{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,8]],"date-time":"2026-07-08T03:12:15Z","timestamp":1783480335915,"version":"3.55.0"},"reference-count":78,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2019,4,1]],"date-time":"2019-04-01T00:00:00Z","timestamp":1554076800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2019,4,1]],"date-time":"2019-04-01T00:00:00Z","timestamp":1554076800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"name":"Erzincan Binali Yildirim University","award":["TSA-2017-495"],"award-info":[{"award-number":["TSA-2017-495"]}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Bioorganic Chemistry"],"published-print":{"date-parts":[[2019,4]]},"DOI":"10.1016\/j.bioorg.2018.12.035","type":"journal-article","created":{"date-parts":[[2019,1,2]],"date-time":"2019-01-02T11:41:59Z","timestamp":1546429319000},"page":"191-197","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":164,"special_numbering":"C","title":["Synthesis and biological evaluation of novel tris-chalcones as potent carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase and \u03b1-glycosidase inhibitors"],"prefix":"10.1016","volume":"85","author":[{"given":"Serdar","family":"Burmaoglu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ali Osman","family":"Yilmaz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M. Fatih","family":"Polat","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R\u00fcya","family":"Kaya","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"\u0130lhami","family":"Gulcin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2838-163X","authenticated-orcid":false,"given":"Oztekin","family":"Algul","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"1\u20132","key":"10.1016\/j.bioorg.2018.12.035_b0005","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1016\/S0022-1139(99)00201-8","article-title":"Fluorine-containing natural products","volume":"100","author":"O'Hagan","year":"1999","journal-title":"J. Fluor. Chem."},{"key":"10.1016\/j.bioorg.2018.12.035_b0010","series-title":"Fluorine in medicinal chemistry and chemical biology","author":"Ojima","year":"2009"},{"key":"10.1016\/j.bioorg.2018.12.035_b0015","series-title":"Organofluorine chemistry, Blackwell Pub","author":"Uneyama","year":"2006"},{"key":"10.1016\/j.bioorg.2018.12.035_b0020","series-title":"Introduction to stereochemistry and conformational analysis","author":"Juaristi","year":"1991"},{"issue":"3","key":"10.1016\/j.bioorg.2018.12.035_b0025","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1021\/j100785a001","article-title":"van der Waals volumes and radii","volume":"68","author":"Bondi","year":"1964","journal-title":"J. Phys. Chem."},{"issue":"24","key":"10.1016\/j.bioorg.2018.12.035_b0030","doi-asserted-by":"crossref","first-page":"13699","DOI":"10.1073\/pnas.93.24.13699","article-title":"The reaction of fluorocitrate with aconitase and the crystal structure of the enzyme-inhibitor complex","volume":"93","author":"Lauble","year":"1996","journal-title":"P. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bioorg.2018.12.035_b0035","series-title":"Handbook of Radiopharmaceuticals: Radiochemistry and Applications","first-page":"195","article-title":"Chemistry of fluorine-18 radiopharmaceuticals","author":"Snyder","year":"2003"},{"key":"10.1016\/j.bioorg.2018.12.035_b0040","unstructured":"C. Hansch, A. Leo, D. Hoekman, D. Livingstone, Exploring QSAR: hydrophobic, electronic, and steric constants, American Chemical Society Washington, DC1995."},{"issue":"49","key":"10.1016\/j.bioorg.2018.12.035_b0045","doi-asserted-by":"crossref","first-page":"12125","DOI":"10.1021\/ja002627n","article-title":"Contribution of fluorine to protein-ligand affinity in the binding of fluoroaromatic inhibitors to carbonic anhydrase II","volume":"122","author":"Kim","year":"2000","journal-title":"J. Am. Chem. Soc."