{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T06:03:50Z","timestamp":1788329030961,"version":"build-2803163510"},"reference-count":97,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2020,11,1]],"date-time":"2020-11-01T00:00:00Z","timestamp":1604188800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,11,1]],"date-time":"2020-11-01T00:00:00Z","timestamp":1604188800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"name":"Erzincan Binali Y\u0131ld\u0131r\u0131m University","award":["FBA-2017-501"],"award-info":[{"award-number":["FBA-2017-501"]}]},{"name":"Ardahan University","award":["2019-007"],"award-info":[{"award-number":["2019-007"]}]},{"DOI":"10.13039\/501100008770","name":"Anadolu University","doi-asserted-by":"publisher","award":["1610S681"],"award-info":[{"award-number":["1610S681"]}],"id":[{"id":"10.13039\/501100008770","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["International Journal of Biological Macromolecules"],"published-print":{"date-parts":[[2020,11]]},"DOI":"10.1016\/j.ijbiomac.2020.09.043","type":"journal-article","created":{"date-parts":[[2020,9,13]],"date-time":"2020-09-13T01:36:35Z","timestamp":1599960995000},"page":"1970-1988","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":105,"special_numbering":"C","title":["Thiazolyl-pyrazoline derivatives: In vitro and in silico evaluation as potential acetylcholinesterase and carbonic anhydrase inhibitors"],"prefix":"10.1016","volume":"163","author":[{"given":"Belgin","family":"Sever","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C\u00fcneyt","family":"T\u00fcrke\u015f","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mehlika Dilek","family":"Alt\u0131ntop","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yeliz","family":"Demir","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"\u015e\u00fckr\u00fc","family":"Beydemir","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0005","doi-asserted-by":"crossref","first-page":"1548","DOI":"10.2174\/138945012803530134","article-title":"Molecular pathology in neurodegenerative diseases","volume":"13","author":"H Peden","year":"2012","journal-title":"Curr. Drug Targets"},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0010","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1007\/978-981-32-9721-0_3","article-title":"Genetic markers of Alzheimer\u2019s disease","volume":"1192","author":"Nikolac Perkovic","year":"2019","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0015","doi-asserted-by":"crossref","first-page":"975","DOI":"10.3233\/JAD-160612","article-title":"Amyloid-beta and phosphorylated tau accumulations cause abnormalities at synapses of Alzheimer\u2019s disease neurons","volume":"57","author":"Rajmohan","year":"2017","journal-title":"J. Alzheimer\u2019s Disease"},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0020","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1021\/acschemneuro.8b00517","article-title":"Classics in chemical neuroscience: Donepezil","volume":"10","author":"Brewster","year":"2018","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0025","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2020.05.162","article-title":"Biological evaluation of BF2-naphthyridine compounds: tyrosinase and acetylcholinesterase activity, CT-DNA and HSA binding property evaluations","author":"Chaves","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0030","doi-asserted-by":"crossref","first-page":"1161","DOI":"10.2174\/1567205015666180813150703","article-title":"Insights into the drug repositioning applied to the Alzheimer's disease treatment and future perspectives","volume":"15","author":"de Castro","year":"2018","journal-title":"Curr. Alzheimer Res."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0035","series-title":"The Bimodal Features of Butyrylcholinesterase in Cholinergic Neurotransmission and Amyloid Suppression, Emerging Drugs and Targets for Alzheimer\u2019s Disease","first-page":"59","author":"Podoly","year":"2010"},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0040","series-title":"Current Medications for the Treatment of Alzheimer\u2019s Disease: Acetylcholinesterase Inhibitors and NMDA Receptor Antagonist, Drug Discovery Approaches for the Treatment of Neurodegenerative Disorders","first-page":"49","author":"Finn","year":"2017"},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0045","doi-asserted-by":"crossref","first-page":"840","DOI":"10.1016\/j.ijbiomac.2017.08.082","article-title":"Biological evaluation of p-toluene sulphonylhydrazone as carbonic anhydrase IX inhibitors: an approach to fight hypoxia-induced tumors","volume":"106","author":"Queen","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0050","doi-asserted-by":"crossref","DOI":"10.1002\/jbt.22385","article-title":"Inhibition profiles of Voriconazole against acetylcholinesterase, \u03b1-glycosidase, and human carbonic anhydrase I and II isoenzymes","volume":"33","author":"Topal","year":"2019","journal-title":"J. Biochem. Mol. Toxicol."