{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T16:44:10Z","timestamp":1790613850095,"version":"4.1.0"},"reference-count":44,"publisher":"Elsevier BV","issue":"16","license":[{"start":{"date-parts":[[2020,8,1]],"date-time":"2020-08-01T00:00:00Z","timestamp":1596240000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,8,1]],"date-time":"2020-08-01T00:00:00Z","timestamp":1596240000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100004035","name":"Jordan University of Science and Technology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004035","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Bioorganic & Medicinal Chemistry"],"published-print":{"date-parts":[[2020,8]]},"DOI":"10.1016\/j.bmc.2020.115608","type":"journal-article","created":{"date-parts":[[2020,7,4]],"date-time":"2020-07-04T11:14:35Z","timestamp":1593861275000},"page":"115608","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":18,"title":["Design, synthesis and biological evaluation of novel glyoxalase I inhibitors possessing diazenylbenzenesulfonamide moiety as potential anticancer agents"],"prefix":"10.1016","volume":"28","author":[{"given":"Buthina A.","family":"Al-Oudat","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hana'a M.","family":"Jaradat","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Qosay A.","family":"Al\u2011Balas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nizar A.","family":"Al-Shar'i","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amanda","family":"Bryant-Friedrich","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mel F.","family":"Bedi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"1","key":"10.1016\/j.bmc.2020.115608_b0005","first-page":"9","article-title":"Cancer statistics","volume":"64","author":"Siegel","year":"2014","journal-title":"CA: Cancer J Clinicians"},{"issue":"8","key":"10.1016\/j.bmc.2020.115608_b0010","doi-asserted-by":"crossref","first-page":"3500","DOI":"10.1158\/0008-5472.CAN-06-4626","article-title":"Cancer immunologists and cancer biologists: why we didn't talk then but need to now","volume":"67","author":"Prendergast","year":"2007","journal-title":"Cancer Res"},{"issue":"5","key":"10.1016\/j.bmc.2020.115608_b0015","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1016\/0006-291X(69)90445-8","article-title":"Glyoxalase inhibitors as potential anticancer agents","volume":"35","author":"Vince","year":"1969","journal-title":"Biochem Biophys Res Commun"},{"issue":"1","key":"10.1016\/j.bmc.2020.115608_b0020","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1021\/jm00283a009","article-title":"Glyoxalase inhibitors. A possible approach to anticancer agents","volume":"14","author":"Vince","year":"1971","journal-title":"J Med Chem"},{"issue":"2","key":"10.1016\/j.bmc.2020.115608_b0025","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1016\/S0021-9258(18)56017-8","article-title":"The mechanism of action of glyoxalase","volume":"190","author":"Racker","year":"1951","journal-title":"J Biol Chem"},{"key":"10.1016\/j.bmc.2020.115608_b0030","series-title":"Functions of glutathione: Biochemical, physiological, toxicological and clinical aspects","author":"Chasseaud","year":"1983"},{"key":"10.1016\/j.bmc.2020.115608_b0035","first-page":"763","article-title":"The glyoxalase enigma. The biological consequences of a ubiquitous enzyme","volume":"14","author":"Carrington","year":"1986","journal-title":"IRCS Med Sci"},{"issue":"18","key":"10.1016\/j.bmc.2020.115608_b0040","doi-asserted-by":"crossref","first-page":"4581","DOI":"10.1021\/bi00232a031","article-title":"Kinetic parameters for the elimination reaction catalyzed by triosephosphate isomerase and an estimation of the reaction's physiological significance","volume":"30","author":"Richard","year":"1991","journal-title":"Biochemistry"},{"issue":"7","key":"10.1016\/j.bmc.2020.115608_b0045","first-page":"1139","article-title":"Chemical modification of proteins by methylglyoxal","volume":"44","author":"Degenhardt","year":"1998","journal-title":"Cell Mol Biol (Noisy-le-Grand, France)"},{"issue":"7","key":"10.1016\/j.bmc.2020.115608_b0050","doi-asserted-by":"crossref","first-page":"16R","DOI":"10.1093\/glycob\/cwi053","article-title":"Advanced glycation end products and