Search results for "Sulfonamide"

showing 10 items of 258 documents

Targeting BCL-2 family proteins to overcome drug resistance in non-small cell lung cancer.

2007

Cytotoxic chemotherapies are standard of care for patients suffering from advanced non-small cell lung cancer (NSCLC). However, objective responses are only achieved in 20% of cases and long-term survival is rarely observed. Clinically applied anticancer drugs exert at least some of their activities by inducing apoptosis. A critical step in apoptotic signal transduction is the permeabilization of the mitochondrial outer membrane (MOM), which is regulated by the BCL-2 family of proteins. Hence, therapeutic targeting of BCL-2 proteins is a promising approach to increase the drug-sensitivity of cancers. To this end we have assessed the impact of conditional expression of the proapoptotic multi…

ElectrophoresisCancer ResearchProgrammed cell deathLung NeoplasmsPaclitaxelmedicine.medical_treatmentImmunoblottingAntineoplastic AgentsApoptosisDrug resistanceBiologyPermeabilityPiperazinesTargeted therapyNitrophenolsCarcinoma Non-Small-Cell LungCell Line TumormedicineCytotoxic T cellHumansLung cancerEtoposideSulfonamidesBcl-2 familyBiphenyl CompoundsButylated Hydroxytoluenemedicine.diseaseFlow CytometryImmunohistochemistryMitochondriaNeoplasm ProteinsGene Expression Regulation Neoplasticbcl-2 Homologous Antagonist-Killer ProteinOncologyProto-Oncogene Proteins c-bcl-2ApoptosisDoxorubicinDrug Resistance NeoplasmImmunologyCancer researchMyeloid Cell Leukemia Sequence 1 ProteinSignal transductionSignal TransductionInternational journal of cancer
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Simultaneous determination of different classes of antibiotics in fish and livestock by CE-MS

2007

A specific CE-MS method was developed for the simultaneous determination of 12 antibacterial residues (four sulfonamides: sulfamethazine, sulfathiazole, sulfadiazine, and sulfachlorpyridazine; four beta-lactams: amoxicillin, ampicillin, oxacillin, and penicillin V, and four quinolones: danofloxacin, enrofloxacin, ofloxacin, and flumequine) in fish and livestock. Separation conditions, sheath liquid composition and electrospray parameters were optimized to obtain adequate CE separation and a high sensitivity. CE employed a 75 cm long fused-silica capillary (50 cm thermostated plus 25 cm at room temperature) 75 microm id and a 60 mM ammonium acetate separation buffer at pH 8 with 10% of metha…

ElectrosprayMeatDanofloxacinFish farmingClinical BiochemistryQuinolonesbeta-LactamsBiochemistryAnalytical Chemistrychemistry.chemical_compoundTandem Mass SpectrometrymedicineEnrofloxacinAnimalsSulfonamidesResidue (complex analysis)ChromatographySelected reaction monitoringFishesElectrophoresis CapillaryDrug ResiduesAnti-Bacterial AgentschemistryAnimals DomesticFlumequineAmmonium acetateFood Analysismedicine.drugELECTROPHORESIS
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Adverse events associated with encorafenib plus binimetinib in the COLUMBUS study: incidence, course and management.

2019

Abstract Background Dual inhibition of the mitogen-activated protein kinase pathway with BRAF/MEK inhibitor (BRAFi/MEKi) therapy is a standard treatment for BRAFV600-mutant metastatic melanoma and has historically been associated with grade III pyrexia or photosensitivity depending on the combination used. The objective of this study was to fully describe adverse events from the COLUMBUS study evaluating the most recent BRAF/MEK inhibitor combination encorafenib+binimetinib. Patients and methods Patients with locally advanced, unresectable or metastatic BRAFV600-mutant melanoma were randomised to receive encorafenib 450 mg once daily plus binimetinib 45 mg twice daily, encorafenib 300 mg on…

Encorafenib0301 basic medicineOncologyMaleCancer ResearchSkin NeoplasmsBinimetinib; Encorafenib; Melanoma; Safety; Vemurafenib;MedizinBinimetinibchemistry.chemical_compound0302 clinical medicineAntineoplastic Combined Chemotherapy Protocols1306 Cancer ResearchVemurafenibMelanomaFatigueeducation.field_of_studySulfonamidesMEK inhibitorMelanomaStandard treatmentIncidence10177 Dermatology ClinicBinimetinibNauseaMiddle AgedOncology030220 oncology & carcinogenesis2730 OncologyFemaleSafetyMitogen-Activated Protein Kinasesmedicine.drugProto-Oncogene Proteins B-rafmedicine.medical_specialtyVomitingPopulation610 Medicine & health03 medical and health sciencesInternal medicinemedicineHumanseducationAdverse effectProtein Kinase Inhibitorsbusiness.industrymedicine.diseaseDiscontinuation030104 developmental biologychemistryVemurafenibMutationBenzimidazolesCarbamatesbusinessEuropean journal of cancer (Oxford, England : 1990)
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Diverse compounds mimic Alzheimer disease–causing mutations by augmenting Aβ42 production

2004

Increased Abeta42 production has been linked to the development of Alzheimer disease. We now identify a number of compounds that raise Abeta42. Among the more potent Abeta42-raising agents identified are fenofibrate, an antilipidemic agent, and celecoxib, a COX-2-selective NSAID. Many COX-2-selective NSAIDs tested raised Abeta42, including multiple COX-2-selective derivatives of two Abeta42-lowering NSAIDs. Compounds devoid of COX activity and the endogenous isoprenoids FPP and GGPP also raised Abeta42. These compounds seem to target the gamma-secretase complex, increasing gamma-secretase-catalyzed production of Abeta42 in vitro. Short-term in vivo studies show that two Abeta42-raising comp…

