PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8667211-6 1996 Association of PGE2 or acetazolamide to NSAIDs reduced NSAID-induced activation of CA I and CA II. Acetazolamide 23-36 carbonic anhydrase 2 Homo sapiens 92-97 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. Acetazolamide 34-47 carbonic anhydrase 2 Homo sapiens 191-196 10768298-2 2000 METHODS: The inhibition constants (Ki) of TPM and acetazolamide (AZM) for CA I, CA II, CA III, CA IV, CA V, and CA VI were determined for human (HCA), rat (RCA), or mouse (MCA). Acetazolamide 50-63 carbonic anhydrase 2 Homo sapiens 80-85 10768298-2 2000 METHODS: The inhibition constants (Ki) of TPM and acetazolamide (AZM) for CA I, CA II, CA III, CA IV, CA V, and CA VI were determined for human (HCA), rat (RCA), or mouse (MCA). Acetazolamide 65-68 carbonic anhydrase 2 Homo sapiens 80-85 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. Acetazolamide 188-201 carbonic anhydrase 2 Homo sapiens 100-105 9113330-4 1997 By comparing I50 and Ki values of the compounds, it has been found that compound 1 is a more potent inhibitor than acetazolamide (b) on carbonic anhydrase II. Acetazolamide 115-128 carbonic anhydrase 2 Homo sapiens 136-157 8667211-7 1996 Indomethacin abolished the inhibitory effect of acetazolamide on CA I and CA II. Acetazolamide 48-61 carbonic anhydrase 2 Homo sapiens 74-79 8399159-6 1993 Intriguingly, Cys-199 of T199C CAII is displaced from zinc coordination by soaking crystals in high concentrations of acetazolamide. Acetazolamide 118-131 carbonic anhydrase 2 Homo sapiens 31-35 7696263-3 1995 In order to understand the structural basis of enzyme-inhibitor affinity, we now report the dissociation rate and equilibrium constants for acetazolamide and dansylamide binding to 13 variants of CAII containing substituted amino acids at position 198. Acetazolamide 140-153 carbonic anhydrase 2 Homo sapiens 196-200 7696263-7 1995 Nevertheless, the F198 side chain undergoes a significant conformation change in order to accommodate the binding of acetazolamide; the same behavior is observed for the engineered side chain of L198R CAII. Acetazolamide 117-130 carbonic anhydrase 2 Homo sapiens 201-205 7803385-7 1994 Additionally, decreases in the dissociation constant (approximately approximately 10(2)-10(5)-fold) for the transition state analog acetazolamide correlate with the decreased catalytic efficiency and increased pKa of these CAII variants. Acetazolamide 132-145 carbonic anhydrase 2 Homo sapiens 223-227 8494570-2 1993 The IC50 values of zonisamide and acetazolamide for the inhibition of erythrocyte enzymes were close to those of purified carbonic anhydrase II. Acetazolamide 34-47 carbonic anhydrase 2 Homo sapiens 122-143 34387019-7 2021 Besides, the IC 50 value of acetazolamide used as a standard was determined as h CA I, h CA II 57.75 nM, 49.50 nM, respectively. Acetazolamide 28-41 carbonic anhydrase 2 Homo sapiens 89-94 2128470-0 1990 Refined structure of the acetazolamide complex of human carbonic anhydrase II at 1.9 A. Acetazolamide 25-38 carbonic anhydrase 2 Homo sapiens 56-77 2128470-1 1990 The binding of acetazolamide to human carbonic anhydrase II (HCA II) has been investigated by X-ray crystallography. Acetazolamide 15-28 carbonic anhydrase 2 Homo sapiens 38-59 1909176-1 1991 Carbonic anhydrase III, a cytosolic enzyme found predominantly in skeletal muscle, has a turnover rate for CO2 hydration 500-fold lower and a KI for inhibition by acetazolamide 700-fold higher (at pH 7.2) than those of red cell