PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 30253337-0 2018 Synthesis of different thio-scaffolds bearing sulfonamide with subnanomolar carbonic anhydrase II and IX inhibitory properties and X-ray investigations for their inhibitory mechanism. Sulfonamides 46-57 carbonic anhydrase 2 Homo sapiens 76-97 30176324-0 2018 Mechanistic investigation of sulfonamide ligands as human carbonic anhydrase II inhibitors. Sulfonamides 29-40 carbonic anhydrase 2 Homo sapiens 58-79 30176324-1 2018 The effect of some sulfonamide ligands on the structure and function of human carbonic anhydrase II (HCA II) was investigated using different spectroscopic techniques including UV-Vis, fluorescence, circular dichroism and molecular dynamics simulation tools. Sulfonamides 19-30 carbonic anhydrase 2 Homo sapiens 78-99 29462772-3 2018 All these sulfonamides were found to be potent inhibitors of the cytosolic isoform hCA II with low nanomolar to sub-nanomolar Kis in the range of 0.2-21.5 nM, as well as a moderate selectivity against other cytosolic isoforms hCA I and hCA VII, and great selectivity against membrane-bound isoform hCA IX was observed. Sulfonamides 10-22 carbonic anhydrase 2 Homo sapiens 83-89 28111158-0 2017 Synthesis of isoxazole-containing sulfonamides with potent carbonic anhydrase II and VII inhibitory properties. Sulfonamides 34-46 carbonic anhydrase 2 Homo sapiens 59-80 28753093-3 2017 Several subnanomolar/low nanomolar, isoform-selective sulfonamide inhibitors targeting hCA II, VII and IX were detected. Sulfonamides 54-65 carbonic anhydrase 2 Homo sapiens 87-93 28110167-0 2017 Chiral separation of new sulfonamide derivatives and evaluation of their enantioselective affinity for human carbonic anhydrase II by microscale thermophoresis and surface plasmon resonance. Sulfonamides 25-36 carbonic anhydrase 2 Homo sapiens 109-130 28110167-1 2017 The aim of this study was to develop a method combining chiral separation and biophysical techniques to evaluate the enantioselective affinity of original sulfonamide derivatives towards their therapeutic target, the human carbonic anhydrase II (hACII). Sulfonamides 155-166 carbonic anhydrase 2 Homo sapiens 223-244 28110167-9 2017 Finally, by comparing the MST and SPR techniques, MST appears especially adapted for further screening of a series of sulfonamide derivatives due to the lower time required to estimate a binding constant while consuming as little hCAII as SPR. Sulfonamides 118-129 carbonic anhydrase 2 Homo sapiens 230-235 27325502-8 2016 In this article, we demonstrate the working principles and benchmark the performance of label-enhanced SPR in a model system-the interaction between carbonic anhydrase II and a number of small-molecule sulfonamide-based inhibitors. Sulfonamides 202-213 carbonic anhydrase 2 Homo sapiens 149-170 28002963-5 2016 In addition, comparisons with the corresponding inhibitor complexes of human carbonic anhydrase II (HCAII) indicated that HpalphaCA possesses an additional, alternative binding site for sulfonamides that is not present in HCAII. Sulfonamides 186-198 carbonic anhydrase 2 Homo sapiens 77-98 27474804-2 2016 In vitro assay for inhibition of carbonic anhydrase showed that some of the compounds having sulfonamide moiety are capable of inhibiting carbonic anhydrase II. Sulfonamides 93-104 carbonic anhydrase 2 Homo sapiens 138-159 27396930-3 2016 The new sulfonamides acted as medium potency inhibitors of hCA I (KIs of 28.5-2954nM), being highly effective as hCA II (KIs in the range of 0.62-12.4nM) and XII (KIs of 0.54-7.11nM) inhibitors. Sulfonamides 8-20 carbonic anhydrase 2 Homo sapiens 113-119 27211329-6 2016 Novel classes of selective sulfonamide CA II/VII inhibitors showed highly improved efficacy in animal models of neuropathic pain, compared to acetazolamide, offering the basis for the development of specific therapies of this syndrome based on selective CA isoforms inhibition. Sulfonamides 27-38 carbonic anhydrase 2 Homo sapiens 39-44 26810836-4 2016 X-ray crystallography of its adduct with hCA II and comparison of the structure with that of other five hCA II-sulfonamide adducts belonging to the SLC-0111 series, afforded us to understand the particular inhibition profile of the new sulfonamide. Sulfonamides 111-122 carbonic anhydrase 2 Homo sapiens 104-110 27234893-3 2016 The new sulfonamides showed excellent inhibition of all three isoforms, with KIs in the range of 0.84-702nM against hCA I, of 0.41-288nM against hCA II and of 5.6-29.2 against the tumor-associated hCA IX, a validated anti-tumor target, with a sulfonamide (SLC-0111) in Phase I clinical trials for the treatment of hypoxic, metastatic solid tumors overexpressing CA IX. Sulfonamides 8-20 carbonic anhydrase 2 Homo sapiens 145-151 27234893-3 2016 The new sulfonamides showed excellent inhibition of all three isoforms, with KIs in the range of 0.84-702nM against hCA I, of 0.41-288nM against hCA II and of 5.6-29.2 against the tumor-associated hCA IX, a validated anti-tumor target, with a sulfonamide (SLC-0111) in Phase I clinical trials for the treatment of hypoxic, metastatic solid tumors overexpressing CA IX. Sulfonamides 8-19 carbonic anhydrase 2 Homo sapiens 145-151 26700575-1 2016 The binding of sulfonamides to human carbonic anhydrase II (hCAII) is a complex and long-debated example of protein-ligand recognition and interaction. Sulfonamides 15-27 carbonic anhydrase 2 Homo sapiens 37-58 26700575-1 2016 The binding of sulfonamides to human carbonic anhydrase II (hCAII) is a complex and long-debated example of protein-ligand recognition and interaction. Sulfonamides 15-27 carbonic anhydrase 2 Homo sapiens 60-65 26810836-5 2016 Similar to SLC-0111, the thioureido sulfonamide primarily interacted with the hydrophobic side of the hCA II active site, with the tail participating in van der Waals interactions with Phe131 and Pro202, in addition to the coordination of the deprotonated sulfonamide