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0055","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1080\/13813455.2017.1303742","article-title":"Natural product inhibitors of carbonic anhydrase I and II isoenzymes: osajin and pomiferin","volume":"123","author":"Dilek","year":"2017","journal-title":"Arch. Physiol. Biochem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0060","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1016\/j.ijbiomac.2018.04.131","article-title":"Implication of sulfonylurea derivatives as prospective inhibitors of human carbonic anhydrase II","volume":"115","author":"Idrees","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0065","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/j.bioorg.2018.12.035","article-title":"Synthesis and biological evaluation of novel tris-chalcones as potent carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase and \u03b1-glycosidase inhibitors","volume":"85","author":"Burmaoglu","year":"2019","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0070","doi-asserted-by":"crossref","first-page":"128657","DOI":"10.1016\/j.molstruc.2020.128657","article-title":"Synthesis, characterization and biological activity evaluation of novel naphthalenylmethylen hydrazine derivatives as carbonic anhydrase inhibitors","author":"Shirinzadeh","year":"2020","journal-title":"J. Mol. Struct."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0075","doi-asserted-by":"crossref","first-page":"1359","DOI":"10.1080\/14756366.2020.1781844","article-title":"The effects of cardiac drugs on human erythrocyte carbonic anhydrase I and II isozymes","volume":"35","author":"Argan","year":"2020","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0080","doi-asserted-by":"crossref","first-page":"2833","DOI":"10.1080\/00958972.2017.1366996","article-title":"Synthesis, crystal structure, spectroscopy, thermal properties and carbonic anhydrase activities of new metal (II) complexes with mefenamic acid and picoline derivatives","volume":"70","author":"Dilek","year":"2017","journal-title":"J. Coord. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0085","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1080\/17460441.2020.1743676","article-title":"Exploring the multiple binding modes of inhibitors to carbonic anhydrases for novel drug discovery","volume":"15","author":"Supuran","year":"2020","journal-title":"Expert Opin. Drug. Disc."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0090","doi-asserted-by":"crossref","first-page":"825","DOI":"10.2174\/156802607780636690","article-title":"Carbonic anhydrases as drug targets-an overview","volume":"7","author":"Supuran","year":"2007","journal-title":"Curr. Top. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0095","doi-asserted-by":"crossref","first-page":"939","DOI":"10.3233\/JAD-2010-100384","article-title":"Plasma carbonic anhydrase II protein is elevated in Alzheimer's disease","volume":"21","author":"Jang","year":"2010","journal-title":"J. Alzheimer's Disease"},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0100","doi-asserted-by":"crossref","first-page":"4724","DOI":"10.3390\/ijms20194724","article-title":"A new kid on the block? Carbonic anhydrases as possible new targets in Alzheimer\u2019s disease","volume":"20","author":"Provensi","year":"2019","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0105","doi-asserted-by":"crossref","first-page":"384","DOI":"10.2174\/1568026615666150813145218","article-title":"Metalloprotein inhibitors for the treatment of human diseases","volume":"16","author":"Yang","year":"2016","journal-title":"Curr. Top. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0110","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.nbd.2015.11.006","article-title":"The carbonic anhydrase inhibitor methazolamide prevents amyloid beta-induced mitochondrial dysfunction and caspase activation protecting neuronal and glial cells in vitro and in the mouse brain","volume":"86","author":"Fossati","year":"2016","journal-title":"Neurobio. Disease"},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0115","doi-asserted-by":"crossref","DOI":"10.1111\/acel.12787","article-title":"Carbonic anhydrase inhibition selectively prevents amyloid \u03b2 neurovascular mitochondrial toxicity","volume":"17","author":"Solesio","year":"2018","journal-title":"Aging Cell"},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0120","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1080\/17425255.2020.1743679","article-title":"An update on drug interaction considerations in the therapeutic use of carbonic anhydrase inhibitors","volume":"16","author":"Supuran","year":"2020","journal-title":"Expert Opin. Drug Metab. Toxicol."