},{"issue":"8","key":"10.1016\/j.bioorg.2018.12.035_b0050","doi-asserted-by":"crossref","first-page":"1100","DOI":"10.1002\/cmdc.200700059","article-title":"Predicting properties and tuning physicochemical in lead optimization: Amine basicities","volume":"2","author":"Morgenthaler","year":"2007","journal-title":"ChemMedChem"},{"issue":"901","key":"10.1016\/j.bioorg.2018.12.035_b0055","first-page":"497","article-title":"Biochemistry of fluoroacetate poisoning. The isolation and some properties of the fluorotricarboxylic acid inhibitor of citrate metabolism","volume":"140","author":"Peters","year":"1953","journal-title":"Proc. R. Soc. Lond. Ser. B - Biol. Sci."},{"issue":"22","key":"10.1016\/j.bioorg.2018.12.035_b0060","doi-asserted-by":"crossref","first-page":"9790","DOI":"10.1016\/j.bmc.2008.09.064","article-title":"Structure-activity relationship of antibacterial chalcones","volume":"16","author":"Avila","year":"2008","journal-title":"Bioorg. Med. Chem."},{"issue":"8","key":"10.1016\/j.bioorg.2018.12.035_b0065","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1016\/S0960-894X(00)00072-X","article-title":"Antitumor agents. Part 202: Novel 2 '-amino chalcones: Design, synthesis and biological evaluation","volume":"10","author":"Xia","year":"2000","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.bioorg.2018.12.035_b0070","doi-asserted-by":"crossref","first-page":"758","DOI":"10.1016\/j.ejmech.2014.08.033","article-title":"Recent developments in biological activities of chalcones: A mini review","volume":"85","author":"Singh","year":"2014","journal-title":"Eur. J. Med. Chem."},{"issue":"4","key":"10.1016\/j.bioorg.2018.12.035_b0075","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1039\/b311404j","article-title":"Anthocyanins and other flavonoids","volume":"21","author":"Williams","year":"2004","journal-title":"Nat. Prod. Rep."},{"issue":"7","key":"10.1016\/j.bioorg.2018.12.035_b0080","doi-asserted-by":"crossref","first-page":"1484","DOI":"10.1021\/tx800115g","article-title":"Structure-activity relationships of methoxychalcones as inducers of heme oxygenase-1","volume":"21","author":"Sawle","year":"2008","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.bioorg.2018.12.035_b0085","series-title":"Synthetic multivalent molecules: concepts and biomedical applications","author":"Choi","year":"2004"},{"issue":"3","key":"10.1016\/j.bioorg.2018.12.035_b0090","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1002\/bit.22056","article-title":"Polyvalency: A promising strategy for drug design","volume":"101","author":"Vance","year":"2008","journal-title":"Biotechnol. Bioeng."},{"issue":"8","key":"10.1016\/j.bioorg.2018.12.035_b0095","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1248\/cpb.c14-00074","article-title":"Use of a Hexasubstituted Benzene Scaffold in the Development of Multivalent HIV-1 Integrase Inhibitors","volume":"62","author":"Tupehiangmai","year":"2014","journal-title":"Chem. Pharm. Bull."},{"issue":"20","key":"10.1016\/j.bioorg.2018.12.035_b0100","doi-asserted-by":"crossref","first-page":"6073","DOI":"10.1021\/ja00410a015","article-title":"Static and dynamic stereochemistry of hexaethylbenzene and of its tricarbonylchromium, tricarbonylmolybdenum, and dicarbonyl(triphenylphosphine)chromium complexes","volume":"103","author":"Iverson","year":"1981","journal-title":"J. Am. Chem. Soc."},{"issue":"10","key":"10.1016\/j.bioorg.2018.12.035_b0105","doi-asserted-by":"crossref","first-page":"2219","DOI":"10.1002\/1521-3765(20020517)8:10<2218::AID-CHEM2218>3.0.CO;2-H","article-title":"1,3,5\u20132,4,6-functionalized, facially segregated benzenes - Exploitation of sterically predisposed systems in supramolecular chemistry","volume":"8","author":"Hennrich","year":"2002","journal-title":"Chem.-Eur. J."},{"issue":"15\u201316","key":"10.1016\/j.bioorg.2018.12.035_b0110","doi-asserted-by":"crossref","first-page":"1742","DOI":"10.1016\/j.ccr.2012.02.001","article-title":"Inorganic and organometallic hemicage podates and cage cryptates incorporating a benzene platform","volume":"256","author":"Zysman-Colman","year":"2012","journal-title":"Coord. Chem. Rev."