to the active site metal ion. Sulfonamides 36-47 carbonic anhydrase 2 Homo sapiens 102-108 26810836-6 2016 On the contrary, the tail of other sulfonamides belonging to the SLC-0111 series (2-isopropyl-phenyl; 3-nitrophenyl) were orientated towards the hydrophilic half of the active site, which was correlated with orders of magnitude better inhibitory activity against hCA II, and a loss of selectivity for the inhibition of the tumor-associated CAs. Sulfonamides 35-47 carbonic anhydrase 2 Homo sapiens 263-269 26796953-2 2016 Most of the new sulfonamides reported here showed excellent inhibitory effects against isoforms hCA II, IX and XII, but no highly isoform-selective inhibition profiles. Sulfonamides 16-28 carbonic anhydrase 2 Homo sapiens 96-114 26199669-2 2015 In the context of our program of photochromic pharmacophores we were interested in the exploration of azobenzene-containing sulfonamides to block the catalytic activity of human carbonic anhydrase II (hCAII). Sulfonamides 124-136 carbonic anhydrase 2 Homo sapiens 178-199 27160030-3 2016 The separation of the CA II and CA IV (both of which are catalytically active isoforms, highly sensitive to sulfonamide-type inhibitors) is particularly remarkable and is adding significantly to the global body of data on the chemical biology of carbonic anhydrases. Sulfonamides 108-119 carbonic anhydrase 2 Homo sapiens 22-27 27435177-2 2016 The inhibition constant (Ki) of these sulfonamides were in the range of 232.16-637.70 nM toward the slow cytosolic isozyme hCA I, and in the range of 342.07-455.80 nM toward hCA II. Sulfonamides 38-50 carbonic anhydrase 2 Homo sapiens 174-180 26639945-3 2015 Most of the new sulfonamides showed excellent inhibitory effects against the four isoforms, with KIs of 7.6-322nM against hCA I, of 0.06-85.4nM against hCA II; of 6.7-152nM against hCA IX and of 0.49-237nM against hCA XII; respectively. Sulfonamides 16-28 carbonic anhydrase 2 Homo sapiens 152-158 26534780-6 2015 Some investigated compounds here showed effective hCA II inhibitory effects, in the same range as the clinically used sulfonamide, sulfanilamide or mafenide and might be used as leads for generating enzyme inhibitors possibly targeting other CA isoforms which have not been yet assayed for their interactions with such agents. Sulfonamides 118-129 carbonic anhydrase 2 Homo sapiens 50-56 26160114-0 2015 Probing the "bipolar" nature of the carbonic anhydrase active site: aromatic sulfonamides containing 1,3-oxazol-5-yl moiety as picomolar inhibitors of cytosolic CA I and CA II isoforms. Sulfonamides 77-89 carbonic anhydrase 2 Homo sapiens 170-175 26199669-2 2015 In the context of our program of photochromic pharmacophores we were interested in the exploration of azobenzene-containing sulfonamides to block the catalytic activity of human carbonic anhydrase II (hCAII). Sulfonamides 124-136 carbonic anhydrase 2 Homo sapiens 201-206 26199669-3 2015 Herein, we report the synthesis and in vitro evaluation of a small library of nine photochromic sulfonamides towards hCAII. Sulfonamides 96-108 carbonic anhydrase 2 Homo sapiens 117-122 24112770-5 2014 The results suggested that sulfonamide derivatives with naphthalene, fluorene, and acridan as the scaffold structures can be the potential isozyme-selective CAIs, especially for isozymes CA II, IV, and IX. Sulfonamides 27-38 carbonic anhydrase 2 Homo sapiens 187-192 25358036-4 2014 X-ray crystal structures of two new sulfonamides bound to the physiologically dominant CA II isoform showed the tails of these derivatives bound within the hydrophobic half of the enzyme active site through van der Waals contacts with Val135, Leu198, Leu204, Trp209, Pro201, and Pro202 amino acids. Sulfonamides 36-48 carbonic anhydrase 2 Homo sapiens 87-92 25310626-3 2014 By means of X-ray crystallography of adducts of several sulfonamides with CA II, the effective inhibitory properties were rationalized at the molecular level. Sulfonamides 56-68 carbonic anhydrase 2 Homo sapiens 74-79 25898725-0 2014 Comparison of QSAR models based on combinations of genetic algorithm, stepwise multiple linear regression, and artificial neural network methods to predict Kd of some derivatives of aromatic sulfonamides as carbonic anhydrase II inhibitors. Sulfonamides 191-203 carbonic anhydrase 2 Homo sapiens 207-228 25733161-4 2015 Here we explain why 6-sulfamoyl-saccharin, unlike saccharin, binds to the metal ion from the hCA II active site by its primary sulfonamide moiety and not the secondary one as saccharin itself. Sulfonamides 127-138 carbonic anhydrase 2 Homo sapiens 93-99 24666294-2 2015 Low nanomolar activity was observed against hCA II (KIs of 0.56-17.1 nM) with these sulfonamides, whereas the slow cytosolic isoform hCA I was less inhibited by these compounds (KIs of 86.4 nM-32.8 microM). Sulfonamides 84-96 carbonic anhydrase 2 Homo sapiens 44-50 23311862-2 2014 The human carbonic anhydrase isozymes hCA I and hCA II inhibition effects of the synthesized sulfonamides were determined. Sulfonamides 93-105 carbonic anhydrase 2 Homo sapiens 48-54 23316861-2 2013 In this study, we report the radiosynthesis and in vitro and in vivo evaluation of 11C and 18F sulfonamide derivatives targeting carbonic anhydrase II (CA II), a metallo-enzyme expressed in RBCs, as potential blood pool tracers. Sulfonamides 95-106 carbonic anhydrase 2 Homo sapiens 129-150 24146387-2 2014 At least three isoforms, CA II, IV and XII are targeted by the sulfonamide inhibitors, some of which are clinically used drugs. Sulfonamides 63-74 carbonic anhydrase 2 Homo sapiens 25-30 24012377-3 2013 This elongated compound binds in an extended conformation to hCA II, with its tail lying towards the hydrophobic half of the active site whereas the sulfonamide moiety coordinates the zinc ion. Sulfonamides 149-160 carbonic anhydrase 2 Homo sapiens 61-67 23777898-0 2013 Sulfonamides containing coumarin moieties selectively and