carbonic anhydrase II. Acetazolamide 163-176 carbonic anhydrase 2 Homo sapiens 228-249 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. Acetazolamide 192-205 carbonic anhydrase 2 Homo sapiens 9-15 31847904-13 2019 CAII inhibition with acetazolamide minimally reduced tumor angiogenesis in vivo. Acetazolamide 21-34 carbonic anhydrase 2 Homo sapiens 0-4 3932950-5 1985 These findings indicate that CA II-deficient patients, who lack detectable CA II in their erythrocytes, still expressed an acetazolamide-inhibitable CA activity in their kidneys. Acetazolamide 123-136 carbonic anhydrase 2 Homo sapiens 29-34 806403-2 1975 The levels of carbonic anhydrase B were determined in normal subjects, patients with hyperthyroidism, and patients with chronic obstructive lung disease and patients with epilepsy under treatment with acetazolamide, using the rapid assay method of single radial immunodiffusion. Acetazolamide 201-214 carbonic anhydrase 2 Homo sapiens 14-34 806403-7 1975 In patients treated with acetazolamide, the "true" specific activity of the carbonic anhydrase B (carbonic anhydrase B-dependent esterase activity/total carbonic anhydrase B protein) decreased remarkably. Acetazolamide 25-38 carbonic anhydrase 2 Homo sapiens 76-96 806403-7 1975 In patients treated with acetazolamide, the "true" specific activity of the carbonic anhydrase B (carbonic anhydrase B-dependent esterase activity/total carbonic anhydrase B protein) decreased remarkably. Acetazolamide 25-38 carbonic anhydrase 2 Homo sapiens 98-118 806403-7 1975 In patients treated with acetazolamide, the "true" specific activity of the carbonic anhydrase B (carbonic anhydrase B-dependent esterase activity/total carbonic anhydrase B protein) decreased remarkably. Acetazolamide 25-38 carbonic anhydrase 2 Homo sapiens 98-118 33249154-8 2021 Compound 3b was found significantly active against carbonic anhydrase-II with an IC50 of 16.5 +- 0.92 muM (acetazolamide; IC50 = 18.2 +- 1.23 muM). Acetazolamide 107-120 carbonic anhydrase 2 Homo sapiens 51-72 33085484-4 2020 Very potent pan-inhibitors with nanomolar potency against CA IX and sub-nanomolar potency against CA II and CA IV, and with potency against CA I one order of magnitude better than the parent acetazolamide 1 were also identified in this study, together with compounds that displayed selectivity against membrane-bound CA IV. Acetazolamide 191-204 carbonic anhydrase 2 Homo sapiens 98-103 31911296-4 2020 Earlier, hCA-II inhibitors were designed based on the sulfonamides e.g. acetazolamide, dichlorphenamide, methazolamide, ethoxzolamide, etc. Acetazolamide 72-85 carbonic anhydrase 2 Homo sapiens 9-15 31555842-6 2019 A proposal that reaction of acetazolamide with carbonic anhydrase II be used as a comparison standard for testing ITCs and procedures is problematic because the binding constant is too large and for several other reasons discussed in the paper. Acetazolamide 28-41 carbonic anhydrase 2 Homo sapiens 47-68 31667562-4 2019 The design of the extraction tool is based on noncovalent and reversible interaction between AAZ and CAII that is immobilized on the SPME extraction phase. Acetazolamide 93-96 carbonic anhydrase 2 Homo sapiens 101-105 31667562-5 2019 Using this approach, we showed a 330% rise in extracted AAZ signal intensity compared to a control, which was performed in the absence of CAII. Acetazolamide 56-59 carbonic anhydrase 2 Homo sapiens 138-142 31345748-3 2019 Most of the derivatives exhibited higher potency than acetazolamide as inhibitors of the purified