},{"key":"10.1016\/j.bioorg.2018.12.035_b0115","doi-asserted-by":"crossref","first-page":"3349","DOI":"10.1039\/DT9910003349","volume":"12","author":"Hunter","year":"1991","journal-title":"J. Chem. Soc.-Dalton Trans."},{"key":"10.1016\/j.bioorg.2018.12.035_b0120","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1016\/j.ijbiomac.2016.10.096","article-title":"Novel eugenol derivatives: Potent acetylcholinesterase and carbonic anhydrase inhibitors","volume":"94","author":"Topal","year":"2017","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.bioorg.2018.12.035_b0125","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1016\/j.bioorg.2018.09.013","article-title":"New azafluorenones with cytotoxic and carbonic anhydrase inhibitory properties: 2-Aryl-4-(4-hydroxyphenyl)-5H-indeno 1,2-b pyridin-5-ones","volume":"81","author":"Tugrak","year":"2018","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.bioorg.2018.12.035_b0130","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/j.bioorg.2018.08.003","article-title":"Novel thymol bearing oxypropanolamine derivatives as potent some metabolic enzyme inhibitors - Their antidiabetic, anticholinergic and antibacterial potentials","volume":"81","author":"Zengin","year":"2018","journal-title":"Bioorganic Chem."},{"key":"10.1016\/j.bioorg.2018.12.035_b0135","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1016\/j.bioorg.2018.11.001","article-title":"Synthesis, characterization, crystal structure of novel bis-thiomethylcyclohexanone derivatives and their inhibitory properties against some metabolic enzymes","volume":"82","author":"Bi\u00e7er","year":"2019","journal-title":"Bioorganic Chem."},{"key":"10.1016\/j.bioorg.2018.12.035_b0140","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1016\/j.molstruc.2018.11.038","article-title":"Imidazolinium chloride salts bearing wing tip groups: Synthesis, molecular docking and metabolic enzymes inhibition","volume":"1179","author":"Yi\u011fit","year":"2019","journal-title":"J. Mol. Struct."},{"key":"10.1016\/j.bioorg.2018.12.035_b0145","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.poly.2018.08.026","article-title":"Synthesis, characterization, crystal structure, electrochemical studies and biological evaluation of metal complexes with thiosemicarbazone of glyoxylic acid","volume":"155","author":"Huseynova","year":"2018","journal-title":"Polyhedron"},{"issue":"27","key":"10.1016\/j.bioorg.2018.12.035_b0150","doi-asserted-by":"crossref","first-page":"7976","DOI":"10.1002\/slct.201801019","article-title":"Novel benzylic substituted imidazolinium, tetrahydropyrimidinium and tetrahydrodiazepinium salts: potent carbonic anhydrase and acetylcholinesterase inhibitors","volume":"3","author":"Yigit","year":"2018","journal-title":"ChemistrySelect"},{"issue":"7","key":"10.1016\/j.bioorg.2018.12.035_b0155","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1080\/13543776.2018.1487400","article-title":"Sulfonamide inhibitors: a patent review 2013-present","volume":"28","author":"Gulcin","year":"2018","journal-title":"Expert Opin. Ther. Patents"},{"key":"10.1016\/j.bioorg.2018.12.035_b0160","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1042\/BJ20051102","article-title":"Characterization of CA XV, a new GPI-anchored form of carbonic anhydrase","volume":"392","author":"Hilvo","year":"2005","journal-title":"Biochem. J."},{"key":"10.1016\/j.bioorg.2018.12.035_b0165","doi-asserted-by":"crossref","first-page":"642","DOI":"10.1016\/j.bioorg.2018.09.028","article-title":"Synthesis of different thio-scaffolds bearing sulfonamide with subnanomolar carbonic anhydrase II and IX inhibitory properties and X-ray investigations for their inhibitory mechanism","volume":"81","author":"Angeli","year":"2018","journal-title":"Bioorganic Chem."},{"key":"10.1016\/j.bioorg.2018.12.035_b0170","first-page":"808-+","article-title":"The first synthesis and antioxidant and anticholinergic activities of 1-(4,5-dihydroxybenzyl)pyrrolidin-2-one derivative bromophenols including natural products","volume":"42(3)","author":"Rezai","year":"2018","journal-title":"Turk. J. Chem."