7","article-title":"Global mortality associated with 33 bacterial pathogens in 2019: a systematic analysis for the global burden of disease study 2019","volume":"400","author":"Ikuta","year":"2022","journal-title":"Lancet"},{"issue":"10442","key":"10.1016\/j.jinorgbio.2026.113272_bb0015","doi-asserted-by":"crossref","first-page":"2426","DOI":"10.1016\/S0140-6736(24)00876-6","article-title":"The scope of the antimicrobial resistance challenge","volume":"403","author":"Okeke","year":"2024","journal-title":"Lancet"},{"key":"10.1016\/j.jinorgbio.2026.113272_bb0020","author":"WHO"},{"key":"10.1016\/j.jinorgbio.2026.113272_bb0025","author":"WHO"},{"key":"10.1016\/j.jinorgbio.2026.113272_bb0030","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1128\/mr.51.1.22-42.1987","article-title":"Nickel utilization by microorganisms","volume":"51","author":"Hausinger","year":"1987","journal-title":"Microbiol. Rev."},{"key":"10.1016\/j.jinorgbio.2026.113272_bb0035","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1128\/mr.53.1.85-108.1989","article-title":"Microbial ureases: significance, regulation, and molecular characterization","volume":"53","author":"Mobley","year":"1989","journal-title":"Microbiol. Rev."},{"key":"10.1016\/j.jinorgbio.2026.113272_bb0040","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1128\/mr.59.3.451-480.1995","article-title":"Molecular biology of microbial ureases","volume":"59","author":"Mobley","year":"1995","journal-title":"Microbiol. Rev."},{"key":"10.1016\/j.jinorgbio.2026.113272_bb0045","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1016\/S0010-8545(99)00093-4","article-title":"Structural properties of the nickel ions in urease: novel insights into the catalytic and inhibition mechanisms","volume":"190-192","author":"Ciurli","year":"1999","journal-title":"Coord. Chem. Rev."},{"key":"10.1016\/j.jinorgbio.2026.113272_bb0050","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1021\/ar200041k","article-title":"Chemistry of Ni2+ in urease: sensing, trafficking, and catalysis","volume":"44","author":"Zambelli","year":"2011","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.jinorgbio.2026.113272_bb0055","doi-asserted-by":"crossref","first-page":"4206","DOI":"10.1021\/cr4004488","article-title":"Nonredox nickel enzymes","volume":"114","author":"Maroney","year":"2014","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jinorgbio.2026.113272_bb0060","series-title":"The Biological Chemistry of Nickel, Metallobiology","first-page":"60","article-title":"Urease","volume":"Vol. 10","author":"Mazzei","year":"2017"},{"key":"10.1016\/j.jinorgbio.2026.113272_bb0065","series-title":"Encyclopedia of Inorganic and Bioinorganic Chemistry","first-page":"1","article-title":"Urease","author":"Mazzei","year":"2021"},{"key":"10.1016\/j.jinorgbio.2026.113272_bb0070","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1004062","article-title":"The emerging role of urease as a general microbial virulence factor","volume":"10","author":"Rutherford","year":"2014","journal-title":"PLoS Pathog."},{"issue":"12","key":"10.1016\/j.jinorgbio.2026.113272_bb0075","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1004472","article-title":"Microbial urease in health and disease","volume":"10","author":"Mora","year":"2014","journal-title":"PLoS Pathog."},{"issue":"4","key":"10.1016\/j.jinorgbio.2026.113272_bb0080","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1128\/CMR.00006-06","article-title":"Helicobacter pylori persistence: an overview of interactions between H. pylori and host immune defenses","volume":"19","author":"Algood Holly","year":"2006","journal-title":"Clin. Microbiol. Rev."},{"key":"10.1016\/j.jinorgbio.2026.113272_bb0085","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/j.jare.2018.05.003","article-title":"A review on the development of urease inhibitors as antimicrobial agents against pathogenic bacteria","volume":"13","author":"Rego","year":"2018","journal-title":"J. Adv. Res."},{"key":"10.1016\/j.jinorgbio.2026.113272_bb0090","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1465-0691.2004.1004.x","article-title":"The need for new antibiotics","volume":"10","author":"Livermore","year":"2004","journal-title":"Clin. Microbiol. Infect."