hCAII, IX and XII isoforms. Acetazolamide 54-67 carbonic anhydrase 2 Homo sapiens 98-103 30535510-3 2019 Here, the repeatability, precision, and accuracy of the measurement of the affinity and the change in enthalpy upon acetazolamide (AZM) interaction with human carbonic anhydrase II (CA II) are discussed based on the measurements using several ITC instruments. Acetazolamide 116-129 carbonic anhydrase 2 Homo sapiens 159-180 30597695-5 2019 In contrast, acetazolamide clinically used as CA inhibitor showed K i value of 1054.38 +- 207.33 nM against hCA I, and 983.78 +- 251.08 nM against hCA II, respectively. Acetazolamide 13-26 carbonic anhydrase 2 Homo sapiens 147-153 30535510-3 2019 Here, the repeatability, precision, and accuracy of the measurement of the affinity and the change in enthalpy upon acetazolamide (AZM) interaction with human carbonic anhydrase II (CA II) are discussed based on the measurements using several ITC instruments. Acetazolamide 116-129 carbonic anhydrase 2 Homo sapiens 182-187 30535510-3 2019 Here, the repeatability, precision, and accuracy of the measurement of the affinity and the change in enthalpy upon acetazolamide (AZM) interaction with human carbonic anhydrase II (CA II) are discussed based on the measurements using several ITC instruments. Acetazolamide 131-134 carbonic anhydrase 2 Homo sapiens 159-180 30535510-3 2019 Here, the repeatability, precision, and accuracy of the measurement of the affinity and the change in enthalpy upon acetazolamide (AZM) interaction with human carbonic anhydrase II (CA II) are discussed based on the measurements using several ITC instruments. Acetazolamide 131-134 carbonic anhydrase 2 Homo sapiens 182-187 30535510-5 2019 To obtain the confidence intervals (CI) of the G and DeltaH of AZM binding to CA II, the binding reaction was repeated numerous times at the optimal concentration of 10 microM and 25 C temperature. Acetazolamide 64-67 carbonic anhydrase 2 Homo sapiens 79-84 30153589-9 2018 2,2"-((6-((4-sulfamoylphenethyl)amino)-1,3,5-triazine-2,4-diyl)bis(imino))disuccinic acid demonstrated highest selectivity to the tumor-associated isoform hCA IX over off-target isozymes, with impressive KI ratio (hCA II/hCA IX) 213.9 and inhibition constant equal to acetazolamide (KI = 25.8 nM). Acetazolamide 268-281 carbonic anhydrase 2 Homo sapiens 214-234 29584404-5 2018 These advantages are demonstrated with the measurements of binding of acetazolamide (222.2 Da) to histidine-tagged human carbonic anhydrase II (his-tagged HCA). Acetazolamide 70-83 carbonic anhydrase 2 Homo sapiens 121-142 29197732-4 2018 The most active tested compounds proved to be potent inhibitors with Ki values equal to that of the well-known inhibitor acetazolamide (AAZ), that lacks selectivity over ubiquitous hCA I and hCA II. Acetazolamide 121-134 carbonic anhydrase 2 Homo sapiens 191-197 28792233-7 2018 On the other hand, acetazolamide, clinically used drug, showed a Ki value of 977.77 +- 227.4 nM against CA I, and 904.47 +- 106.3 nM against CA II, respectively. Acetazolamide 19-32 carbonic anhydrase 2 Homo sapiens 141-146 29283199-6 2018 On the other hand, acetazolamide clinically used as CA inhibitor showed Ki value of 13.9 +- 5.1 nM against hCA I and 18.1 +- 8.5 nM against hCA II. Acetazolamide 19-32 carbonic anhydrase 2 Homo sapiens 140-146 29197732-4 2018 The most active tested compounds proved to be potent inhibitors with Ki values equal to that of the well-known inhibitor acetazolamide (AAZ), that lacks selectivity over ubiquitous hCA I and