},{"issue":"8","key":"10.1016\/j.bioorg.2018.12.035_b0175","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1002\/jbt.22173","article-title":"Intermolecular amination of allylic and benzylic alcohols leads to effective inhibitions of acetylcholinesterase enzyme and carbonic anhydrase I and II isoenzymes","volume":"32","author":"Atmaca","year":"2018","journal-title":"J. Biochem. Mol. Toxicol."},{"issue":"3","key":"10.1016\/j.bioorg.2018.12.035_b0180","doi-asserted-by":"crossref","first-page":"e12516","DOI":"10.1111\/jfbc.12516","article-title":"Antioxidant and anticholinergic properties of olivetol","volume":"42","author":"Taslimi","year":"2018","journal-title":"J. Food Biochem."},{"issue":"9","key":"10.1016\/j.bioorg.2018.12.035_b0185","doi-asserted-by":"crossref","first-page":"e1800150","DOI":"10.1002\/ardp.201800150","article-title":"Synthesis of novel sulfamides incorporating phenethylamines and determination of their inhibition profiles against some metabolic enzymes","volume":"351","author":"Aksu","year":"2018","journal-title":"Arch. Pharm."},{"issue":"10","key":"10.1016\/j.bioorg.2018.12.035_b0190","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1002\/ardp.201800200","article-title":"Some pyrazoles derivatives: Potent carbonic anhydrase, \u03b1-glycosidase, and cholinesterase enzymes inhibitors","volume":"351","author":"Turkan","year":"2018","journal-title":"Arch. Pharm."},{"key":"10.1016\/j.bioorg.2018.12.035_b0195","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1016\/j.biopha.2017.01.003","article-title":"Oxidative stress and mRNA expression of acetylcholinesterase in the leukocytes of ischemic patients","volume":"87","author":"Isik","year":"2017","journal-title":"Biomed. Pharmacother."},{"key":"10.1016\/j.bioorg.2018.12.035_b0200","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1016\/j.indcrop.2015.05.034","article-title":"LC-MS\/MS analysis, antioxidant and anticholinergic properties of galanga (Alpinia officinarum Hance) rhizomes","volume":"74","author":"Kose","year":"2015","journal-title":"Ind. Crop. Prod."},{"issue":"2","key":"10.1016\/j.bioorg.2018.12.035_b0205","first-page":"266","article-title":"Antioxidant antiradical, and anticholinergic properties of cynarin purified from the Illyrian thistle (Onopordum illyricum L.), J. Enzym. Inhib","volume":"31","author":"Topal","year":"2016","journal-title":"Med. Chem."},{"issue":"3","key":"10.1016\/j.bioorg.2018.12.035_b0210","first-page":"441","article-title":"Acetylcholinesterase and carbonic anhydrase isoenzymes I and II inhibition profiles of taxifolin","volume":"31","author":"Gocer","year":"2016","journal-title":"J. Enzym. Inhib. Med. Chem."},{"issue":"6","key":"10.1016\/j.bioorg.2018.12.035_b0215","doi-asserted-by":"crossref","first-page":"1698","DOI":"10.3109\/14756366.2015.1135914","article-title":"Rosmarinic acid inhibits some metabolic enzymes including glutathione S-transferase, lactoperoxidase, acetylcholinesterase, butyrylcholinesterase and carbonic anhydrase isoenzymes","volume":"31","author":"Gulcin","year":"2016","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.bioorg.2018.12.035_b0220","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1016\/j.ijbiomac.2018.08.001","article-title":"Antidiabetic and antiparasitic potentials: Inhibition effects of some natural antioxidant compounds on alpha-glycosidase, alpha-amylase and human glutathione S-transferase enzymes","volume":"119","author":"Gulcin","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.bioorg.2018.12.035_b0225","doi-asserted-by":"crossref","first-page":"857","DOI":"10.1016\/j.ijbiomac.2018.08.004","article-title":"Diarylmethanon, bromophenol and diarylmethane compounds: Discovery of potent aldose reductase, alpha-amylase and alpha-glycosidase inhibitors as new therapeutic approach in diabetes and functional hyperglycemia","volume":"119","author":"Taslimi","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"issue":"9","key":"10.1016\/j.bioorg.2018.12.035_b0230","doi-asserted-by":"crossref","first-page":"e22197","DOI":"10.1002\/jbt.22197","article-title":"Synthesis, crystal structure and biological evaluation of spectroscopic characterization of Ni(II) and Co(II) complexes with N-salicyloil-N-maleoil-hydrazine as anticholinergic and antidiabetic agents","volume":"32","author":"Gondolova","year":"2018","journal-title":"J. Biochem. Mol. Toxicol."