},{"issue":"10","key":"10.1016\/j.jinorgbio.2026.113272_bb0095","doi-asserted-by":"crossref","first-page":"726","DOI":"10.1038\/s41570-021-00313-1","article-title":"Towards the sustainable discovery and development of new antibiotics","volume":"5","author":"Miethke","year":"2021","journal-title":"Nat. Rev. Chem."},{"issue":"10","key":"10.1016\/j.jinorgbio.2026.113272_bb0100","doi-asserted-by":"crossref","first-page":"4910","DOI":"10.7150\/thno.56205","article-title":"Drug repurposing for next-generation combination therapies against multidrug-resistant bacteria","volume":"11","author":"Liu","year":"2021","journal-title":"Theranostics"},{"issue":"8","key":"10.1016\/j.jinorgbio.2026.113272_bb0105","doi-asserted-by":"crossref","first-page":"1388","DOI":"10.1128\/AAC.33.8.1388","article-title":"Susceptibility of methicillin-resistant Staphylococcus aureus to the selenium-containing compound 2-phenyl-1,2-benzoisoselenazol-3(2H)-one (PZ51)","volume":"33","author":"Nozawa","year":"1989","journal-title":"Antimicrob. Agents Chemother."},{"issue":"28","key":"10.1016\/j.jinorgbio.2026.113272_bb0110","doi-asserted-by":"crossref","first-page":"4106","DOI":"10.2174\/1381612821666150506154434","article-title":"Repurposing non-antimicrobial drugs and clinical molecules to treat bacterial infections","volume":"21","author":"Waleed","year":"2015","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/j.jinorgbio.2026.113272_bb0115","series-title":"New Frontiers in Organoselenium Compounds","first-page":"99","article-title":"Bioactive organoselenium compounds and therapeutic perspectives","author":"Lenard\u00e3o","year":"2018"},{"issue":"17","key":"10.1016\/j.jinorgbio.2026.113272_bb0120","doi-asserted-by":"crossref","first-page":"8125","DOI":"10.1021\/acs.jmedchem.6b00986","article-title":"1,2-Benzisoselenazol-3(2H)-one derivatives as a new class of bacterial urease inhibitors","volume":"59","author":"Macegoniuk","year":"2016","journal-title":"J. Med. Chem."},{"issue":"3","key":"10.1016\/j.jinorgbio.2026.113272_bb0125","doi-asserted-by":"crossref","first-page":"2054","DOI":"10.1021\/acs.jmedchem.2c01799","article-title":"Optimized Ebselen-based inhibitors of bacterial ureases with nontypical mode of action","volume":"66","author":"Macegoniuk","year":"2023","journal-title":"J. Med. Chem."},{"issue":"4","key":"10.1016\/j.jinorgbio.2026.113272_bb0130","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1021\/acsmedchemlett.5c00057","article-title":"Halogenated N-Benzylbenzisoselenazolones efficiently inhibit Helicobacter pylori ureolysis in vitro","volume":"16","author":"Grabarek","year":"2025","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.jinorgbio.2026.113272_bb0135","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF chimera - a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J. Comput. Chem."},{"issue":"4","key":"10.1016\/j.jinorgbio.2026.113272_bb0140","doi-asserted-by":"crossref","first-page":"1179","DOI":"10.1007\/s00204-021-03003-5","article-title":"Toxicology and pharmacology of synthetic organoselenium compounds: an update","volume":"95","author":"Nogueira","year":"2021","journal-title":"Arch. Toxicol."},{"issue":"9","key":"10.1016\/j.jinorgbio.2026.113272_bb0145","doi-asserted-by":"crossref","first-page":"1248","DOI":"10.1016\/j.bcp.2013.08.028","article-title":"The early research and development of ebselen","volume":"86","author":"Parnham","year":"2013","journal-title":"Biochem. Pharmacol."},{"issue":"8","key":"10.1016\/j.jinorgbio.2026.113272_bb0150","doi-asserted-by":"crossref","first-page":"4865","DOI":"10.1007\/s11033-014-3417-x","article-title":"Ebselen, a promising antioxidant drug: mechanisms of action and targets of biological pathways","volume":"41","author":"Azad","year":"2014","journal-title":"Mol. Biol. Rep."},{"issue":"12","key":"10.1016\/j.jinorgbio.2026.113272_bb0155","doi-asserted-by":"crossref","first-page":"6255","DOI":"10.1021\/cr0406559","article-title":"Organoselenium and organotellurium compounds: toxicology and pharmacology","volume":"104","author":"Nogueira","year":"2004","journal-title":"Chem. Rev."