RAGE: a common thread in aging, diabetes, neurodegeneration, and inflammation","volume":"15","author":"Ramasamy","year":"2005","journal-title":"Glycobiology"},{"issue":"2","key":"10.1016\/j.bmc.2020.115608_b0055","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1042\/bj3240565","article-title":"N\u03b5-(carboxyethyl) lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins","volume":"324","author":"Ahmed","year":"1997","journal-title":"Biochem J"},{"issue":"1","key":"10.1016\/j.bmc.2020.115608_b0060","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/0005-2787(68)90290-6","article-title":"Reactions of glyoxal with nucleic acids, nucleotides and their component bases","volume":"161","author":"Nakaya","year":"1968","journal-title":"Biochim Biophys Acta (BBA)-Nucl Acids Protein Synth"},{"issue":"1","key":"10.1016\/j.bmc.2020.115608_b0065","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/bj2690001","article-title":"The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life","volume":"269","author":"Thornalley","year":"1990","journal-title":"Biochem J"},{"issue":"1","key":"10.1016\/j.bmc.2020.115608_b0070","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/BJ20121743","article-title":"The glyoxalase pathway: the first hundred years\u2026 and beyond","volume":"453","author":"Sousa Silva","year":"2013","journal-title":"Biochem J"},{"key":"10.1016\/j.bmc.2020.115608_b0075","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/S0009-2797(97)00157-9","article-title":"Glutathione-dependent detoxification of \u03b1-oxoaldehydes by the glyoxalase system: involvement in disease mechanisms and antiproliferative activity of glyoxalase I inhibitors","volume":"111","author":"Thornalley","year":"1998","journal-title":"Chem Biol Interact"},{"issue":"1","key":"10.1016\/j.bmc.2020.115608_b0080","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1023\/A:1010632919129","article-title":"Expression of glyoxalase I and II in normal and breast cancer tissues","volume":"66","author":"Rulli","year":"2001","journal-title":"Breast Cancer Res Treat"},{"issue":"3","key":"10.1016\/j.bmc.2020.115608_b0085","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1097\/00130404-200605000-00011","article-title":"Overexpression of glyoxalase system enzymes in human kidney tumor","volume":"12","author":"Antognelli","year":"2006","journal-title":"Cancer J"},{"issue":"14","key":"10.1016\/j.bmc.2020.115608_b0090","doi-asserted-by":"crossref","first-page":"1946","DOI":"10.1016\/S0959-8049(02)00236-8","article-title":"Differing expression of enzymes of the glyoxalase system in superficial and invasive bladder carcinomas","volume":"38","author":"Mearini","year":"2002","journal-title":"Eur J Cancer"},{"issue":"10","key":"10.1016\/j.bmc.2020.115608_b0095","doi-asserted-by":"crossref","first-page":"3214","DOI":"10.1182\/blood.V95.10.3214","article-title":"Glyoxalase I is involved in resistance of human leukemia cells to antitumor agent-induced apoptosis","volume":"95","author":"Sakamoto","year":"2000","journal-title":"Blood"},{"issue":"12","key":"10.1016\/j.bmc.2020.115608_b0100","doi-asserted-by":"crossref","first-page":"2357","DOI":"10.1016\/0006-2952(92)90680-H","article-title":"Inhibition of proliferation of human leukaemia 60 cells by diethyl esters of glyoxalase inhibitors in vitro","volume":"44","author":"Lo","year":"1992","journal-title":"Biochem Pharmacol"},{"issue":"6","key":"10.1016\/j.bmc.2020.115608_b0105","doi-asserted-by":"crossref","first-page":"1343","DOI":"10.1042\/bst0311343","article-title":"Glyoxalase I\u2013structure, function and a critical role in the enzymatic defence against glycation","volume":"31","author":"Thornalley","year":"2003","journal-title":"Biochem Soc Trans"},{"issue":"12","key":"10.1016\/j.bmc.2020.115608_b0110","doi-asserted-by":"crossref","first-page":"13740","DOI":"10.3390\/molecules171213740","article-title":"Generation of the first structure-based pharmacophore model containing a selective \u201czinc binding group\u201d feature to identify potential glyoxalase-1 inhibitors","volume":"17","author":"Al-Balas","year":"2012","journal-title":"Molecules"},{"issue":"4","key":"10.1016\/j.bmc.2020.115608_b0115","doi-asserted-by":"crossref","first-page":"281","DOI":"10.2174\/1389557518666181009141231","article-title":"Recent