potently inhibit carbonic anhydrases II and IX: design, synthesis, inhibitory activity and 3D-QSAR analysis. Sulfonamides 0-12 carbonic anhydrase 2 Homo sapiens 75-104 23352754-1 2013 By using phthalimido-substituted aromatic sufonamides as lead molecules, a series of new sulfonamides incorporating ortho-benzenedisulfonimide moieties have been synthesized and tested against the human (h) cytosolic carbonic anhydrase (CA, EC 4.2.1.1) isozymes hCA I and hCA II and the transmembrane, tumor-associated isozymes hCA IX and hCA XII. Sulfonamides 89-101 carbonic anhydrase 2 Homo sapiens 272-346 23859774-2 2013 The new sulfonamides were investigated as inhibitors of the zinc metalloenzyme CA (EC 4.2.1.1), and more specifically against the human (h) cytosolic isoforms hCA I and II and the transmembrane, tumor-associated ones hCA IX and XII: The new compounds were medium-weak hCA I inhibitors (KIs in the range of 224-7544nM), but were compactly, highly effective, low nanomolar hCA II inhibitors (KIs of 2.2-7.7nM). Sulfonamides 8-20 carbonic anhydrase 2 Homo sapiens 371-377 23859774-5 2013 Highly favorable, predominantly hydrophobic interactions between the sulfonamide scaffold and the hCA II active site were responsible for the binding, in addition to the coordination of the sulfamoyl moiety to the zinc ion. Sulfonamides 69-80 carbonic anhydrase 2 Homo sapiens 98-104 23316861-2 2013 In this study, we report the radiosynthesis and in vitro and in vivo evaluation of 11C and 18F sulfonamide derivatives targeting carbonic anhydrase II (CA II), a metallo-enzyme expressed in RBCs, as potential blood pool tracers. Sulfonamides 95-106 carbonic anhydrase 2 Homo sapiens 152-157 22775345-2 2012 Crystallographic studies on the complex of hCA II with the lead compound of this series, namely, 4-sulfamido-benzenesulfonamide, revealed the binding of two molecules in the enzyme active site cavity, the first one canonically coordinated to the zinc ion by means of the sulfonamide group and the second one located at the entrance of the cavity. Sulfonamides 116-127 carbonic anhydrase 2 Homo sapiens 43-49 19796939-2 2009 The high affinity of hCA II isozyme towards some sulfonamide inhibitors obtained here was used to select from the dynamic library specific inhibitors of this isoform. Sulfonamides 49-60 carbonic anhydrase 2 Homo sapiens 21-27 21371595-8 2011 Guidelines are presented to demonstrate the limits of detection for weak-binding ligands, as applied to sulfonamide-based inhibitors of carbonic anhydrase II and applied to nucleotide binding to the death-associated protein kinase 1 catalytic domain. Sulfonamides 104-115 carbonic anhydrase 2 Homo sapiens 136-157 20371220-2 2010 Using carbonic anhydrase II as a model system, we characterized a set of 10 sulfonamide-based inhibitors that range in molecular mass from 98 to 341Da and approximately 10,000-fold in affinity (0.4mM to 20nM). Sulfonamides 76-87 carbonic anhydrase 2 Homo sapiens 6-27 20598552-4 2010 An X-ray crystal structure of hCA II in complex with 4-(7-methoxy-coumarin-4-yl-acetamido)-benzenesulfonamide (KI of 9.1 nM against hCA II) showed the intact inhibitor coordinated to the zinc ion from the enzyme active site by the sulfonamide moiety, and participating in a edge-to-face stacking with Phe131, in addition to other hydrophobic and hydrophilic interactions with water molecules and amino acid residues from the active site. Sulfonamides 98-109 carbonic anhydrase 2 Homo sapiens 30-36 20598552-4 2010 An X-ray crystal structure of hCA II in complex with 4-(7-methoxy-coumarin-4-yl-acetamido)-benzenesulfonamide (KI of 9.1 nM against hCA II) showed the intact inhibitor coordinated to the zinc ion from the enzyme active site by the sulfonamide moiety, and participating in a edge-to-face stacking with Phe131, in addition to other hydrophobic and hydrophilic interactions with water molecules and amino acid residues from the active site. Sulfonamides 98-109 carbonic anhydrase 2 Homo sapiens 132-138 22386980-4 2012 Affinity for sulfonamides/sulfamates was decreased in all three mutants compared to wt hCA II. Sulfonamides 13-25 carbonic anhydrase 2 Homo sapiens 87-93 21706094-0 2011 Human carbonic anhydrase II as a host for piano-stool complexes bearing a sulfonamide anchor. Sulfonamides 74-85 carbonic anhydrase 2 Homo sapiens 6-27 20005709-1 2010 X-ray crystal studies of the carbonic anhydrase II-trithiocarbonate adduct--an inhibitor mimicking the sulfonamide and urea binding to the enzyme. Sulfonamides 103-114 carbonic anhydrase 2 Homo sapiens 29-50 20819062-6 2010 As the X-ray crystal structure of one such sulfonamide with the human isoform CA II is also know, the 3-substituted-phenyl-1H-indole-5-sulfonamides represent a totally new class of inhibitors obtained by structure-based drug design, which show efficiency in inhibiting both alpha- and beta-CAs from several species. Sulfonamides 43-54 carbonic anhydrase 2 Homo sapiens 78-83 19824891-5 2009 Many of these sulfonamides were also selective inhibitors for their interaction with CA VI over the physiologically dominant and ubiquitous isoform CA II, with selectivity ratios of 4.11-35.93 for inhibiting the secreted over the cytosolic isozyme. Sulfonamides 14-26 carbonic anhydrase 2 Homo sapiens 148-153 19827837-4 2009 We present the crystal structures of anomeric sulfonamides 4, 7, and 10 and the sugar sulfamate drug topiramate in complex with human recombinant CA II. Sulfonamides 46-58 carbonic anhydrase 2 Homo sapiens 146-151 19778001-1 2009 Spin-labeled sulfonamides incorporating TEMPO moieties showed efficient activity as inhibitors of the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1) and, in particular, of the physiologically relevant isoenzymes hCA II, hCA IX, and hCA XIV. Sulfonamides 13-25 carbonic anhydrase 2 Homo sapiens 215-221 19778001-4 2009 Analysis and fitting of the ESR spectra of several spin-labeled sulfonamides with isoforms CA II (cytosolic), CA IX (catalytic domain and full length transmembrane, tumor-associated isoform) and CA XIV (transmembrane isozyme) provided information about polarity and dynamics of specific microenvironments sensed by the nitroxyl group within the active site cavity of these isozymes. Sulfonamides 64-76 carbonic anhydrase 2 Homo sapiens 91-96 18600270-6 2008 The X-ray crystal structure of the CA II-indapamide adduct was also resolved at high resolution, and the binding of this sulfonamide to the enzyme was compared to that of dichlorophenamide, sulpiride and a pyridinium containing sulfonamide. Sulfonamides 121-132 carbonic anhydrase 2 Homo sapiens 35-40 19201197-4 2009 Some of these sulfonamides also showed a good selectivity profile for the inhibition of the nematode over the human isozymes CA I and II (selectivity ratios in the range of 1.78-4.95 for the inhibition of ceCA over hCA II). Sulfonamides 14-26 carbonic anhydrase 2 Homo sapiens 215-221 19231207-5 2009 Some antioxidant phenol derivatives investigated here showed effective hCA II inhibitory effects, in the same range as the clinically used sulfonamide acetazolamide, and might be used as leads for generating enzyme inhibitors possibly targeting other CA isoforms which have not been yet assayed for their interactions with such agents. Sulfonamides 139-150 carbonic anhydrase 2 Homo sapiens 71-77 18599640-7 2008 Several examples of the applicability of the model are presented, including specific sulfonamide binding to recombinant hCAII, peptide and ANS binding to the Polo-box domain of Plk1, and zinc ion binding to the recombinant porcine growth hormone. Sulfonamides 85-96 carbonic anhydrase 2 Homo sapiens 120-125 19303173-1 2009 In this study, we present an application of EVA descriptors for a QSAR model of inhibition of carbonic anhydrase isozyme CA II by an heterogeneous set of 66 sulfonamide compounds. Sulfonamides 157-168 carbonic anhydrase 2 Homo sapiens 121-126 18600270-6 2008 The X-ray crystal structure of the CA II-indapamide adduct was also resolved at high resolution, and the binding of this sulfonamide to the enzyme was compared to that of dichlorophenamide, sulpiride and a pyridinium containing sulfonamide. Sulfonamides 228-239 carbonic anhydrase 2 Homo sapiens 35-40 18179217-2 2008 It shows that the binding of a derivative of alamethicin carrying a covalently attached sulfonamide ligand to carbonic anhydrase II (CA II) resulted in the inhibition of ion channel conductance through the bilayer. Sulfonamides 88-99 carbonic anhydrase 2 Homo sapiens 110-131 18037297-6 2008 The flaked shape of affinity resin (100-400 microm) presumably simplified affinity experimental procedures and the affinity resin immobilizing Sulfonamide effectively captured one of the target proteins, CAII, without non-specifically bound proteins. Sulfonamides 143-154 carbonic anhydrase 2 Homo sapiens 204-208 18162396-4 2008 The crystal structure of the hCA II adduct of this sulfonamide revealed interesting interactions between the inhibitor and the enzyme which are quite different from those observed in the adducts of CA II with the structurally related aliphatic derivatives zonisamide, 2-amino-1,3,4-thiadiazolyl-5-difluoromethanesulfonamide, and 2-dimethylamino-5-[sulfonamido-(aminomethyl)]-1,3,4-thiadiazole reported earlier. Sulfonamides 51-62 carbonic anhydrase 2 Homo sapiens 30-35 18179217-2 2008 It shows that the binding of a derivative of alamethicin carrying a covalently attached sulfonamide ligand to carbonic anhydrase II (CA II) resulted in the inhibition of ion channel conductance through the bilayer. Sulfonamides 88-99 carbonic anhydrase 2 Homo sapiens 133-138 18179217-7 2008 This method gave a dissociation constant of approximately 2 microM for the binding of CA II to alamethicin-sulfonamide in the bilayer recording chamber: this value is consistent with a value obtained independently with CA II and a related sulfonamide derivative by isothermal titration calorimetry. Sulfonamides 107-118 carbonic anhydrase 2 Homo sapiens 86-91 17504133-7 2007 Moreover, the inhibition of CA isozymes, critical for the development and invasion of cancer cells, such as CA II, IX and XII, may constitute an important mechanism of antitumor action of such sulfonamide compounds. Sulfonamides 193-204 carbonic anhydrase 2 Homo sapiens 108-113 17118494-0 2007 3D-QSAR study of sulfonamide inhibitors of human carbonic anhydrase II. Sulfonamides 17-28 carbonic anhydrase 2 Homo sapiens 49-70 17118494-1 2007 3D-QSAR models of Comparative of Molecular Field Analysis (CoMFA) and Comparative of Molecular Similarity Indices Analysis (CoMSIA) of 61 potent carbonic anhydrase II (CAII) sulfonamide inhibitors were performed using two methods. Sulfonamides 174-185 carbonic anhydrase 2 Homo sapiens 145-166 17118494-1 2007 3D-QSAR models of Comparative of Molecular Field Analysis (CoMFA) and Comparative of Molecular Similarity Indices Analysis (CoMSIA) of 61 potent carbonic anhydrase II (CAII) sulfonamide inhibitors were performed using two methods. Sulfonamides 174-185 carbonic anhydrase 2 Homo sapiens 168-172 17007806-1 2006 In this benchmark study, 26 investigators were asked to characterize the kinetics and affinities of 10 sulfonamide inhibitors binding to the enzyme carbonic anhydrase II using Biacore optical biosensors. Sulfonamides 103-114 carbonic anhydrase 2 Homo sapiens 148-169 16165351-2 2005 The unsubstituted sulfonamides inhibited hCA I with inhibition constants in the range of 63-138 nM, hCA II with inhibition constants in the range of 6.3-8.8 nM, and hCA IX with inhibition constants in the range of 2.8-15 nM, being thus more active than clinically used inhibitors such as acetazolamide, methazolamide, ethoxzolamide, dichlorophenamide or indisulam (E 7070). Sulfonamides 18-30 carbonic anhydrase 2 Homo sapiens 100-106 16962556-4 2006 We found that the affinities determined for nine sulfonamide-based inhibitors of the