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0125","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1080\/13543776.2018.1523897","article-title":"Carbonic anhydrase inhibitors and their potential in a range of therapeutic areas","volume":"28","author":"Supuran","year":"2018","journal-title":"Expert Opin. Ther. Pat."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0130","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1517\/13543776.2012.667403","article-title":"Recent advances in the therapeutic applications of pyrazolines","volume":"22","author":"Shaaban","year":"2012","journal-title":"Expert Opin. Ther. Pat."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0135","doi-asserted-by":"crossref","first-page":"S18","DOI":"10.1007\/PL00014264","article-title":"Breath tests: concepts, applications and limitations","volume":"156","author":"Langhans","year":"1997","journal-title":"Eur. J. Pediatric."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0140","doi-asserted-by":"crossref","first-page":"427","DOI":"10.3109\/14756366.2013.795956","article-title":"4, 5-Dihydro-1H-pyrazole: an indispensable scaffold","volume":"29","author":"Alex","year":"2014","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0145","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1038\/nchembio.128","article-title":"Chemo-enzymatic fluorination of unactivated organic compounds","volume":"5","author":"Rentmeister","year":"2009","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0150","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1517\/13543776.2014.858121","article-title":"Novel thiazole derivatives: a patent review (2008\u20132012; part 1)","volume":"24","author":"Leoni","year":"2014","journal-title":"Expert Opin. Ther. Pat."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0155","first-page":"333","article-title":"Synthesis and evaluation of a new series of thiazolyl-pyrazoline derivatives as cholinesterase inhibitors","volume":"15","author":"Temel","year":"2018","journal-title":"Turk. J. Pharm. Sci."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0160","doi-asserted-by":"crossref","DOI":"10.1002\/jhet.3985","article-title":"Synthesis, cytotoxic, and carbonic anhydrase inhibitory effects of new 2-(3-(4-methoxyphenyl)-5-(aryl)-4,5-dihydro-1H-pyrazol-1-yl)benzo[d]thiazole derivatives","author":"Tugrak","year":"2020","journal-title":"J. Heterocycl. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0165","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/j.ejmech.2016.02.030","article-title":"Synthetic approaches, structure activity relationship and biological applications for pharmacologically attractive pyrazole\/pyrazoline\u2013thiazolidine-based hybrids","volume":"113","author":"Havrylyuk","year":"2016","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0170","article-title":"Development of a multivalent acetylcholinesterase inhibitor via dynamic combinatorial chemistry","author":"Xu","year":"2019","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0175","doi-asserted-by":"crossref","first-page":"1029","DOI":"10.1016\/j.ijbiomac.2019.10.071","article-title":"Purification and characterization of acetylcholinesterase in Rhynchophorus ferrugineus (Olivier)(Coleoptera: Curculionidae)","volume":"147","author":"Mohamed","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0180","doi-asserted-by":"crossref","DOI":"10.1002\/jbt.22313","article-title":"The antidiabetic and anticholinergic effects of chrysin on cyclophosphamide-induced multiple organ toxicity in rats: pharmacological evaluation of some metabolic enzyme activities","volume":"33","author":"Taslimi","year":"2019","journal-title":"J. Biochem. Mol. Toxicol."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0185","first-page":"515","article-title":"Carbonic anhydrase activity responses and histopathological changes in gill and liver tissues after acute exposure to chromium in brown trout juveniles","volume":"44","author":"Demir","year":"2016","journal-title":"Hacettepe J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0190","doi-asserted-by":"crossref","first-page":"e12956","DOI":"10.1111\/jsr.12956","article-title":"Carbonic anhydrase, obstructive sleep apnea and hypertension: effects of intervention","volume":"29","author":"Hoff","year":"2020","journal-title":"J. Sleep Res."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0195","doi-asserted-by":"crossref","first-page":"5185","DOI":"10.1016\/j.bmcl.2014.09.076","article-title":"Carbonic anhydrase inhibitory activity of sulfonamides and carboxylic acids incorporating cyclic imide scaffolds","volume":"24","author":"Alaa","year":"2014","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0200","doi-asserted-by":"crossref","first-page":"1400","DOI":"10.1080\/14756366.2019.1651315","article-title":"Design, synthesis and biological activity of selective hCAs inhibitors based on 2-(benzylsulfinyl) benzoic acid scaffold","volume":"34","author":"Rotondi","year":"2019","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0205","doi-asserted-by":"crossref","DOI":"10.1021\/acsmedchemlett.0c00094","article-title":"Benzofuran-based