hCA II. Acetazolamide 136-139 carbonic anhydrase 2 Homo sapiens 191-197 28100082-6 2017 Moreover, acetazolamide showed Ki values of 43.69 +- 6.44 nM against hCA I and 31.67 +- 8.39 nM against hCA II. Acetazolamide 10-23 carbonic anhydrase 2 Homo sapiens 104-110 29149534-4 2018 On the other hand, acetazolamide, a clinically used molecule, utilized as CA inhibitor, obtained a Ki value of 1246.7 nM against hCA I and 1407.6 nM against hCA II. Acetazolamide 19-32 carbonic anhydrase 2 Homo sapiens 157-163 28544359-7 2017 On the other hand, acetazolamide showed Ki value of 482.63 +- 56.20 nM against hCA I, and 1019.60 +- 163.70 nM against hCA II. Acetazolamide 19-32 carbonic anhydrase 2 Homo sapiens 119-125 28943245-1 2017 The small molecule inhibitor acetazolamide (AZM) was conjugated to a set of designed polypeptides and the resulting conjugates were evaluated for their affinity to Human Carbonic Anhydrase II (HCA II) using surface plasmon resonance. Acetazolamide 29-42 carbonic anhydrase 2 Homo sapiens 170-191 28943245-1 2017 The small molecule inhibitor acetazolamide (AZM) was conjugated to a set of designed polypeptides and the resulting conjugates were evaluated for their affinity to Human Carbonic Anhydrase II (HCA II) using surface plasmon resonance. Acetazolamide 44-47 carbonic anhydrase 2 Homo sapiens 170-191 28117934-5 2017 Additionally, acetazolamide (AZA), clinically used as a CA inhibitor, with a Ki value of 883.68 +- 121.27 nM in hCA I and 1008.66 +- 144.70 nM in hCA II. Acetazolamide 14-27 carbonic anhydrase 2 Homo sapiens 146-152 28117934-5 2017 Additionally, acetazolamide (AZA), clinically used as a CA inhibitor, with a Ki value of 883.68 +- 121.27 nM in hCA I and 1008.66 +- 144.70 nM in hCA II. Acetazolamide 29-32 carbonic anhydrase 2 Homo sapiens 146-152 27780313-7 2017 On the other hand, acetazolamide clinically used as CA inhibitor, showed Ki value of 19.92 nM against hCA I and 33.60 nM against hCA II, respectively. Acetazolamide 19-32 carbonic anhydrase 2 Homo sapiens 129-135 28110167-6 2017 The optimizations of both methods were performed using a reference compound, i.e. acetazolamide, which affinity for hCAII has previously been demonstrated. Acetazolamide 82-95 carbonic anhydrase 2 Homo sapiens 116-121 27984137-10 2017 On the other hand, acetazolamide clinically used as CA inhibitor, shoed Ki value of 594.11nM against hCA I, and 120.68nM against hCA II, respectively. Acetazolamide 19-32 carbonic anhydrase 2 Homo sapiens 129-135 26985691-7 2016 Acetazolamide, which was clinically used carbonic anhydrase (CA) inhibitor demonstrated Ki values of 281.33 nM for hCA I and 9.07 nM for hCA II. Acetazolamide 0-13 carbonic anhydrase 2 Homo sapiens 137-143 27717855-3 2016 The binding between carbonic anhydrase II and acetazolamide was measured by four ITC instruments - PEAQ-ITC, iTC200, VP-ITC, and MCS-ITC and the standard deviation of DeltaG and DeltaH was determined. Acetazolamide 46-59 carbonic anhydrase 2 Homo sapiens 20-41 27050248-5 2016 On the other hand, acetazolamide clinically used as CA inhibitor, showed Ki value of 281.33 nM against hCA I, and 202.70 nM against hCA II. Acetazolamide 19-32 carbonic anhydrase 2 Homo sapiens 132-138 27579806-4 2016 All compounds synthesized showed superior CA inhibitory activity than the reference compound acetazolamide on hCA I, and II isoenzymes, with inhibition constants in the range of 26.5-55.5 nM against hCA I and of 18.9-28.8 nM against hCA II, respectively. Acetazolamide 93-106 carbonic anhydrase 2 Homo sapiens 233-239 