enzyme carbonic anhydrase II were highly correlated with the values determined using isothermal titration calorimetry. Sulfonamides 49-60 carbonic anhydrase 2 Homo sapiens 92-113 16858005-8 2006 Thus many, but not all, sulfonamide drugs appear to interact with CA II and may target other CA isozymes. Sulfonamides 24-35 carbonic anhydrase 2 Homo sapiens 66-71 16820676-2 2006 The crystal structure of human CA II has been determined in complex with two CA inhibitors (CAIs) containing conventional sulfonamide and thiadiazole moieties separated by a -CF2- or -CHNH2- spacer group. Sulfonamides 122-133 carbonic anhydrase 2 Homo sapiens 31-36 16787097-2 2006 Its binding to hCA II is similar to that of other benzesulfonamides, with the ionized sulfonamide coordinated to the Zn2+ ion within the enzyme active site, and also participating in a network of hydrogen bonds with residues Thr199 and Glu106. Sulfonamides 55-66 carbonic anhydrase 2 Homo sapiens 15-21 16298304-2 2005 The sulfonamide group binds to the active site zinc ion of human carbonic anhydrase II located in a 15 A deep cleft. Sulfonamides 4-15 carbonic anhydrase 2 Homo sapiens 65-86 16134940-1 2005 Structure for the adduct of carbonic anhydrase II with 1-N-(4-sulfamoylphenyl-ethyl)-2,4,6-trimethylpyridinium perchlorate, a membrane-impermeant antitumor sulfonamide, is reported. Sulfonamides 156-167 carbonic anhydrase 2 Homo sapiens 28-49 16134002-12 2004 These data showing inhibition of hCAII by the unsubstituted sulfonamides celecoxib and valdecoxib, but not by rofecoxib, may have important implications for the elucidation of the mechanisms of action as well as the side effects associated with COX-2 inhibitors. Sulfonamides 60-72 carbonic anhydrase 2 Homo sapiens 33-38 15686888-0 2005 QSAR studies on benzene sulfonamide carbonic anhydrase inhibitors: need of hydrophobic parameter for topological modeling of binding constants of sulfonamides to human CA-II. Sulfonamides 146-158 carbonic anhydrase 2 Homo sapiens 168-173 15686888-1 2005 The binding constants (logK) of benzene sulfonamides to human CA-II have been modeled using a large series of distance-based topological indices. Sulfonamides 40-52 carbonic anhydrase 2 Homo sapiens 62-67 15603956-5 2005 Several low nanomolar CA I and CA II inhibitors were detected both in the aromatic and heterocyclic sulfonamide series, whereas the best hCA IX inhibitors (inhibition constants in the range of 22-35 nM) all belonged to the acetazolamide-like derivatives. Sulfonamides 100-111 carbonic anhydrase 2 Homo sapiens 31-36 15482952-5 2004 Isozyme V showed an inhibition profile with these sulfonamides different of that of hCA II. Sulfonamides 50-62 carbonic anhydrase 2 Homo sapiens 84-90 15081039-4 2004 Some of these compounds showed excellent CA IX inhibitory properties and also selectivity ratios favorable to CA IX over CA II, the other physiologically relevant isozyme with high affinity for sulfonamide inhibitors. Sulfonamides 194-205 carbonic anhydrase 2 Homo sapiens 121-126 15499997-2 2004 These sulfonamides were assayed for inhibition of human carbonic anhydrase I (hCA-I) and human carbonic anhydrase II (hCA-II) which were purified by affinity chromatography. Sulfonamides 6-18 carbonic anhydrase 2 Homo sapiens 95-116 15499997-2 2004 These sulfonamides were assayed for inhibition of human carbonic anhydrase I (hCA-I) and human carbonic anhydrase II (hCA-II) which were purified by affinity chromatography. Sulfonamides 6-18 carbonic anhydrase 2 Homo sapiens 118-124 15070333-1 2004 Polypeptides designed to fold into helix-loop-helix motifs and to dimerize to form four-helix bundles were functionalized by the introduction of a sulfonamide derivative known to bind human carbonic anhydrase II (HCAII) and one or both of the dansyl- and methoxycoumarin fluorescent probes. Sulfonamides 147-158 carbonic anhydrase 2 Homo sapiens 190-211 11676494-5 2001 Human CA IX was very strongly inhibited by three classic sulfonamides and cyanate, with inhibition constants that are close to those for CA II. Sulfonamides 57-69 carbonic anhydrase 2 Homo sapiens 137-142 12873509-1 2003 The X-ray crystal structure for the adduct of human carbonic anhydrase II (hCA II) with 4-(4-sulfamoylphenylcarboxamidoethyl)benzenesulfonamide, a topically acting antiglaucoma sulfonamide has been resolved at a resolution of 1.8 A. Sulfonamides 132-143 carbonic anhydrase 2 Homo sapiens 52-73 12873509-1 2003 The X-ray crystal structure for the adduct of human carbonic anhydrase II (hCA II) with 4-(4-sulfamoylphenylcarboxamidoethyl)benzenesulfonamide, a topically acting antiglaucoma sulfonamide has been resolved at a resolution of 1.8 A. Sulfonamides 132-143 carbonic anhydrase 2 Homo sapiens 75-81 14698154-4 2004 The binding of sulpiride to the hCA II active site is similar to that of other sulfonamide inhibitors, considering the interactions of the sulfonamide zinc anchoring group, but differs considerably when the organic scaffold of the molecule is analyzed. Sulfonamides 79-90 carbonic anhydrase 2 Homo sapiens 32-38 14698154-4 2004 The binding of sulpiride to the hCA II active site is similar to that of other sulfonamide inhibitors, considering the interactions of the sulfonamide zinc anchoring group, but differs considerably when the organic scaffold of the molecule is analyzed. Sulfonamides 139-150 carbonic anhydrase 2 Homo sapiens 32-38 14611844-5 2003 Similarly to hCA II, the mitochondrial isozymes show micro-nanomolar affinity for sulfonamides such as sulfanilamide and acetazolamide. Sulfonamides 82-94 carbonic anhydrase 2 Homo sapiens 13-19 11807116-8 2001 Sensitivity to sulphonamides was similar in all species and was within the range of the mammalian CA II isoform. Sulfonamides 15-28 carbonic anhydrase 2 Homo sapiens 98-103 11021544-0 2000 Docking of sulfonamides to carbonic anhydrase II and IV. Sulfonamides 11-23 carbonic anhydrase 2 Homo sapiens 27-48 11310605-8 2001 The mechanism