carboxylic acids as carbonic anhydrase inhibitors and antiproliferative agents against breast cancer","author":"Eldehna","year":"2020","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0210","doi-asserted-by":"crossref","first-page":"1453","DOI":"10.1080\/14756366.2018.1512597","article-title":"Steroids interfere with human carbonic anhydrase activity by using alternative binding mechanisms","volume":"33","author":"Nocentini","year":"2018","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0215","doi-asserted-by":"crossref","first-page":"4421","DOI":"10.1021\/cr200176r","article-title":"Multiple binding modes of inhibitors to carbonic anhydrases: how to design specific drugs targeting 15 different isoforms?","volume":"112","author":"Alterio","year":"2012","journal-title":"Chem. Rev."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0220","doi-asserted-by":"crossref","first-page":"1900292","DOI":"10.1002\/ardp.201900292","article-title":"Synthesis and characterization of some new pyrazolines and their inhibitory potencies against carbonic anhydrases","volume":"353","author":"\u00c7elik","year":"2020","journal-title":"Arch. Pharm. (Weinheim, Ger.)"},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0225","doi-asserted-by":"crossref","first-page":"414","DOI":"10.1134\/S1068162015040111","article-title":"Synthesis and evaluation of new phthalazine substituted \u03b2-lactam derivatives as carbonic anhydrase inhibitors","volume":"41","author":"Berber","year":"2015","journal-title":"Russ. J. Bioorg. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0230","doi-asserted-by":"crossref","first-page":"615","DOI":"10.2174\/138161208783877848","article-title":"Design of zinc binding functions for carbonic anhydrase inhibitors","volume":"14","author":"Winum","year":"2008","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0235","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1080\/14756366.2019.1695791","article-title":"Design, synthesis and molecular modelling studies of some pyrazole derivatives as carbonic anhydrase inhibitors","volume":"35","author":"Dizdaroglu","year":"2020","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0240","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1016\/j.bioorg.2019.02.013","article-title":"Synthesis, biological evaluation and molecular docking of novel pyrazole derivatives as potent carbonic anhydrase and acetylcholinesterase inhibitors","volume":"86","author":"Turkan","year":"2019","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0245","doi-asserted-by":"crossref","first-page":"1800359","DOI":"10.1002\/ardp.201800359","article-title":"Synthesis, characterization, molecular docking and biological activities of novel pyrazoline derivatives","volume":"352","author":"Turkan","year":"2019","journal-title":"Arch. Pharm. (Weinheim, Ger.)"},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0250","doi-asserted-by":"crossref","first-page":"2313","DOI":"10.1080\/00397911.2017.1373406","article-title":"Synthesis and investigation of antibacterial activities and carbonic anhydrase and acetyl cholinesterase inhibition profiles of novel 4,5-dihydropyrazol and pyrazolyl-thiazole derivatives containing methanoisoindol-1,3-dion unit","volume":"47","author":"Budak","year":"2017","journal-title":"Synth. Commun."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0255","doi-asserted-by":"crossref","first-page":"4079","DOI":"10.1074\/jbc.RA119.012400","article-title":"Rational design, synthesis, and evaluation of uncharged,\u201csmart\u201d bis-oxime antidotes of organophosphate-inhibited human acetylcholinesterase","volume":"295","author":"Gorecki","year":"2020","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0260","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2019.111600","article-title":"Carbonic anhydrase inhibitors based on sorafenib scaffold: design, synthesis, crystallographic investigation and effects on primary breast cancer cells","volume":"182","author":"Bozdag","year":"2019","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0265","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1016\/j.ejmech.2018.11.073","article-title":"Exploring structural properties of potent human carbonic anhydrase inhibitors bearing a 4-(cycloalkylamino-1-carbonyl) benzenesulfonamide moiety","volume":"163","author":"Buemi","year":"2019","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0270","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2019.111648","article-title":"Design, synthesis and biological evaluation of a new series of thiazolyl-pyrazolines as dual EGFR and HER2 inhibitors","volume":"182","author":"Sever","year":"2019","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0275","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/0006-2952(61)90145-9","article-title":"A new and rapid colorimetric determination of