},{"issue":"11","key":"10.1016\/j.jinorgbio.2026.113272_bb0160","doi-asserted-by":"crossref","first-page":"1313","DOI":"10.1007\/s00204-011-0720-3","article-title":"Toxicology and pharmacology of selenium: emphasis on synthetic organoselenium compounds","volume":"85","author":"Nogueira","year":"2011","journal-title":"Arch. Toxicol."},{"issue":"10","key":"10.1016\/j.jinorgbio.2026.113272_bb0165","doi-asserted-by":"crossref","first-page":"1643","DOI":"10.1016\/S0006-2952(03)00114-X","article-title":"Dual effect of ebselen on mitochondrial permeability transition","volume":"65","author":"Morin","year":"2003","journal-title":"Biochem. Pharmacol."},{"issue":"6","key":"10.1016\/j.jinorgbio.2026.113272_bb0170","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1179\/135100000101535924","article-title":"Effect of ebselen on Ca2+ transport in mitochondria","volume":"5","author":"Gogvadze","year":"2000","journal-title":"Redox Rep."},{"issue":"2","key":"10.1016\/j.jinorgbio.2026.113272_bb0175","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1006\/abbi.2000.1939","article-title":"Intracellular thiol depletion causes mitochondrial permeability transition in ebselen-induced apoptosis","volume":"380","author":"Yang","year":"2000","journal-title":"Arch. Biochem. Biophys."},{"issue":"2","key":"10.1016\/j.jinorgbio.2026.113272_bb0180","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1093\/mutage\/gem048","article-title":"Antioxidant and anti-mutagenic effects of ebselen in yeast and in cultured mammalian V79 cells","volume":"23","author":"Miorelli","year":"2008","journal-title":"Mutagenesis"},{"issue":"2","key":"10.1016\/j.jinorgbio.2026.113272_bb0185","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1016\/j.bcp.2011.10.011","article-title":"Multifunctional Ebselen drug functions through the activation of DNA damage response and alterations in nuclear proteins","volume":"83","author":"Azad","year":"2012","journal-title":"Biochem. Pharmacol."},{"issue":"3","key":"10.1016\/j.jinorgbio.2026.113272_bb0190","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/j.jinorgbio.2008.12.007","article-title":"Mechanisms of inhibition of zinc-finger transcription factors by selenium compounds ebselen and selenite","volume":"103","author":"Larabee","year":"2009","journal-title":"J. Inorg. Biochem."},{"issue":"2","key":"10.1016\/j.jinorgbio.2026.113272_bb0195","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1006\/abbi.1999.1574","article-title":"Ebselen induces apoptosis in HepG2 cells through rapid depletion of intracellular thiols","volume":"374","author":"Yang","year":"2000","journal-title":"Arch. Biochem. Biophys."},{"issue":"2","key":"10.1016\/j.jinorgbio.2026.113272_bb0200","first-page":"299","article-title":"Bimodal actions of selenium essential for antioxidant and toxic pro-oxidant activities: the selenium paradox (review)","volume":"5","author":"Lee","year":"2012","journal-title":"Mol. Med. Rep."},{"key":"10.1016\/j.jinorgbio.2026.113272_bb0205","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1016\/j.ejca.2021.07.013","article-title":"Selenium stimulates the antitumour immunity: insights to future research","volume":"155","author":"Razaghi","year":"2021","journal-title":"Eur. J. Cancer"},{"issue":"7","key":"10.1016\/j.jinorgbio.2026.113272_bb0210","first-page":"170","article-title":"Selenium: the cancer shield","volume":"12","author":"Uysal","year":"2024","journal-title":"J. Biosci. Med."},{"key":"10.1016\/j.jinorgbio.2026.113272_bb0215","doi-asserted-by":"crossref","first-page":"407","DOI":"10.3389\/fonc.2018.00407","article-title":"Methylseleninic acid sensitizes ovarian cancer cells to T-cell mediated killing by decreasing PDL1 and VEGF levels","volume":"8","author":"Nair","year":"2018","journal-title":"Front. Oncol."