28461893-4 2016 Presented in this article, along with only the second neutron structure of a clinical drug-bound hCA, is an in-depth structural comparison and analyses of differences in hydrogen-bonding network, water-molecule orientation and solvent displacement that take place upon the binding of AZM and MZM in the active site of hCA II. Acetazolamide 284-287 carbonic anhydrase 2 Homo sapiens 318-324 28461893-7 2016 This study not only allows a direct comparison of the hydrogen bonding, protonation states and solvent orientation/displacement of AZM and MZM, but also shows the significant effect that the methyl derivative has on the solvent organization in the hCA II active site. Acetazolamide 131-134 carbonic anhydrase 2 Homo sapiens 248-254 27232456-0 2016 Molecular dynamics study of human carbonic anhydrase II in complex with Zn(2+) and acetazolamide on the basis of all-atom force field simulations. Acetazolamide 83-96 carbonic anhydrase 2 Homo sapiens 34-55 27232456-4 2016 We compute the hydration free energy of Zn(2+), the characteristics of hCAII-Zn(2+) complexation, and the absolute free energy of binding acetazolamide to the hCAII-Zn(2+) complex. Acetazolamide 138-151 carbonic anhydrase 2 Homo sapiens 159-164 27075164-5 2016 On the other hand, acetazolamide and dorzolamide clinically used as CA inhibitors, showed Ki value of 170.34 and 129.26 nM against hCA I, and 115.43 and 135.67 nM against hCA II, respectively. Acetazolamide 19-32 carbonic anhydrase 2 Homo sapiens 171-177 24682061-4 2014 Acetazolamide (5-acetamido-1,3,4-thiadiazole-2-sulfonamide) AAZ, a clinically used in CAII inhibition has also been investigated as standard inhibitor. Acetazolamide 0-13 carbonic anhydrase 2 Homo sapiens 86-90 26105196-4 2015 Against hCA II, all of the tested compounds were better than the standard drug especially compounds 6c, 6d, 7c and 7d (Ki = 1.1-1.7 nM) were many fold better inhibitors than AZA (Ki = 12.1 nM). Acetazolamide 174-177 carbonic anhydrase 2 Homo sapiens 8-14 25581127-2 2015 By appending dual tail groups onto the par excellence CA inhibitor acetazolamide, compounds that may interact with the distinct hydrophobic and hydrophilic halves of the CA II active site were prepared. Acetazolamide 67-80 carbonic anhydrase 2 Homo sapiens 170-175 26041446-7 2015 Inhibition of endogenous CAII activity with acetazolamide significantly decreased NHE3 activity, indicating that CAII activates NHE3. Acetazolamide 44-57 carbonic anhydrase 2 Homo sapiens 25-29 25456084-3 2014 Against hCA II, all the compounds showed excellent to moderate inhibition with Ki values of compounds 5a, 5d, 5f, 6a-6f, 8d and 8f lower than 12nM (Ki of AZA). Acetazolamide 154-157 carbonic anhydrase 2 Homo sapiens 8-14 23633596-0 2013 Effects of cryoprotectants on the structure and thermostability of the human carbonic anhydrase II-acetazolamide complex. Acetazolamide 99-112 carbonic anhydrase 2 Homo sapiens 77-98 23633596-2 2013 Here, a case study of the effects of cryoprotectants on the kinetics of carbonic anhydrase II (CA II) and its inhibition by the clinically used inhibitor acetazolamide (AZM) is presented. Acetazolamide 154-167 carbonic anhydrase 2 Homo sapiens 72-93 23633596-2 2013 Here, a case study of the effects of cryoprotectants on the kinetics of carbonic anhydrase II (CA II) and its inhibition by the clinically used inhibitor acetazolamide (AZM) is presented. Acetazolamide 154-167 carbonic anhydrase 2 Homo sapiens 95-100 23633596-2 2013 Here, a case study of the effects of cryoprotectants on