acetylcholinesterase activity","volume":"7","author":"Ellman","year":"1961","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0280","doi-asserted-by":"crossref","first-page":"103134","DOI":"10.1016\/j.bioorg.2019.103134","article-title":"Novel 2-aminopyridine liganded Pd (II) N-heterocyclic carbene complexes: synthesis, characterization, crystal structure and bioactivity properties","volume":"91","author":"Erdemir","year":"2019","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0285","first-page":"1","article-title":"Inhibition effects of some pesticides and heavy metals on carbonic anhydrase enzyme activity purified from horse mackerel (Trachurus trachurus) gill tissues","author":"Caglayan","year":"2020","journal-title":"Environ. Sci. Pol. Res."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0290","doi-asserted-by":"crossref","first-page":"103153","DOI":"10.1016\/j.bioorg.2019.103153","article-title":"Synthesis, molecular docking analysis and carbonic anhydrase I-II inhibitory evaluation of new sulfonamide derivatives","volume":"91","author":"Sa\u011fl\u0131k","year":"2019","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0295","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0300","doi-asserted-by":"crossref","first-page":"104110","DOI":"10.1016\/j.bioorg.2020.104110","article-title":"Design, synthesis, in vitro and in silico investigation of aldose reductase inhibitory effects of new thiazole-based compounds","author":"Sever","year":"2020","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0305","doi-asserted-by":"crossref","first-page":"1576","DOI":"10.1111\/jphp.13144","article-title":"The behaviour of some antihypertension drugs on human serum paraoxonase-1: an important protector enzyme against atherosclerosis","volume":"71","author":"Demir","year":"2019","journal-title":"J. Pharm. Pharmacol."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0310","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0315","doi-asserted-by":"crossref","DOI":"10.1002\/ddr.21667","article-title":"Naphthoquinones, benzoquinones, and anthraquinones: molecular docking, ADME and inhibition studies on human serum paraoxonase-1 associated with cardiovascular diseases","author":"Demir","year":"2020","journal-title":"Drug Dev. Res."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0320","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1016\/j.ijbiomac.2020.01.192","article-title":"Study of glycation process of human carbonic anhydrase II as well as investigation concerning inhibitory influence of 3-beta-hydroxybutyrate on it","volume":"149","author":"Gharib","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0325","doi-asserted-by":"crossref","first-page":"1198","DOI":"10.1016\/j.ijbiomac.2018.08.186","article-title":"Mechanistic investigation of sulfonamide ligands as human carbonic anhydrase II inhibitors","volume":"120","author":"Alaei","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0330","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1016\/j.ijbiomac.2019.11.012","article-title":"Effect of disease-linked mutations on the structure, function, stability and aggregation of human carbonic anhydrase II","volume":"143","author":"Gupta","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0335","doi-asserted-by":"crossref","first-page":"4221","DOI":"10.1016\/S0021-9258(18)95800-X","article-title":"Esterase activities of human carbonic anhydrases B and C","volume":"242","author":"Verpoorte","year":"1967","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0340","doi-asserted-by":"crossref","DOI":"10.1002\/jbt.22381","article-title":"The effects of zingerone against vancomycin-induced lung, liver, kidney and testis toxicity in rats: the behavior of some metabolic enzymes","volume":"33","author":"\u00c7a\u011flayan","year":"2019","journal-title":"J. Biochem. Mol. Toxicol."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0345","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.3109\/14756366.2012.715287","article-title":"Synthesis and paroxonase activities of novel bromophenols","volume":"28","author":"Akbaba","year":"2013","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0350","doi-asserted-by":"crossref","first-page":"8264","DOI":"10.1021\/bi201284u","article-title":"The original Michaelis constant: translation of the 1913 Michaelis\u2013Menten paper","volume":"50","author":"Johnson","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0355","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1021\/ja01318a036","article-title":"The determination of enzyme dissociation constants","volume":"56","author":"Lineweaver","year":"1934","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0360","first-page":"10","article-title":"Inhibition effects of gemcitabine hydrochloride, acyclovir, and 5-fluorouracil on human serum paraoxonase-1 (hPON1): in vitro","volume":"1","author":"T\u00fcrke\u015f","year":"2013","journal-title":"Open J. Biochem"},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0365","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/j.pharep.2013.08.007","article-title":"Effect of calcium channel blockers on paraoxonase-1 (PON1) activity and oxidative stress","volume":"66","author":"T\u00fcrke\u015f","year":"2014","journal-title":"Pharmacol. Rep."