},{"issue":"3","key":"10.1016\/j.jinorgbio.2026.113272_bb0220","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1007\/BF01972806","article-title":"Structure-activity relationships of a series of anti-inflammatory benzisoselenazolones (BISAs)","volume":"27","author":"Parnham","year":"1989","journal-title":"Agents Actions"},{"issue":"24","key":"10.1016\/j.jinorgbio.2026.113272_bb0225","doi-asserted-by":"crossref","first-page":"6298","DOI":"10.1016\/j.bmc.2016.03.060","article-title":"Development of ebsulfur analogues as potent antibacterials against methicillin-resistant Staphylococcus aureus","volume":"24","author":"Ngo","year":"2016","journal-title":"Bioorg. Med. Chem."},{"issue":"13","key":"10.1016\/j.jinorgbio.2026.113272_bb0230","doi-asserted-by":"crossref","first-page":"1745","DOI":"10.1016\/j.tet.2017.02.025","article-title":"Synthesis and anti-bacterial activity of a library of 1,2-benzisothiazol-3(2H)-one (BIT) derivatives amenable of crosslinking to polysaccharides","volume":"73","author":"Viani","year":"2017","journal-title":"Tetrahedron"},{"key":"10.1016\/j.jinorgbio.2026.113272_bb0235","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1016\/j.jinorgbio.2015.11.003","article-title":"Kinetic and structural studies reveal a unique binding mode of sulfite to the nickel center in urease","volume":"154","author":"Mazzei","year":"2016","journal-title":"J. Inorg. Biochem."},{"issue":"4","key":"10.1016\/j.jinorgbio.2026.113272_bb0240","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1007\/s007750050231","article-title":"The complex of Bacillus pasteurii urease with b-mercaptoethanol from X-ray data at 1.65 \u00c5 resolution","volume":"3","author":"Benini","year":"1998","journal-title":"J. Biol. Inorg. Chem."},{"issue":"13","key":"10.1016\/j.jinorgbio.2026.113272_bb0245","doi-asserted-by":"crossref","first-page":"5455","DOI":"10.1039\/C6DT00652C","article-title":"Inactivation of urease by 1,4-benzoquinone: chemistry at the protein surface","volume":"45","author":"Mazzei","year":"2016","journal-title":"Dalton Trans."},{"issue":"5","key":"10.1016\/j.jinorgbio.2026.113272_bb0250","doi-asserted-by":"crossref","first-page":"1984","DOI":"10.1021\/bi00833a031","article-title":"Jack bean urease (EC 3.5.1.5). A new purification and reliable rate assay","volume":"8","author":"Blakeley","year":"1969","journal-title":"Biochemistry"},{"issue":"6","key":"10.1016\/j.jinorgbio.2026.113272_bb0255","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1016\/0038-0717(96)00017-X","article-title":"Bacillus pasteurii urease: a heteropolymeric enzyme with a binuclear nickel active site","volume":"28","author":"Benini","year":"1996","journal-title":"Soil Biol. Biochem."},{"issue":"1\u20133","key":"10.1016\/j.jinorgbio.2026.113272_bb0260","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.molcatb.2009.01.003","article-title":"Ureases I. Functional, catalytic and kinetic properties: a review","volume":"59","author":"Krajewska","year":"2009","journal-title":"J. Mol. Catal. B Enzym."},{"issue":"1","key":"10.1016\/j.jinorgbio.2026.113272_bb0265","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1107\/S1600577516016465","article-title":"P13, the EMBL macromolecular crystallography beamline at the low-emittance PETRA III ring for high- and low-energy phasing with variable beam focusing","volume":"24","author":"Cianci","year":"2017","journal-title":"J. Synchrotron Radiat."},{"issue":"Pt 2","key":"10.1016\/j.jinorgbio.2026.113272_bb0270","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"Xds","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"issue":"Pt 1","key":"10.1016\/j.jinorgbio.2026.113272_bb0275","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1107\/S0907444905036693","article-title":"Scaling and assessment of data quality","volume":"62","author":"Evans","year":"2006","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"issue":"Pt 4","key":"10.1016\/j.jinorgbio.2026.113272_bb0280","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1107\/S090744491003982X","article-title":"An introduction to data reduction: space-group determination, scaling and intensity statistics","volume":"67","author":"Evans","year":"2011","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jinorgbio.2026.113272_bb0285","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1016\/j.jinorgbio.2016.11.016","article-title":"Inactivation of urease by catechol: kinetics and structure","volume":"166","author":"Mazzei","year":"2017","journal-title":"J. Inorg. Biochem."