},{"issue":"11","key":"10.1016\/j.bioorg.2018.12.035_b0235","doi-asserted-by":"crossref","first-page":"e1800209","DOI":"10.1002\/ardp.201800209","article-title":"Novel sulfamate derivatives of menthol: Synthesis, characterization, and cholinesterases and carbonic anhydrase enzymes inhibition properties","volume":"351","author":"Daryadel","year":"2018","journal-title":"Arch. Pharm."},{"key":"10.1016\/j.bioorg.2018.12.035_b0240","doi-asserted-by":"crossref","first-page":"e1800263","DOI":"10.1002\/ardp.201800263","article-title":"Antidiabetic potential: In vitro inhibition effects of bromophenol and diarylmethanones derivatives on metabolic enzymes","author":"Demir","year":"2018","journal-title":"Arch. Pharm."},{"issue":"12","key":"10.1016\/j.bioorg.2018.12.035_b0245","doi-asserted-by":"crossref","first-page":"e22221","DOI":"10.1002\/jbt.22221","article-title":"Synthesis, characterization, antioxidant, antidiabetic, anticholinergic, and antiepileptic properties of novel N-substituted tetrahydropyrimidines based on phenylthiourea","volume":"32","author":"Maharramova","year":"2018","journal-title":"J. Biochem. Mol. Toxicol."},{"issue":"4","key":"10.1016\/j.bioorg.2018.12.035_b0250","doi-asserted-by":"crossref","first-page":"586","DOI":"10.3109\/14756366.2014.956310","article-title":"Carbonic anhydrase inhibitors: guaiacol and catechol derivatives effectively inhibit certain human carbonic anhydrase isoenzymes (hCA I, II, IX and XII)","volume":"30","author":"Scozzafava","year":"2015","journal-title":"J. Enzym. Inhib. Med. Chem."},{"issue":"7","key":"10.1016\/j.bioorg.2018.12.035_b0255","doi-asserted-by":"crossref","first-page":"10103","DOI":"10.3390\/molecules190710103","article-title":"Capsaicin: A Potent Inhibitor of Carbonic Anhydrase Isoenzymes","volume":"19","author":"Arabaci","year":"2014","journal-title":"Molecules"},{"issue":"5","key":"10.1016\/j.bioorg.2018.12.035_b0260","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1111\/j.1747-0285.2010.00965.x","article-title":"Carbonic Anhydrase Inhibitors: Inhibition of Human Erythrocyte Isozymes I and II with a Series of Phenolic Acids","volume":"75","author":"Sarikaya","year":"2010","journal-title":"Chem. Biol. Drug Des."},{"issue":"11","key":"10.1016\/j.bioorg.2018.12.035_b0265","doi-asserted-by":"crossref","first-page":"2925","DOI":"10.1016\/j.bmc.2013.03.077","article-title":"Synthesis and carbonic anhydrase inhibitory properties of sulfamides structurally related to dopamine","volume":"21","author":"Aksu","year":"2013","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.bioorg.2018.12.035_b0270","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/j.bioorg.2018.08.005","article-title":"Novel sulfonamides incorporating 1,3,5-triazine and amino acid structural motifs as inhibitors of the physiological carbonic anhydrase isozymes I II and IV and tumor-associated isozyme IX","volume":"81","author":"Mikus","year":"2018","journal-title":"Bioorganic Chem."},{"issue":"12","key":"10.1016\/j.bioorg.2018.12.035_b0275","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1002\/ardp.201700198","article-title":"Synthesis and carbonic anhydrase inhibition of tetrabromo chalcone derivatives","volume":"350","author":"Kocyigit","year":"2017","journal-title":"Arch. Pharm."},{"issue":"1","key":"10.1016\/j.bioorg.2018.12.035_b0280","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1080\/13813455.2017.1360914","article-title":"Synthesis of chalcone-imide derivatives and investigation of their anticancer and antimicrobial activities, carbonic anhydrase and acetylcholinesterase enzymes inhibition profiles","volume":"124","author":"Kocyigit","year":"2018","journal-title":"Arch. Physiol. Biochem."