advances in glyoxalase-I inhibition","volume":"19","author":"Al-Balas","year":"2019","journal-title":"Mini Rev Med Chem"},{"issue":"5","key":"10.1016\/j.bmc.2020.115608_b0120","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1021\/jm00287a006","article-title":"Inhibition of glyoxalase I by S-substituted glutathiones","volume":"14","author":"Vince","year":"1971","journal-title":"J Med Chem"},{"issue":"35","key":"10.1016\/j.bmc.2020.115608_b0125","doi-asserted-by":"crossref","first-page":"24933","DOI":"10.1016\/S0021-9258(19)73986-6","article-title":"Inhibition of glyoxalase I by the enediol mimic S-(N-hydroxy-N-methylcarbamoyl) glutathione. The possible basis of a tumor-selective anticancer strategy","volume":"267","author":"Hamilton","year":"1992","journal-title":"J Biol Chem"},{"issue":"14","key":"10.1016\/j.bmc.2020.115608_b0130","doi-asserted-by":"crossref","first-page":"2161","DOI":"10.1021\/jm00040a007","article-title":"S-(N-aryl-N-hydroxycarbamoyl) glutathione derivatives are tight-binding inhibitors of glyoxalase I and slow substrates for glyoxalase II","volume":"37","author":"Murthy","year":"1994","journal-title":"J Med Chem"},{"issue":"1\u20132","key":"10.1016\/j.bmc.2020.115608_b0135","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/j.bpc.2009.12.007","article-title":"Binding of curcumin with glyoxalase I: Molecular docking, molecular dynamics simulations, and kinetics analysis","volume":"147","author":"Liu","year":"2010","journal-title":"Biophys Chem"},{"issue":"3","key":"10.1016\/j.bmc.2020.115608_b0140","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.1016\/j.bmc.2010.12.039","article-title":"Identification of curcumin derivatives as human glyoxalase I inhibitors: a combination of biological evaluation, molecular docking, 3D-QSAR and molecular dynamics simulation studies","volume":"19","author":"Yuan","year":"2011","journal-title":"Bioorg Med Chem"},{"key":"10.1016\/j.bmc.2020.115608_b0145","doi-asserted-by":"crossref","first-page":"2623","DOI":"10.2147\/DDDT.S110997","article-title":"Novel glyoxalase-i inhibitors possessing a \u201czinc-binding feature\u201d as potential anticancer agents","volume":"10","author":"Al-Balas","year":"2016","journal-title":"Drug Des, Dev Ther"},{"issue":"4","key":"10.1016\/j.bmc.2020.115608_b0150","doi-asserted-by":"crossref","first-page":"460","DOI":"10.2174\/1568026615666150813150944","article-title":"In Vitro inhibition of glyoxalase \u0426# 134; by flavonoids: new insights from crystallographic analysis","volume":"16","author":"Zhang","year":"2016","journal-title":"Curr Top Med Chem"},{"issue":"5","key":"10.1016\/j.bmc.2020.115608_b0155","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1080\/07391102.2015.1064830","article-title":"Evaluation of potential flavonoid inhibitors of glyoxalase-I based on virtual screening and in vitro studies","volume":"34","author":"Yadav","year":"2016","journal-title":"J Biomol Struct Dyn"},{"issue":"24","key":"10.1016\/j.bmc.2020.115608_b0160","doi-asserted-by":"crossref","first-page":"7486","DOI":"10.1016\/j.bmcl.2012.10.045","article-title":"Design and evaluation of azaindole-substituted N-hydroxypyridones as glyoxalase I inhibitors","volume":"22","author":"Chiba","year":"2012","journal-title":"Bioorg Med Chem Lett"},{"issue":"14","key":"10.1016\/j.bmc.2020.115608_b0165","doi-asserted-by":"crossref","first-page":"4337","DOI":"10.1016\/j.bmcl.2011.05.046","article-title":"Discovery of a new type inhibitor of human glyoxalase I by myricetin-based 4-point pharmacophore","volume":"21","author":"Takasawa","year":"2011","journal-title":"Bioorg Med Chem Lett"},{"issue":"13","key":"10.1016\/j.bmc.2020.115608_b0170","doi-asserted-by":"crossref","first-page":"3793","DOI":"10.1016\/j.bmcl.2006.12.056","article-title":"Design, synthesis, and binding studies of bidentate Zn-chelating peptidic inhibitors of glyoxalase-I","volume":"17","author":"More","year":"2007","journal-title":"Bioorg Med Chem Lett"},{"issue":"3","key":"10.1016\/j.bmc.2020.115608_b0175","doi-asserted-by":"crossref","first-page":"1609","DOI":"10.1021\/acs.jmedchem.8b01868","article-title":"Metal-binding pharmacophore library yields the discovery of a glyoxalase 1 