the kinetics of carbonic anhydrase II (CA II) and its inhibition by the clinically used inhibitor acetazolamide (AZM) is presented. Acetazolamide 169-172 carbonic anhydrase 2 Homo sapiens 72-93 23633596-2 2013 Here, a case study of the effects of cryoprotectants on the kinetics of carbonic anhydrase II (CA II) and its inhibition by the clinically used inhibitor acetazolamide (AZM) is presented. Acetazolamide 169-172 carbonic anhydrase 2 Homo sapiens 95-100 23633596-3 2013 Comparative studies of crystal structure, kinetics, inhibition and thermostability were performed on CA II and its complex with AZM in the presence of either GOL or sucrose. Acetazolamide 128-131 carbonic anhydrase 2 Homo sapiens 101-106 22145674-3 2013 The compounds displayed relatively strong actions on hCA II, in the same range as the clinically used sulfonamidesethoxzolamide, zonisamide and acetazolamide. Acetazolamide 144-157 carbonic anhydrase 2 Homo sapiens 53-59 18295485-2 2008 The agents were very weak inhibitors of isozymes CA II and CA IX, but unexpectedly, strongly influenced the binding of the low nanomolar sulfonamide inhibitor acetazolamide (5-acetamido-1,3,4-thiadiazole-2-sulfonamide). Acetazolamide 159-172 carbonic anhydrase 2 Homo sapiens 49-54 22928733-0 2012 Neutron diffraction of acetazolamide-bound human carbonic anhydrase II reveals atomic details of drug binding. Acetazolamide 23-36 carbonic anhydrase 2 Homo sapiens 49-70 19851004-0 2009 High-resolution structure of human carbonic anhydrase II complexed with acetazolamide reveals insights into inhibitor drug design. Acetazolamide 72-85 carbonic anhydrase 2 Homo sapiens 35-56 19851004-1 2009 The crystal structure of human carbonic anhydrase II (CA II) complexed with the inhibitor acetazolamide (AZM) has been determined at 1.1 A resolution and refined to an R(cryst) of 11.2% and an R(free) of 14.7%. Acetazolamide 90-103 carbonic anhydrase 2 Homo sapiens 31-52 19851004-1 2009 The crystal structure of human carbonic anhydrase II (CA II) complexed with the inhibitor acetazolamide (AZM) has been determined at 1.1 A resolution and refined to an R(cryst) of 11.2% and an R(free) of 14.7%. Acetazolamide 90-103 carbonic anhydrase 2 Homo sapiens 54-59 19851004-1 2009 The crystal structure of human carbonic anhydrase II (CA II) complexed with the inhibitor acetazolamide (AZM) has been determined at 1.1 A resolution and refined to an R(cryst) of 11.2% and an R(free) of 14.7%. Acetazolamide 105-108 carbonic anhydrase 2 Homo sapiens 31-52 19851004-1 2009 The crystal structure of human carbonic anhydrase II (CA II) complexed with the inhibitor acetazolamide (AZM) has been determined at 1.1 A resolution and refined to an R(cryst) of 11.2% and an R(free) of 14.7%. Acetazolamide 105-108 carbonic anhydrase 2 Homo sapiens 54-59 19851004-2 2009 As observed in previous CA II-inhibitor complexes, AZM binds directly to the zinc and makes several key interactions with active-site residues. Acetazolamide 51-54 carbonic anhydrase 2 Homo sapiens 24-29 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. Acetazolamide 151-164 carbonic anhydrase 2 Homo sapiens 71-77 17614791-9 2007 Moreover, its affinity for acetazolamide was high, comparable with that of the most efficient human isoenzyme, CA II (in the low nanomolar range). Acetazolamide 27-40 carbonic anhydrase 2 Homo sapiens 111-116 12372813-3 2002 DRA-mediated bicarbonate transport activity of 18 +/- 1 mM H+ equivalents/min was inhibited 53 +/- 2% by 100 mM of the CAII inhibitor, acetazolamide, but was unaffected