},{"issue":"Pt 5","key":"10.1016\/j.jinorgbio.2026.113272_bb0290","first-page":"760","article-title":"The CCP4 suite: programs for protein crystallography","volume":"50","year":"1994","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"issue":"Pt 3","key":"10.1016\/j.jinorgbio.2026.113272_bb0295","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1107\/S0907444996012255","article-title":"Refinement of macromolecular structures by the maximum-likelihood method","volume":"53","author":"Murshudov","year":"1997","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"issue":"Pt 4","key":"10.1016\/j.jinorgbio.2026.113272_bb0300","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"issue":"Pt 12","key":"10.1016\/j.jinorgbio.2026.113272_bb0305","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"issue":"64","key":"10.1016\/j.jinorgbio.2026.113272_bb0310","doi-asserted-by":"crossref","DOI":"10.1002\/chem.202201770","article-title":"Inhibition of urease by hydroquinones: a structural and kinetic study","volume":"28","author":"Mazzei","year":"2022","journal-title":"Chem. Eur. J."},{"key":"10.1016\/j.jinorgbio.2026.113272_bb0315","doi-asserted-by":"crossref","DOI":"10.1016\/j.jinorgbio.2023.112398","article-title":"Kinetic and structural details of urease inactivation by thiuram disulphides","volume":"250","author":"Mazzei","year":"2024","journal-title":"J. Inorg. Biochem."},{"issue":"3","key":"10.1016\/j.jinorgbio.2026.113272_bb0320","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1007\/s00775-013-0983-7","article-title":"The crystal structure of Sporosarcina pasteurii urease in a complex with citrate provides new hints for inhibitor design","volume":"18","author":"Benini","year":"2013","journal-title":"J. Biol. Inorg. Chem."},{"issue":"1","key":"10.1016\/j.jinorgbio.2026.113272_bb0325","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-021-23313-7","article-title":"Inhibition mechanism of SARS-CoV-2 main protease by ebselen and its derivatives","volume":"12","author":"Amporndanai","year":"2021","journal-title":"Nat. Commun."},{"issue":"22","key":"10.1016\/j.jinorgbio.2026.113272_bib336","doi-asserted-by":"crossref","first-page":"7415","DOI":"10.1002\/anie.201903565","article-title":"The structure of the elusive urease-urea complex unveils the mechanism of a paradigmatic nickel-dependent enzyme","volume":"58","author":"L. Mazzei","year":"2019","journal-title":"Angew Chem Int, Engl"},{"issue":"10","key":"10.1016\/j.jinorgbio.2026.113272_bb0330","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1515\/BC.2007.138","article-title":"Selenium in chemistry and biochemistry in comparison to sulfur","volume":"388","author":"Wessjohann","year":"2007","journal-title":"Biol. Chem."},{"key":"10.1016\/j.jinorgbio.2026.113272_bb0335","series-title":"Handbook of Chemistry and Physics","year":"2016"}],"container-title":["Journal of Inorganic Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0162013426000619?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0162013426000619?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,17]],"date-time":"2026-05-17T08:28:59Z","timestamp":1779006539000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0162013426000619"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,6]]},"references-count":68,"alternative-id":["S0162013426000619"],"URL":"https:\/\/doi.org\/10.1016\/j.jinorgbio.2026.113272","relation":{},"ISSN":["0162-0134"],"issn-type":[{"value":"0162-0134","type":"print"}],"subject":[],"published":{"date-parts":[[2026,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structure-activity studies reveal efficient inactivation of urease by Ebsulfur-based compounds","name":"articletitle","label":"Article Title"},{"value":"Journal of Inorganic Biochemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jinorgbio.2026.113272","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Crown Copyright \u00a9 2026 Published by Elsevier Inc.","name":"copyright","label":"Copyright"}],"article-number":"113272"}}