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0370","doi-asserted-by":"crossref","first-page":"622","DOI":"10.3109\/14756366.2014.959511","article-title":"Human serum paraoxonase-1 (hPON1): in vitro inhibition effects of moxifloxacin hydrochloride, levofloxacin hemihidrate, cefepime hydrochloride, cefotaxime sodium and ceftizoxime sodium","volume":"30","author":"T\u00fcrke\u015f","year":"2015","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0375","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1016\/j.etap.2015.11.024","article-title":"In vitro inhibitory effects of palonosetron hydrochloride, bevacizumab and cyclophosphamide on purified paraoxonase-I (hPON1) from human serum","volume":"42","author":"T\u00fcrke\u015f","year":"2016","journal-title":"Environ. Toxicol. Pharmacol."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0380","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1007\/s12010-019-03009-x","article-title":"Anti-diabetic properties of calcium channel blockers: inhibition effects on aldose reductase enzyme activity","volume":"189","author":"T\u00fcrke\u015f","year":"2019","journal-title":"Appl. Biochem. Biotechnol."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0385","first-page":"1","article-title":"Some calcium-channel blockers: kinetic and in silico studies on paraoxonase-I","author":"T\u00fcrke\u015f","year":"2020","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0390","doi-asserted-by":"crossref","first-page":"13347","DOI":"10.1002\/slct.201903458","article-title":"New Isoindole-1, 3-dione substituted sulfonamides as potent inhibitors of carbonic anhydrase and acetylcholinesterase: design, synthesis, and biological evaluation","volume":"4","author":"G\u00fcndo\u011fdu","year":"2019","journal-title":"ChemistrySelect"},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0395","doi-asserted-by":"crossref","first-page":"103004","DOI":"10.1016\/j.bioorg.2019.103004","article-title":"Synthesis, biological evaluation and in silico studies of novel N-substituted phthalazine sulfonamide compounds as potent carbonic anhydrase and acetylcholinesterase inhibitors","volume":"89","author":"T\u00fcrke\u015f","year":"2019","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0400","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/S0169-409X(96)00423-1","article-title":"Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings","volume":"23","author":"Lipinski","year":"1997","journal-title":"Adv. Drug Deliv. Rev."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0405","doi-asserted-by":"crossref","first-page":"2878","DOI":"10.1021\/ja993663t","article-title":"Prediction of properties from simulations: free energies of solvation in hexadecane, octanol, and water","volume":"122","author":"Duffy","year":"2000","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0410","doi-asserted-by":"crossref","first-page":"2719","DOI":"10.1021\/jm901137j","article-title":"New substructure filters for removal of pan assay interference compounds (PAINS) from screening libraries and for their exclusion in bioassays","volume":"53","author":"Baell","year":"2010","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0415","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1007\/s12010-019-03073-3","article-title":"Inhibition of human serum paraoxonase-I with antimycotic drugs: in vitro and in silico studies","volume":"190","author":"T\u00fcrke\u015f","year":"2020","journal-title":"Appl. Biochem. Biotechnol."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0420","first-page":"1","article-title":"Gadolinium-based contrast agents: in vitro paraoxonase 1 inhibition, in silico studies","author":"Beydemir","year":"2019","journal-title":"Drug Chem. Toxicol."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0425","doi-asserted-by":"crossref","first-page":"1395","DOI":"10.1007\/s11696-019-00988-3","article-title":"Molecular docking and investigation of 4-(benzylideneamino)-and 4-(benzylamino)-benzenesulfonamide derivatives as potent AChE inhibitors","volume":"74","author":"I\u015f\u0131k","year":"2020","journal-title":"Chem. Pap."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0430","doi-asserted-by":"crossref","first-page":"1553","DOI":"10.1111\/jphp.13141","article-title":"A potential risk factor for paraoxonase 1: in silico and in-vitro analysis of the biological activity of proton-pump inhibitors","volume":"71","author":"T\u00fcrke\u015f","year":"2019","journal-title":"J. Pharm. Pharmacol."