C11804

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Showing 1-30 of 38 results for "C11804" within Papers

Carbonic anhydrase inhibitors: inhibition of the beta-class enzyme from the yeast Saccharomyces cerevisiae with sulfonamides and sulfamates.

Semra Isik et al.

Bioorganic & medicinal chemistry, 17(3), 1158-1163 (2009-01-07)

The protein encoded by the Nce103 gene of Saccharomyces cerevisiae, a beta-carbonic anhydrase (CA, EC 4.2.1.1) designated as scCA, has been cloned, purified, characterized kinetically and investigated for its inhibition with a series of sulfonamides and one sulfamate. The enzyme

Synthesis and structure-activity relationships of novel benzene sulfonamides with potent binding affinity for bovine carbonic anhydrase II.

Sally-Ann Poulsen et al.

Bioorganic & medicinal chemistry letters, 15(24), 5429-5433 (2005-10-11)

This manuscript reports the identification of a novel series of mono- and bis- benzene sulfonamides with potent binding affinity for bovine carbonic anhydrase II (bCAII). These compounds exhibited nanomolar equilibrium dissociation constants with K(i)'s ranging from 4.7 to 9.3nM. All

Molecular cloning, characterization, and inhibition studies of the Rv1284 beta-carbonic anhydrase from Mycobacterium tuberculosis with sulfonamides and a sulfamate.

Tomoko Minakuchi et al.

Journal of medicinal chemistry, 52(8), 2226-2232 (2009-03-26)

The beta-carbonic anhydrase (CA, EC 4.2.1.1) encoded by the gene Rv1284 (mtCA 1) of Mycobacterium tuberculosis shows appreciable catalytic activity for CO(2) hydration, with a k(cat) of 3.9 x 10(5) s(-1) and a k(cat)/K(m) of 3.7 x 10(7) M(-1) s(-1).

Carbonic anhydrase inhibitors. Inhibition of the transmembrane isozyme XII with sulfonamides-a new target for the design of antitumor and antiglaucoma drugs?

Daniela Vullo et al.

Bioorganic & medicinal chemistry letters, 15(4), 963-969 (2005-02-03)

The inhibition of a newly cloned human carbonic anhydrase (CA, EC 4.2.1.1), isozyme XII (hCA XII), has been investigated with a series of sulfonamides, including some clinically used derivatives (acetazolamide, methazolamide, ethoxzolamide, dichlorophenamide, dorzolamide, brinzolamide, benzolamide, and sulpiride, or indisulam

Carbonic anhydrase inhibitors. The mitochondrial isozyme VB as a new target for sulfonamide and sulfamate inhibitors.

Isao Nishimori et al.

Journal of medicinal chemistry, 48(24), 7860-7866 (2005-11-24)

A lately discovered carbonic anhydrase (hCA, EC 4.2.1.1), the mitochondrial hCA VB, was cloned, expressed, and purified. Kinetic parameters proved it to be 3.37 times more effective than hCA VA as a catalyst for the physiological reaction, with kcat =

Anti-mycobacterial activity of a bis-sulfonamide.

Brendan L Wilkinson et al.

Bioorganic & medicinal chemistry letters, 17(5), 1355-1357 (2007-01-30)

A bis-arylsulfonamide, 7, has been identified that exhibits growth inhibition of Mycobacterium smegmatis at less than 25 microg/mL, but has no such activity against Escherichia coli or Staphylococcus aureus. A closely related bis-arylsulfonamide (8) was much less active, but was

Carbonic anhydrase inhibitors: inhibition of the transmembrane isozyme XIV with sulfonamides.

Isao Nishimori et al.

Bioorganic & medicinal chemistry letters, 15(17), 3828-3833 (2005-07-26)

The inhibition of the last human carbonic anhydrase (CA, EC 4.2.1.1) isozyme (hCA XIV) discovered has been investigated with a series of sulfonamides, including some clinically used derivatives (acetazolamide, methazolamide, ethoxzolamide, dichlorophenamide, dorzolamide, brinzolamide, benzolamide, and zonisamide), as well as

Cloning, characterization, and inhibition studies of a beta-carbonic anhydrase from Brucella suis.

Pascale Joseph et al.

Journal of medicinal chemistry, 53(5), 2277-2285 (2010-02-18)

A beta-carbonic anhydrase (CA, EC 4.2.1.1) from the bacterial pathogen Brucella suis, bsCA 1, has been cloned, purified, and characterized kinetically. bsCA 1 has appreciable activity as catalyst for the hydration of CO(2) to bicarbonate, with a k(cat) of 6.4

Furan-based inhibitors of pyruvate dehydrogenase: SAR study, biochemical evaluation and computational analysis

AHY Chan

Organic & Biomolecular Chemistry, 21, 1755-1763 (2023)

Cloning, characterization and sulfonamide inhibition studies of an α-carbonic anhydrase from the living fossil sponge Astrosclera willeyana.

Anna Ohradanova et al.