of antitumor action with the new sulfonamides reported here remains obscure, but may involve inhibition of CA isozymes which predominate in tumor cell membranes (CA IX and CA XII), perhaps causing acidification of the intercellular milieu, or inhibition of intracellular isozymes which provide bicarbonate for the synthesis of nucleotides and other essential cell components (CA II and CA V). Sulfonamides 47-59 carbonic anhydrase 2 Homo sapiens 390-395 11021544-4 2000 Specifically, we report on the docking of sulfonamides to carbonic anhydrase II and IV, which are of interest due to their application in glaucoma therapy. Sulfonamides 42-54 carbonic anhydrase 2 Homo sapiens 58-79 10445050-7 1999 Spectroscopic studies on Co(II)-substituted hCA II proved that the new inhibitors directly bind to the metal ion within the enzyme active site, similarly to the classical inhibitors of the unsubstituted sulfonamide type. Sulfonamides 203-214 carbonic anhydrase 2 Homo sapiens 44-50 10811034-2 2000 The new derivatives generally act as stronger inhibitors of two carbonic anhydrase (CA) isozymes, CA I and CA II, as compared to the parent unsubstituted sulfonamides from which they were obtained. Sulfonamides 154-166 carbonic anhydrase 2 Homo sapiens 107-112 11140609-5 2000 An interesting behavior was evidenced for some of the ortho-substituted arylsulfonylcarbamato-sulfonamides, which showed higher affinities for the isozyme hCA I, as compared to hCA II and bCA IV (generally hCA I is 10-1000 less sensitive to "normal" sulfonamide inhibitors, such as acetazolamide, methazolamide or dorzolamide, as compared to hCA II). Sulfonamides 94-105 carbonic anhydrase 2 Homo sapiens 177-183 11140609-5 2000 An interesting behavior was evidenced for some of the ortho-substituted arylsulfonylcarbamato-sulfonamides, which showed higher affinities for the isozyme hCA I, as compared to hCA II and bCA IV (generally hCA I is 10-1000 less sensitive to "normal" sulfonamide inhibitors, such as acetazolamide, methazolamide or dorzolamide, as compared to hCA II). Sulfonamides 94-105 carbonic anhydrase 2 Homo sapiens 342-348 10995069-0 2000 Carbonic anhydrase inhibitors: synthesis of sulfonamides incorporating 2,4,6-trisubstituted-pyridinium-ethylcarboxamido moieties possessing membrane-impermeability and in vivo selectivity for the membrane-bound (CA IV) versus the cytosolic (CA I and CA II) isozymes. Sulfonamides 44-56 carbonic anhydrase 2 Homo sapiens 250-255 9857211-3 1999 Inhibition constants (KI) towards acetazolamide (ACTZ) were 8.4.10(-9) M for erythrocyte CA and 7.6.10(-9) M for gill CA, indicating a high sensitivity to sulfonamides, as exhibited by human CA II. Sulfonamides 155-167 carbonic anhydrase 2 Homo sapiens 191-196 10488246-4 1999 Potent inhibition was observed against all three isozymes but especially against CA I, which is generally 10-75 times less susceptible to inhibition by the classical sulfonamides in clinical use as compared to the other major red cell isozyme, CA II, or the membrane-bound one, CA IV. Sulfonamides 166-178 carbonic anhydrase 2 Homo sapiens 244-249 9629531-4 1998 Good inhibition of all these three CA isozymes was observed with the new compounds, but a novel finding was that the ureas/thioureas reported here had an increased affinity for the slow isozyme CA I, which generally is less sensitive to inhibition by sulfonamides when compared to the rapid isozymes CA II and IV. Sulfonamides 251-263 carbonic anhydrase 2 Homo sapiens 300-305 9865942-1 1998 X-ray crystal structures of carbonic anhydrase II (CAII) complexed with sulfonamide inhibitors illuminate the structural determinants of high affinity binding in the nanomolar regime. Sulfonamides 72-83 carbonic anhydrase 2 Homo sapiens 28-49 9865942-1 1998 X-ray crystal structures of carbonic anhydrase II (CAII) complexed with sulfonamide inhibitors illuminate the structural determinants of high affinity binding in the nanomolar regime. Sulfonamides 72-83 carbonic anhydrase 2 Homo sapiens 51-55 9692974-3 1998 CA VII has steady-state constants similar to two of the most active isozymes of carbonic anhydrase, CA II and IV; also, it is very strongly inhibited by the sulfonamides ethoxzolamide and acetazolamide, yielding the lowest Ki values measured by the exchange of 18O between CO2 and water for any of the mammalian isozymes of carbonic anhydrase. Sulfonamides 157-169 carbonic anhydrase 2 Homo sapiens 100-105 8639494-3 1996 However, E117 of human carbonic anhydrase II (CAII), which is part of the E117-119-Zn(2+) triad, is a notable exception: E117-substituted CAIIs exhibit dramatically increased kinetics of zinc complexation, and the E117Q variant exhibits enormously diminished catalytic activity and sulfonamide affinity. Sulfonamides 282-293 carbonic anhydrase 2 Homo sapiens 23-44 8639494-3 1996 However, E117 of human carbonic anhydrase II (CAII), which is part of the E117-119-Zn(2+) triad, is a notable exception: E117-substituted CAIIs exhibit dramatically increased kinetics of zinc complexation, and the E117Q variant exhibits enormously diminished catalytic activity and sulfonamide affinity. Sulfonamides 282-293 carbonic anhydrase 2 Homo sapiens 46-50 7608893-0 1995 Secondary interactions significantly removed from the sulfonamide binding pocket of carbonic anhydrase II influence inhibitor binding constants. Sulfonamides 54-65 carbonic anhydrase 2 Homo sapiens 84-105 8557623-0 1996 Unexpected binding mode of the sulfonamide fluorophore 5-dimethylamino-1-naphthalene sulfonamide to human carbonic anhydrase II. Sulfonamides 31-42 carbonic anhydrase 2 Homo sapiens 106-127 8557623-2 1996 The three-dimensional structure of human carbonic anhydrase II (CAII) complexed with the sulfonamide fluorophore 5-dimethylamino-1-naphthalene sulfonamide (dansylamide) has been determined to 2.1-A resolution by x-ray crystallographic methods. Sulfonamides 89-100 carbonic anhydrase 2 Homo sapiens 41-62 8557623-2 