},{"key":"10.1016\/j.bioorg.2018.12.035_b0285","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/j.ejmech.2018.07.054","article-title":"Novel hydrazido benzenesulfonamides-isatin conjugates: Synthesis, carbonic anhydrase inhibitory activity and molecular modeling studies","volume":"157","author":"Abo-Ashour","year":"2018","journal-title":"Eur. J. Med. Chem."},{"issue":"10","key":"10.1016\/j.bioorg.2018.12.035_b0290","doi-asserted-by":"crossref","first-page":"2598","DOI":"10.1016\/j.bmc.2014.12.054","article-title":"N-Acylsulfonamides strongly inhibit human carbonic anhydrase isoenzymes I and II","volume":"23","author":"Yildirim","year":"2015","journal-title":"Bioorg. Med. Chem."},{"issue":"8","key":"10.1016\/j.bioorg.2018.12.035_b0295","doi-asserted-by":"crossref","first-page":"1303","DOI":"10.1111\/head.13144","article-title":"The idiopathic intracranial hypertension treatment trial: a review of the outcomes","volume":"57","author":"Smith","year":"2017","journal-title":"Headache"},{"issue":"2","key":"10.1016\/j.bioorg.2018.12.035_b0300","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. Pharma."},{"issue":"13","key":"10.1016\/j.bioorg.2018.12.035_b0305","doi-asserted-by":"crossref","first-page":"3592","DOI":"10.1016\/j.bmc.2015.04.019","article-title":"Discovery of potent carbonic anhydrase and acetylcholine esterase inhibitors: Novel sulfamoylcarbamates and sulfamides derived from acetophenones","volume":"23","author":"Akincioglu","year":"2015","journal-title":"Bioorg. Med. Chem."},{"issue":"2","key":"10.1016\/j.bioorg.2018.12.035_b0310","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1002\/bmc.2761","article-title":"Rapid screening and identification of alpha-glucosidase inhibitors from mulberry leaves using enzyme-immobilized magnetic beads coupled with HPLC\/MS and NMR","volume":"27","author":"Tao","year":"2013","journal-title":"Biomed. Chromatogr."},{"issue":"12","key":"10.1016\/j.bioorg.2018.12.035_b0315","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1002\/jbt.21995","article-title":"The impact of some natural phenolic compounds on carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase, and \u03b1-glycosidase enzymes: An antidiabetic, anticholinergic, and antiepileptic study","volume":"31","author":"Taslimi","year":"2017","journal-title":"J. Biochem. Mol. Toxicol."},{"issue":"6","key":"10.1016\/j.bioorg.2018.12.035_b0320","doi-asserted-by":"crossref","first-page":"2251","DOI":"10.1016\/j.bmcl.2012.01.089","article-title":"One pot synthesis and anticancer activity of dimeric phloroglucinols","volume":"22","author":"Chauthe","year":"2012","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"2","key":"10.1016\/j.bioorg.2018.12.035_b0325","doi-asserted-by":"crossref","first-page":"864","DOI":"10.1016\/j.foodchem.2012.08.072","article-title":"One-step purification of lactoperoxidase from bovine milk by affinity chromatography","volume":"136","author":"Atasever","year":"2013","journal-title":"Food Chem."},{"key":"10.1016\/j.bioorg.2018.12.035_b0330","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/j.bioorg.2015.04.006","article-title":"Antioxidant and acetylcholinesterase inhibition properties of novel bromophenol derivatives","volume":"60","author":"Oztaskin","year":"2015","journal-title":"Bioorg. Chem."},{"issue":"1","key":"10.1016\/j.bioorg.2018.12.035_b0335","doi-asserted-by":"crossref","first-page":"35","DOI":"10.3109\/14756366.2012.750311","article-title":"Carbonic anhydrase inhibitory properties of novel sulfonamide derivatives of aminoindanes and aminotetralins","volume":"29","author":"Akbaba","year":"2014","journal-title":"J. Enzym. Inhib. Med. Chem."},{"issue":"18","key":"10.1016\/j.bioorg.2018.12.035_b0340","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."