Bioorganic & medicinal chemistry, 20(4), 1403-1410 (2012-01-31)

The α-carbonic anhydrase (CA, EC 4.2.1.1) Astrosclerin-3 previously isolated from the living fossil sponge Astrosclera willeyana (Jackson et al., Science 2007, 316, 1893), was cloned, kinetically characterized and investigated for its inhibition properties with sulfonamides and sulfamates. Astrosclerin-3 has a

Polysubstrates: substances that interact with renal contraluminal PAH, sulfate, and NMeN transport: sulfamoyl-, sulfonylurea-, thiazide- and benzeneamino-carboxylate (nicotinate) compounds.

K J Ullrich et al.

The Journal of pharmacology and experimental therapeutics, 269(2), 684-692 (1994-05-01)

Some N-containing xenobiotics were recently shown to behave as bisubstrates; that is, they interact with and are transported by both the contraluminal transport system for organic anions (PAH) and the contraluminal transport system for organic cations (NMeN). Thus we determined

Carbonic anhydrase inhibitors. Characterization and inhibition studies of the most active beta-carbonic anhydrase from Mycobacterium tuberculosis, Rv3588c.

Fabrizio Carta et al.

Bioorganic & medicinal chemistry letters, 19(23), 6649-6654 (2009-10-23)

The Rv3588c gene product of Mycobacterium tuberculosis, a beta-carbonic anhydrase (CA, EC 4.2.1.1) denominated here mtCA 2, shows the highest catalytic activity for CO(2) hydration (k(cat) of 9.8 x 10(5)s(-1), and k(cat)/K(m) of 9.3 x 10(7)M(-1)s(-1)) among the three beta-CAs

Carbonic anhydrase inhibitors. Inhibition studies with anions and sulfonamides of a new cytosolic enzyme from the scleractinian coral Stylophora pistillata.

Anthony Bertucci et al.

Bioorganic & medicinal chemistry letters, 21(2), 710-714 (2011-01-07)

The catalytic activity and the inhibition of a new coral carbonic anhydrase (CA, EC 4.2.1.1), from the scleractinian coral Stylophora pistillata, STPCA-2, has been investigated. STPCA-2 has high catalytic activity for the physiological reaction being less sensitive to anion and

Carbonic anhydrase inhibitors. DNA cloning, characterization, and inhibition studies of the human secretory isoform VI, a new target for sulfonamide and sulfamate inhibitors.

Isao Nishimori et al.

Journal of medicinal chemistry, 50(2), 381-388 (2007-01-19)

The secretory isozyme of human carbonic anhydrase (hCA, EC 4.2.1.1), hCA VI, has been cloned, expressed, and purified in a bacterial expression system. The kinetic parameters for the CO2 hydration reaction proved hCA VI to possess a kcat of 3.4

Cloning, expression, post-translational modifications and inhibition studies on the latest mammalian carbonic anhydrase isoform, CA XV.

Mika Hilvo et al.

Journal of medicinal chemistry, 52(3), 646-654 (2009-02-06)

We have cloned and purified to homogeneity the latest member of the mammalian alpha-carbonic anhydrase (CA, EC 4.2.1.1) family, the mouse CA XV (mCA XV) protein. An investigation on the post-translational modifications of the enzyme has also been performed. The

Sensitivity of cAMP-stimulated salt secretion in shark rectal gland to "loop" diuretics.

H C Palfrey et al.

The American journal of physiology, 246(3 Pt 1), C242-C246 (1984-03-01)

The secretory response of isolated perfused shark rectal gland was characterized with respect to its inhibition by a chemically related series of 5-sulfamoylbenzoic acid derivatives and certain phenoxyacetic acid derivatives. Maximal fluid and salt secretion was elicited with dibutyryl adenosine

Optimizing Multiple Analyte Injections in Surface Plasmon Resonance Biosensors with Analytes having Different Refractive Index Increments.

Massinissa Si Mehand et al.

Scientific reports, 5, 15855-15855 (2015-10-31)

Surface plasmon resonance-based biosensors have been successfully applied to the study of the interactions between macromolecules and small molecular weight compounds. In an effort to increase the throughput of these SPR-based experiments, we have already proposed to inject multiple compounds

A new β-carbonic anhydrase from Brucella suis, its cloning, characterization, and inhibition with sulfonamides and sulfamates, leading to impaired pathogen growth.

Pascale Joseph et al.

Bioorganic & medicinal chemistry, 19(3), 1172-1178 (2011-01-22)

A β-carbonic anhydrase (CA, EC 4.2.1.1) from the bacterial pathogen Brucella suis, bsCA II, has been cloned, purified, and characterized kinetically. bsCA II showed high catalytic activity for the hydration of CO(2) to bicarbonate, with a k(cat) of 1.1×10(6), and

Carbonic anhydrase inhibitors: DNA cloning and inhibition studies of the alpha-carbonic anhydrase from Helicobacter pylori, a new target for developing sulfonamide and sulfamate gastric drugs.

Isao Nishimori et al.