1996 The three-dimensional structure of human carbonic anhydrase II (CAII) complexed with the sulfonamide fluorophore 5-dimethylamino-1-naphthalene sulfonamide (dansylamide) has been determined to 2.1-A resolution by x-ray crystallographic methods. Sulfonamides 89-100 carbonic anhydrase 2 Homo sapiens 64-68 7565629-6 1995 For CA II and I, entropy changes associated with sulfonamide binding were in general modest and ranged from -5.3 to +4.1 entropy units (eu) for five of the compounds tested. Sulfonamides 49-60 carbonic anhydrase 2 Homo sapiens 4-9 7565629-8 1995 Also, the variatione in k(on) and k(off) with temperature were studied for three sulfonamides binding to CA II. Sulfonamides 81-93 carbonic anhydrase 2 Homo sapiens 105-110 8218160-2 1993 The CO2 hydrase activity and affinity for sulfonamide inhibitors of P202A CAII are virtually identical to those of wild type. Sulfonamides 42-53 carbonic anhydrase 2 Homo sapiens 74-78 7783137-2 1995 To accomplish this we have evaluated whether the FEP technique can accurately predict energetic and structural quantities relating to the inhibition of human carbonic anhydrase II (HCAII) by sulfonamides. Sulfonamides 191-203 carbonic anhydrase 2 Homo sapiens 158-179 18472783-2 1995 The new complexes are more potent CA inhibitors than the parent sulfonamides, with IC(50) values around 0.1 nM, against isozyme CA II. Sulfonamides 64-76 carbonic anhydrase 2 Homo sapiens 128-133 32891000-4 2020 These sulfonamides were generally potent inhibitors of CA II and CA I too. Sulfonamides 6-18 carbonic anhydrase 2 Homo sapiens 55-60 2111324-5 1990 CA IV resembles CA II in being a "high activity" isozyme, relatively resistant to inhibition by halide ions and sensitive to inhibition by sulfonamides. Sulfonamides 139-151 carbonic anhydrase 2 Homo sapiens 16-21 34596922-6 2022 Further, hCA II was strongly inhibited by nearly all the newly synthesized sulfonamides, while all the compounds were less effective as hCA IX and XII inhibitors compared to the standard drug acetazolamide. Sulfonamides 75-87 carbonic anhydrase 2 Homo sapiens 9-15 10354450-6 1999 These results indicate that specific interactions between the sulfonamide group on the inhibitor and the Zn(II) ion on CAII were preserved in the gas phase. Sulfonamides 62-73 carbonic anhydrase 2 Homo sapiens 119-123 34481530-0 2021 Inhibition of carbonic anhydrase II by sulfonamide derivatives. Sulfonamides 39-50 carbonic anhydrase 2 Homo sapiens 14-35 34728369-0 2021 Discovery of novel aminosaccharide-based sulfonamide derivatives as potential carbonic anhydrase II inhibitors. Sulfonamides 41-52 carbonic anhydrase 2 Homo sapiens 78-99 34324968-0 2021 Novel carbohydrate-based sulfonamide derivatives as selective carbonic anhydrase II inhibitors: Synthesis, biological and molecular docking analysis. Sulfonamides 25-36 carbonic anhydrase 2 Homo sapiens 62-83 34605430-6 2021 The method was validated using a set of sulfonamide-based inhibitors of human carbonic anhydrase II with known activity in the subnanomolar to submicromolar range. Sulfonamides 40-51 carbonic anhydrase 2 Homo sapiens 78-99 34481530-1 2021 A series of sulfonamide derivatives were synthesized, and the enzyme inhibitory activity of the synthesized compounds on carbonic anhydrase II was evaluated. Sulfonamides 12-23 carbonic anhydrase 2 Homo sapiens 121-142 6716242-0 1984 Structure-activity relationships of sulfonamide drugs and human carbonic anhydrase C: modeling of inhibitor molecules into the receptor site of the enzyme with an interactive computer graphics display. Sulfonamides 36-47 carbonic anhydrase 2 Homo sapiens 64-84 34358123-4 2021 The physiologically dominant hCA II was significantly inhibited by most of the sulphonamide with the Kis ranging between 2.4 and 4515 nM. Sulfonamides 79-91 carbonic anhydrase 2 Homo sapiens 29-35 35489270-0 2022 Targeting the interplay between MMP-2, CA II and VEGFR-2 via new sulfonamide-tethered isomeric triazole hybrids; Microwave-assisted synthesis, computational studies and evaluation. Sulfonamides 65-76 carbonic anhydrase 2 Homo sapiens 39-44 35489270-8 2022 Herein, we report concomitant inhibition of MMP-2, CA II, and VEGFR-2 via rationally designed 1,2,3- and 1,2,4-triazole hybrids bearing various sulfonamide appendages following pharmacophore hybridization strategy. Sulfonamides 144-155 carbonic anhydrase 2 Homo sapiens 51-56 35618035-1 2022 A simple and time-saving colorimetric method was developed to quantify sulfonamides (SAAs) in milk via inhibition of the human carbonic anhydrase II (hCAII)-like activity of ZIF-8 that can hydrolyze p-nitrophenyl acetate (pNPA) to p-nitrophenol (pNP), following the color change from yellow to colorless. Sulfonamides 71-83 carbonic anhydrase 2 Homo sapiens 127-148 35618035-1 2022 A simple and time-saving colorimetric method was developed to quantify sulfonamides (SAAs) in milk via inhibition of the human carbonic anhydrase II (hCAII)-like activity of ZIF-8 that can hydrolyze p-nitrophenyl acetate (pNPA) to p-nitrophenol (pNP), following the color change from yellow to colorless. Sulfonamides 71-83 carbonic anhydrase 2 Homo sapiens 150-155 2496258-11 1989 Kinetically the enzyme was similar to CA II with respect to hydrase and esterase activities and to inhibition by various sulfonamides. Sulfonamides 121-133 carbonic anhydrase 2 Homo sapiens 38-43 6716242-1 1984 We have analyzed the molecular interaction of 28 sulfonamide inhibitors with human carbonic anhydrase C (HCAC) using an interactive computer graphic display. Sulfonamides 49-60 carbonic anhydrase 2 Homo sapiens 83-103 33038795-9 2021 Furthermore, molecular modelling studies were applied to get a deep focus about the feasible affinities and binding interactions for target coumarin-sulfonamides 4, 5, 13 and 14 with the active site for CA II, IX and XII isoforms. Sulfonamides 149-161 carbonic anhydrase 2 Homo sapiens 203-208 234739-3 1975 The seven resonances