},{"issue":"2","key":"10.1016\/j.bioorg.2018.12.035_b0345","doi-asserted-by":"crossref","first-page":"316","DOI":"10.3109\/14756366.2014.928704","article-title":"Carbonic anhydrase and acetylcholinesterase inhibitory effects of carbamates and sulfamoylcarbamates","volume":"30","author":"Gocer","year":"2015","journal-title":"J. Enzym. Inhib. Med. Chem."},{"issue":"1","key":"10.1016\/j.bioorg.2018.12.035_b0350","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1002\/ardp.201300273","article-title":"Novel Sulphamides and Sulphonamides Incorporating the Tetralin Scaffold as Carbonic Anhydrase and Acetylcholine Esterase Inhibitors","volume":"347","author":"Akincioglu","year":"2014","journal-title":"Arch. Pharm."},{"issue":"1-2","key":"10.1016\/j.bioorg.2018.12.035_b0355","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."},{"issue":"5259","key":"10.1016\/j.bioorg.2018.12.035_b0360","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"},{"issue":"6","key":"10.1016\/j.bioorg.2018.12.035_b0365","doi-asserted-by":"crossref","first-page":"1379","DOI":"10.1016\/j.bmc.2013.01.019","article-title":"Novel sulfamides as potential carbonic anhydrase isoenzymes inhibitors","volume":"21","author":"Akincioglu","year":"2013","journal-title":"Bioorg. Med. Chem."},{"issue":"1","key":"10.1016\/j.bioorg.2018.12.035_b0370","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1080\/1475636040001704461","article-title":"Effects of low molecular weight plasma inhibitors of rainbow trout (Oncorhynchus mykiss) on human erythrocyte carbonic anhydrase-II isozyme activity in vitro and rat erythrocytes in vivo","volume":"20","author":"Hisar","year":"2005","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.bioorg.2018.12.035_b0375","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.bioorg.2014.07.009","article-title":"Carbonic anhydrase inhibitory properties of novel benzylsulfamides using molecular modeling and experimental studies","volume":"56","author":"Goksu","year":"2014","journal-title":"Bioorganic Chem."},{"key":"10.1016\/j.bioorg.2018.12.035_b0380","doi-asserted-by":"crossref","first-page":"906","DOI":"10.1016\/j.molstruc.2018.08.063","article-title":"Synthesis, characterization, crystal structures, theoretical calculations and biological evaluations of novel substituted tacrine derivatives as cholinesterase and carbonic anhydrase enzymes inhibitors","volume":"1175","author":"Okten","year":"2019","journal-title":"J. Mol. Struct."},{"issue":"9","key":"10.1016\/j.bioorg.2018.12.035_b0385","doi-asserted-by":"crossref","first-page":"e22191","DOI":"10.1002\/jbt.22191","article-title":"Novel amides of 1,1-bis-(carboxymethylthio)-1-arylethanes: Synthesis, characterization, acetylcholinesterase, butyrylcholinesterase, and carbonic anhydrase inhibitory properties","volume":"32","author":"Taslimi","year":"2018","journal-title":"J. Biochem. Mol. Toxicol."},{"issue":"3","key":"10.1016\/j.bioorg.2018.12.035_b0390","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."}],"container-title":["Bioorganic Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0045206818315013?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0045206818315013?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,23]],"date-time":"2025-09-23T07:46:12Z","timestamp":1758613572000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0045206818315013"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,4]]},"references-count":78,"alternative-id":["S0045206818315013"],"URL":"https:\/\/doi.org\/10.1016\/j.bioorg.2018.12.035","relation":{},"ISSN":["0045-2068"],"issn-type":[{"value":"0045-2068","type":"print"}],"subject":[],"published":{"date-parts":[[2019,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Synthesis and biological evaluation of novel tris-chalcones as potent carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase and \u03b1-glycosidase inhibitors","name":"articletitle","label":"Article Title"},{"value":"Bioorganic Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bioorg.2018.12.035","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}