Journal of medicinal chemistry, 49(6), 2117-2126 (2006-03-17)

We have cloned and sequenced Helicobacter pylori alpha-class carbonic anhydrase (hpCA) from patients with different gastric mucosal lesions, including gastritis (n=15), ulcer (n=6), and cancer (n=16). Although several polymorphisms were newly identified such as 12Ala, 13Thr, 16Ile, and 168Phe, there

Chiral separation of new sulfonamide derivatives and evaluation of their enantioselective affinity for human carbonic anhydrase II by microscale thermophoresis and surface plasmon resonance.

Tiphaine Rogez-Florent et al.

Journal of pharmaceutical and biomedical analysis, 137, 113-122 (2017-01-23)

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). The first step consisted in

A QSAR study on relationship between structure of sulfonamides and their carbonic anhydrase inhibitory activity using the eigenvalue (EVA) method.

Oral Oltulu et al.

European journal of medicinal chemistry, 44(9), 3439-3444 (2009-03-24)

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. For each of the compounds, geometry optimization and frequency calculations

Novel synthesized SLC-0111 thiazole and thiadiazole analogues: Determination of their carbonic anhydrase inhibitory activity and molecular modeling studies

MF Abo-Ashour

Bioorganic Chemistry, 87, 794-802 (2019)

Carbonic anhydrase inhibitors: cloning and sulfonamide inhibition studies of a carboxyterminal truncated alpha-carbonic anhydrase from Helicobacter pylori.

Isao Nishimori et al.

Bioorganic & medicinal chemistry letters, 16(8), 2182-2188 (2006-02-07)

A library of sulfonamides/sulfamates has been investigated for the inhibition of the carboxyterminal truncated form of the alpha-carbonic anhydrase (CA, EC 4.2.1.1) isolated from the gastric pathogen Helicobacter pylori (hpCA). This enzyme, incorporating 202 amino acid residues, showed a catalytic

Carbonic anhydrase inhibitors: the beta-carbonic anhydrase from Helicobacter pylori is a new target for sulfonamide and sulfamate inhibitors.

Isao Nishimori et al.

Bioorganic & medicinal chemistry letters, 17(13), 3585-3594 (2007-05-08)

DNA clones for the beta-class carbonic anhydrase (CA, EC 4.2.1.1) of Helicobactor pylori (hpbetaCA) were obtained. A recombinant hpbetaCA protein lacking the N-terminal 15-amino acid residues was produced and purified, representing a catalytically efficient CA. hpbetaCA was strongly inhibited (K(I)s

Carbonic anhydrase inhibitors. Inhibition of the human cytosolic isozyme VII with aromatic and heterocyclic sulfonamides.

Daniela Vullo et al.

Bioorganic & medicinal chemistry letters, 15(4), 971-976 (2005-02-03)

The inhibition of a newly cloned human carbonic anhydrase (CA, EC 4.2.1.1), isozyme VII (hCA VII), has been investigated with a series of aromatic and heterocyclic sulfonamides, including some of the clinically used derivatives (acetazolamide, methazolamide, ethoxzolamide, dichlorophenamide, dorzolamide, brinzolamide

A Customizable Flow Injection System for Automated, High Throughput, and Time Sensitive Ion Mobility Spectrometry and Mass Spectrometry Measurements.

Daniel J Orton et al.

Analytical chemistry, 90(1), 737-744 (2017-11-22)

To better understand disease conditions and environmental perturbations, multiomic studies combining proteomic, lipidomic, and metabolomic analyses are vastly increasing in popularity. In a multiomic study, a single sample is typically extracted in multiple ways, and various analyses are performed using

Saccharin: para forms of some impurities are not mutagenic in Salmonella typhimurium.

F Poncelet et al.

Food and cosmetics toxicology, 18(4), 453-453 (1980-08-01)

Carbonic anhydrase inhibitors. Inhibition and homology modeling studies of the fungal beta-carbonic anhydrase from Candida albicans with sulfonamides.

Alessio Innocenti et al.

Bioorganic & medicinal chemistry, 17(13), 4503-4509 (2009-05-20)

The beta-carbonic anhydrase (CA, EC 4.2.1.1) from the fungal pathogen Candida albicans (Nce103) is involved in a CO(2) sensing pathway critical for the pathogen life cycle and amenable to drug design studies. Herein we report an inhibition study of Nce103

Probenecid inhibits the human bitter taste receptor TAS2R16 and suppresses bitter perception of salicin.

Tiffani A Greene et al.

PloS one, 6(5), e20123-e20123 (2011-06-02)

Bitter taste stimuli are detected by a diverse family of G protein-coupled receptors (GPCRs) expressed in gustatory cells. Each bitter taste receptor (TAS2R) responds to an array of compounds, many of which are toxic and can be found in nature.

Carbonic anhydrase inhibitors: synthesis and inhibition of cytosolic/membrane-associated carbonic anhydrase isozymes I, II, and IX with sulfonamides incorporating hydrazino moieties.

Jean-Yves Winum et al.

Journal of medicinal chemistry, 48(6), 2121-2125 (2005-03-18)

Targeting proteins overexpressed in hypoxic tumors is as an important means of controlling cancer disease. One such protein is the carbonic anhydrase (CA) isoenzyme IX, which in some types of tumors is overexpressed 150-200-fold. We report here a series of

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