observed in the histidine region of the proton magnetic resonance (pmr) spectrum of human carbonic anhydrase B and reported in the preceding paper are studied in the presence of sulfonamide, azide, cyanide, and chloride inhibitors and in metal-free, cadmium substituted, cobalt substituted, and carboxymethylated forms of the enzyme. Sulfonamides 199-210 carbonic anhydrase 2 Homo sapiens 111-131 234740-3 1975 Resonances of the histidine region of human carbonic anhydrase B have been studied by proton magnetic resonance spectroscopy in the presence of seven sulfonamide inhibitors. Sulfonamides 150-161 carbonic anhydrase 2 Homo sapiens 44-64 4212119-0 1974 Kinetics of complex formation between human carbonic anhydrase B and heterocyclic sulfonamides. Sulfonamides 82-94 carbonic anhydrase 2 Homo sapiens 44-64 32182519-3 2020 Depending on the substitution pattern at the piperidine ring, low nanomolar inhibitors were detected against hCA II, hCA IX and hCA XII, making the new class of sulfonamides of interest for various pharmacologic applications. Sulfonamides 161-173 carbonic anhydrase 2 Homo sapiens 109-115 32456080-5 2020 Quantitative structure-activity relationship (QSAR) analysis indicated an impressive KI ratio (hCA II/hCA IX) 139.1 and hCA IX inhibition constant very similar to acetazolamide (KI = 29.6 nM) for the sulfonamide derivative disubstituted with Gln. Sulfonamides 200-211 carbonic anhydrase 2 Homo sapiens 95-115 31825195-3 2020 Herein we report the synthesis of amphiphilic monomers, dimers and trimers conjugated to sulfonamide ligands via triazole rings, their assembly at aqueous-LC interfaces, and the orientational response of LCs to the inter-actions of carbonic anhydrase II (CAII) and serum albumin with the oligomer-decorated LC interfaces. Sulfonamides 89-100 carbonic anhydrase 2 Homo sapiens 232-253 31825195-3 2020 Herein we report the synthesis of amphiphilic monomers, dimers and trimers conjugated to sulfonamide ligands via triazole rings, their assembly at aqueous-LC interfaces, and the orientational response of LCs to the inter-actions of carbonic anhydrase II (CAII) and serum albumin with the oligomer-decorated LC interfaces. Sulfonamides 89-100 carbonic anhydrase 2 Homo sapiens 255-259 31825195-7 2020 We illustrate the utility of the approach by reporting (i) the relative activity of two small molecule inhibitors (6-ethoxy-2-benzothiazolesulfonamide and benzenesulfonamide) of binding of CAII to sulfonamide, and (ii) proteolytic digestion of a protein (CAII) by thermolysin. Sulfonamides 139-150 carbonic anhydrase 2 Homo sapiens 189-193 31825195-7 2020 We illustrate the utility of the approach by reporting (i) the relative activity of two small molecule inhibitors (6-ethoxy-2-benzothiazolesulfonamide and benzenesulfonamide) of binding of CAII to sulfonamide, and (ii) proteolytic digestion of a protein (CAII) by thermolysin. Sulfonamides 139-150 carbonic anhydrase 2 Homo sapiens 255-259 31911296-4 2020 Earlier, hCA-II inhibitors were designed based on the sulfonamides e.g. acetazolamide, dichlorphenamide, methazolamide, ethoxzolamide, etc. Sulfonamides 54-66 carbonic anhydrase 2 Homo sapiens 9-15 31515058-7 2019 This new non-sulfonamide class of selective inhibitors of hCA II, IX and XII over the hCA I isoform may be used for further understanding the physiological roles of some of these isoforms in various pathologies. Sulfonamides 13-24 carbonic anhydrase 2 Homo sapiens 58-76 31129502-4 2019 Most screened sulfonamides showed high potency in inhibiting hCA II, widely involved in glaucoma, epilepsy, edema, and other pathologies (Kis in the ranging from 6.32 +- 0.06 to 128.93 +- 23.11 nM). Sulfonamides 14-26 carbonic anhydrase 2 Homo sapiens 61-67 30807935-0 2019 Synthesis of sulfonamide, amide and amine hybrid pharmacophore, an entry of new class of carbonic anhydrase II inhibitors and evaluation of chemo-informatics and binding analysis. Sulfonamides 13-24 carbonic anhydrase 2 Homo sapiens 89-110 30807935-2 2019 In the current account, a hybrid pharmacophore approach was employed to design sulfonamide, amide and amine containing new series of potent carbonic anhydrase II inhibitors. Sulfonamides 79-90 carbonic anhydrase 2 Homo sapiens 140-161 30811749-2 2019 In this study, we investigated the inhibition effects of some sulfonamides on hCA I, hCA II, and AChE enzymes. Sulfonamides 62-74 carbonic anhydrase 2 Homo sapiens 85-91 31718943-3 2020 The four examined isoforms were inhibited by the prepared sulfonamides (9a-d, 11a-h, 13a-c, 15a,b, 17a,b and 21a-g) in variable degrees with KIs ranges: 94.4-4953.5 nM for hCA I, 6.9-837.6 nM for hCA II, 3.3-85.0 nM for hCA XI, and 4.4-105.0 nM for hCA XII. Sulfonamides 58-70 carbonic anhydrase 2 Homo sapiens 196-202 31136893-2 2019 In this study, we combine the anticonvulsant propriety of spyrohydantoin and the CA inhibitor moiety of benzenesulfonamide to synthesize a novel series of spyrohydantoin bearing sulfonamides with strong activity against hCA II and VII. Sulfonamides 178-190 carbonic anhydrase 2 Homo sapiens 220-234 31207328-0 2019 Chemometrical-electrochemical investigation for comparing inhibitory effects of quercetin and its sulfonamide derivative on human carbonic anhydrase II: Theoretical and experimental evidence. Sulfonamides 98-109 carbonic anhydrase 2 Homo sapiens 130-151 31207328-1 2019 This paper reports results of a valuable study on investigation of inhibitory effects of the sulfonamide derivative of quercetin (QD) on human carbonic anhydrase II (CA-II) by electrochemical and chemometrical approaches. Sulfonamides 93-104 carbonic anhydrase 2 Homo sapiens 143-164 31207328-1 2019 This paper reports results of a valuable study on investigation of inhibitory effects of the sulfonamide derivative of quercetin (QD) on human carbonic anhydrase II (CA-II) by electrochemical and chemometrical approaches. Sulfonamides 93-104 carbonic anhydrase 2 Homo sapiens 166-171