inhibitor","volume":"62","author":"Perez","year":"2019","journal-title":"J Med Chem"},{"key":"10.1016\/j.bmc.2020.115608_b0180","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1016\/j.compbiolchem.2019.03.011","article-title":"Combination of pharmacophore modeling and 3D-QSAR analysis of potential glyoxalase-I inhibitors as anticancer agents","volume":"80","author":"Al-Sha'er","year":"2019","journal-title":"Comput Biol Chem"},{"issue":"20","key":"10.1016\/j.bmc.2020.115608_b0185","doi-asserted-by":"crossref","first-page":"7093","DOI":"10.1016\/j.bmc.2009.09.003","article-title":"Carbonic anhydrase inhibitors. Diazenylbenzenesulfonamides are potent and selective inhibitors of the tumor-associated isozymes IX and XII over the cytosolic isoforms I and II","volume":"17","author":"Carta","year":"2009","journal-title":"Bioorg Med Chem"},{"issue":"3","key":"10.1016\/j.bmc.2020.115608_b0190","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1007\/s00044-019-02486-3","article-title":"Discovery of a nanomolar glyoxalase-I inhibitor using integrated ligand-based pharmacophore modeling and molecular docking","volume":"29","author":"Al-Shari","year":"2019","journal-title":"Med Chem Res"},{"issue":"11","key":"10.1016\/j.bmc.2020.115608_b0195","doi-asserted-by":"crossref","first-page":"1324","DOI":"10.2174\/1570180814666170306120954","article-title":"Novel thiazole carboxylic acid derivatives possessing a \u201czinc binding feature\u201d as potential human glyoxalase-i inhibitors","volume":"14","author":"Al-Balasa","year":"2017","journal-title":"Lett Drug Des Discov"},{"issue":"Pt 1","key":"10.1016\/j.bmc.2020.115608_b0200","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1107\/S0108767307035623","article-title":"The Protein Data Bank: a historical perspective","volume":"64","author":"Berman","year":"2008","journal-title":"Acta Crystallogr Sect A, Found Crystallogr"},{"key":"10.1016\/j.bmc.2020.115608_b0205","doi-asserted-by":"crossref","unstructured":"H.M. Berman T. Battistuz T.N. Bhat et al. The Protein Data Bank. Acta Crystallogr. Sect D, Biol Crystallogr 2002, 58 (Pt 6 No 1), 899-907.","DOI":"10.1107\/S0907444902003451"},{"issue":"2","key":"10.1016\/j.bmc.2020.115608_b0210","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1093\/protein\/gzm083","article-title":"LOOPER: a molecular mechanics-based algorithm for protein loop prediction","volume":"21","author":"Spassov","year":"2008","journal-title":"Protein Eng, Des Selection: PEDS"},{"issue":"11","key":"10.1016\/j.bmc.2020.115608_b0215","doi-asserted-by":"crossref","first-page":"1955","DOI":"10.1110\/ps.036335.108","article-title":"A fast and accurate computational approach to protein ionization","volume":"17","author":"Spassov","year":"2008","journal-title":"Protein Sci"},{"issue":"13","key":"10.1016\/j.bmc.2020.115608_b0220","doi-asserted-by":"crossref","first-page":"1549","DOI":"10.1002\/jcc.10306","article-title":"Detailed analysis of grid-based molecular docking: a case study of CDOCKER-A CHARMm-based MD docking algorithm","volume":"24","author":"Wu","year":"2003","journal-title":"J Comput Chem"}],"container-title":["Bioorganic & Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0968089620304387?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0968089620304387?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,19]],"date-time":"2025-10-19T01:08:35Z","timestamp":1760836115000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0968089620304387"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,8]]},"references-count":44,"journal-issue":{"issue":"16","published-print":{"date-parts":[[2020,8]]}},"alternative-id":["S0968089620304387"],"URL":"https:\/\/doi.org\/10.1016\/j.bmc.2020.115608","relation":{},"ISSN":["0968-0896"],"issn-type":[{"value":"0968-0896","type":"print"}],"subject":[],"published":{"date-parts":[[2020,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Design, synthesis and biological evaluation of novel glyoxalase I inhibitors possessing diazenylbenzenesulfonamide moiety as potential anticancer agents","name":"articletitle","label":"Article Title"},{"value":"Bioorganic & Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bmc.2020.115608","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"115608"}}