by the membrane-impermeant carbonic anhydrase inhibitor, 1-[5-sulfamoyl-1,3,4-thiadiazol-2-yl-(aminosulfonyl-4-phenyl)]-2,6-dimethyl-4-phenyl-pyridinium perchlorate. Acetazolamide 135-148 carbonic anhydrase 2 Homo sapiens 119-123 15183767-2 2004 Acetazolamide (222 g/mol) binding to carbonic anhydrase II (CAII; 30000 Da) was chosen as a model system. Acetazolamide 0-13 carbonic anhydrase 2 Homo sapiens 37-58 15183767-2 2004 Acetazolamide (222 g/mol) binding to carbonic anhydrase II (CAII; 30000 Da) was chosen as a model system. Acetazolamide 0-13 carbonic anhydrase 2 Homo sapiens 60-64 14611844-5 2003 Similarly to hCA II, the mitochondrial isozymes show micro-nanomolar affinity for sulfonamides such as sulfanilamide and acetazolamide. Acetazolamide 121-134 carbonic anhydrase 2 Homo sapiens 13-19 12767917-4 2003 These compounds therefore have a similar CAII inhibitory potency to that of acetazolamide (IC(50)=25 nM), a known hCAII inhibitor. Acetazolamide 76-89 carbonic anhydrase 2 Homo sapiens 114-119 15110853-3 2004 Some of these derivatives showed good inhibitory potency against two human CA isozymes involved in important physiological processes, CA I, and CA II, of the same order of magnitude as the clinically used drugs acetazolamide and methazolamide. Acetazolamide 211-224 carbonic anhydrase 2 Homo sapiens 144-149 12429455-5 2002 Furthermore, oral ACZ is reported to be more physiologically effective than 2% dorzolamide hydrochloride administered topically, even though in isolated tissues dorzolamide appears to be the most active as it shows the lowest IC(50) values for CA-II and CA-IV [M.F. Acetazolamide 18-21 carbonic anhydrase 2 Homo sapiens 244-249 11430635-7 2001 Acetazolamide, a specific inhibitor of CA, reduces the activity of CA I and CA II from red cells. Acetazolamide 0-13 carbonic anhydrase 2 Homo sapiens 76-81 12027220-4 2002 NBC1 is directly stimulated by carbonic anhydrase (CA) II, indicating that its inhibition by CA inhibitor acetazolamide is, in part, direct and due to the inhibition of CAII which in turn binds to the carboxy terminal tail of NBC1. Acetazolamide 106-119 carbonic anhydrase 2 Homo sapiens 31-57 12027220-4 2002 NBC1 is directly stimulated by carbonic anhydrase (CA) II, indicating that its inhibition by CA inhibitor acetazolamide is, in part, direct and due to the inhibition of CAII which in turn binds to the carboxy terminal tail of NBC1. Acetazolamide 106-119 carbonic anhydrase 2 Homo sapiens 169-173 11606574-4 2001 AE1-mediated chloride/bicarbonate exchange was reduced 50-60% by inhibition of endogenous carbonic anhydrase with acetazolamide, which indicates that CAII activity is required for full anion transport activity. Acetazolamide 114-127 carbonic anhydrase 2 Homo sapiens 150-154 11875254-7 2001 Treatment of AE1-transfected cells with acetazolamide, a CAII inhibitor, almost fully inhibited anion exchange activity, indicating that endogenous CAII activity is essential for transport. Acetazolamide 40-53 carbonic anhydrase 2 Homo sapiens 57-61 11875254-7 2001 Treatment of AE1-transfected cells with acetazolamide, a CAII inhibitor, almost fully inhibited anion exchange activity, indicating that endogenous CAII activity is essential for transport. Acetazolamide 40-53 carbonic anhydrase 2 Homo sapiens 148-152 12138085-7 2002 The CAII inhibitor acetazolamide significantly decreased the H(+) transport rate of NHE1 and transfection with a dominant negative CAII inhibited NHE1 activity. Acetazolamide 19-32 carbonic anhydrase 2 Homo sapiens 4-8