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0435","doi-asserted-by":"crossref","first-page":"e2000102","DOI":"10.1002\/ardp.202000102","article-title":"Synthesis, characterization, biological evaluation, and in silico studies of novel 1,3-diaryltriazene-substituted sulfathiazole derivatives","volume":"353","author":"I\u015f\u0131k","year":"2020","journal-title":"Arch. Pharm. (Weinheim, Ger.)"},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0440","first-page":"1013","article-title":"Inhibition effects of phenolic compounds on human serum paraoxonase-1 enzyme","volume":"9","author":"T\u00fcrke\u015f","year":"2019","journal-title":"J. Inst. Sci. Tech."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0445","doi-asserted-by":"crossref","first-page":"887","DOI":"10.2174\/1871520620666200218110645","article-title":"Molecular docking studies and inhibition properties of some antineoplastic agents against paraoxonase-I","volume":"20","author":"Demir","year":"2020","journal-title":"Anti Cancer Agents Med. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0450","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1080\/07391102.2020.1763838","article-title":"Benzenesulfonamide derivatives as potent acetylcholinesterase, \u03b1-glycosidase, and glutathione S-transferase inhibitors: biological evaluation and molecular docking studies","author":"Taslimi","year":"2020","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0455","doi-asserted-by":"crossref","first-page":"950","DOI":"10.1080\/14756366.2020.1746784","article-title":"Synthesis, characterization, biological evaluation and in silico studies of sulfonamide Schiff bases","volume":"35","author":"Durgun","year":"2020","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0460","doi-asserted-by":"crossref","first-page":"392","DOI":"10.2174\/0929866526666190226162225","article-title":"Investigation of potential paraoxonase-I inhibitors by kinetic and molecular docking studies: chemotherapeutic drugs","volume":"26","author":"T\u00fcrke\u015f","year":"2019","journal-title":"Protein Pept. Lett."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0465","first-page":"1","article-title":"Calcium Channel blockers: molecular docking and inhibition studies on carbonic anhydrase I and II isoenzymes","author":"T\u00fcrke\u015f","year":"2020","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0470","doi-asserted-by":"crossref","first-page":"9731","DOI":"10.1002\/slct.201902424","article-title":"In vitro and in silico studies on the toxic effects of antibacterial drugs as human serum paraoxonase 1 inhibitor","volume":"4","author":"T\u00fcrke\u015f","year":"2019","journal-title":"ChemistrySelect"},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0475","doi-asserted-by":"crossref","first-page":"103897","DOI":"10.1016\/j.bioorg.2020.103897","article-title":"Synthesis, characterization, inhibition effects, and molecular docking studies as acetylcholinesterase, \u03b1-glycosidase, and carbonic anhydrase inhibitors of novel benzenesulfonamides incorporating 1,3,5-triazine structural motifs","volume":"100","author":"Lolak","year":"2020","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0480","doi-asserted-by":"crossref","first-page":"e1900383","DOI":"10.1002\/ardp.201900383","article-title":"Sulfonamides incorporating ketene N,S-acetal bioisosteres as potent carbonic anhydrase and acetylcholinesterase inhibitors","volume":"353","author":"Istrefi","year":"2020","journal-title":"Arch. Pharm. (Weinheim, Ger.)"},{"key":"10.1016\/j.ijbiomac.2020.09.043_bb0485","doi-asserted-by":"crossref","first-page":"1111","DOI":"10.1016\/j.ijbiomac.2019.09.237","article-title":"Benzenesulfonamide derivatives containing imine and amine groups: inhibition on human paraoxonase and molecular docking studies","volume":"146","author":"I\u015f\u0131k","year":"2020","journal-title":"Int. J. Biol. Macromol."}],"container-title":["International Journal of Biological Macromolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813020343993?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813020343993?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,26]],"date-time":"2025-09-26T08:37:19Z","timestamp":1758875839000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0141813020343993"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,11]]},"references-count":97,"alternative-id":["S0141813020343993"],"URL":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2020.09.043","relation":{},"ISSN":["0141-8130"],"issn-type":[{"value":"0141-8130","type":"print"}],"subject":[],"published":{"date-parts":[[2020,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Thiazolyl-pyrazoline derivatives: In vitro and in silico evaluation as potential acetylcholinesterase and carbonic anhydrase inhibitors","name":"articletitle","label":"Article Title"},{"value":"International Journal of Biological Macromolecules","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2020.09.043","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}