Enzyme-Linked Immunosorbent AssayEndogenyProtein Serine-Threonine KinasesPharmacologyTransfectionMass SpectrometryGeneral Biochemistry Genetics and Molecular BiologyPresenilinCell LineFenofibrateAlzheimer DiseaseIn vivoEndopeptidasesmedicineAspartic Acid EndopeptidasesHumansImmunoprecipitationCyclooxygenase InhibitorsProtein precursorHypolipidemic AgentsSulfonamidesrho-Associated KinasesAmyloid beta-PeptidesFenofibratebusiness.industryAnti-Inflammatory Agents Non-SteroidalIntracellular Signaling Peptides and ProteinsBrainGeneral Medicinemedicine.diseaseIn vitroEnzyme ActivationBiochemistryCelecoxibPyrazolesFemaleAmyloid Precursor Protein SecretasesAlzheimer's diseaserhoA GTP-Binding ProteinbusinessAntilipidemic Agentmedicine.drugNature Medicine
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Distribution of chlorpromazine in a simplified blood influenced by various drugs

1973

The binding of chlorpromazine to erythrocytes and to albumin as influenced by other drugs was studied in a simplified blood (31.5±0.3% bovine erythrocytes, 4 g-% bovine serum albumin in 0.02 M phosphate buffer solution containing 0.15 M NaCl). the total concentration of chlorpromazine in the simplified blood was 10−4 M, the concentration of the displacing drugs was 10−3 M. After an incubation period of 3 h at 22° C the chlorpromazine concentration was determined in the albumin solution after centrifugation of the blood at 3000×g and in the aqueous phase after ultracentrifugation at 150000×g. Under control conditions 68.1±0.9% of chlorpromazine was bound to the erythrocytes, 28.5±0.9% was bo…

ErythrocytesChlorpromazineIndomethacinSuraminBenzoatesBinding CompetitiveIncubation periodCoumarinsmedicineAnimalsDistribution (pharmacology)CentrifugationThiopentalBovine serum albuminChlorpromazinePharmacologySulfonamidesBinding SitesChromatographyQuininebiologyProbenecidChemistryFatty AcidsAqueous two-phase systemAlbuminSerum Albumin BovineGeneral MedicineChlorothiazideTetracyclineAntidepressive AgentsSalicylatesAcetazolamidePhenylbutazoneSolubilityPhenytoinbiology.proteinCattleUltracentrifugeDeoxycholic AcidProtein Bindingmedicine.drugNaunyn-Schmiedeberg's Archives of Pharmacology
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5-Substituted-benzylsulfanyl-thiophene-2-sulfonamides with effective carbonic anhydrase inhibitory activity: Solution and crystallographic investigat…

2017

Abstract A series of 5-substituted-benzylsulfanyl-thiophene-2-sulfonamides was prepared by reacting 5-bromo-thiophene-2-sulfonamide with 5-substituted-benzyl mercaptans. The new compounds were investigated as carbonic anhydrase (CA, EC 4.2.1.1) inhibitors. The cytosolic human (h) isoforms hCA I was poorly inhibited by the new sulfonamides (KIs in the range of 683–4250 nM), whereas hCA II, and the transmembrane, tumor associated isoforms hCA IX and XII were effectively inhibited in the subnanomolar–nanomolar range. A high resolution X-ray crystal structure of the adduct of hCA II with one of the new sulfonamides allowed us to rationalize the excellent inhibitory activity of these heterocycli…

Gene isoformModels MolecularStereochemistryClinical BiochemistryPharmaceutical ScienceCrystal structureThiophenesCrystallography X-Ray01 natural sciencesBiochemistryAdductchemistry.chemical_compoundStructure-Activity RelationshipCarbonic anhydraseDrug DiscoveryThiopheneHumansCarbonic Anhydrase InhibitorsMolecular BiologyCarbonic AnhydrasesSulfonamidesbiologyDose-Response Relationship DrugMolecular Structure010405 organic chemistryOrganic ChemistryLyaseTransmembrane protein0104 chemical sciencesSolutions010404 medicinal & biomolecular chemistryCytosolchemistrybiology.proteinMolecular MedicineBioorganicmedicinal chemistry
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In silico identification and experimental validation of hits active against KPC-2 β-lactamase

2018

Bacterial resistance has become a worldwide concern, particularly after the emergence of resistant strains overproducing carbapenemases. Among these, the KPC-2 carbapenemase represents a significant clinical challenge, being characterized by a broad substrate spectrum that includes aminothiazoleoxime and cephalosporins such as cefotaxime. Moreover, strains harboring KPC-type β-lactamases are often reported as resistant to available β-lactamase inhibitors (clavulanic acid, tazobactam and sulbactam). Therefore, the identification of novel non β-lactam KPC-2 inhibitors is strongly necessary to maintain treatment options. This study explored novel, non-covalent inhibitors active against KPC-2, …

Genetics and Molecular Biology (all)Proteomics0301 basic medicineCefotaximeKlebsiella pneumoniaePathology and Laboratory MedicinePhysical ChemistryBiochemistryKlebsiella PneumoniaeDatabase and Informatics MethodsBiochemistry Genetics and Molecular Biology (all); Agricultural and Biological Sciences (all)AntibioticsKlebsiellaCatalytic DomainMedicine and Health Sciencespolycyclic compoundsDrug InteractionsCrystallographyMultidisciplinarybiologyAntimicrobialsOrganic CompoundsProteomic DatabasesChemistryPhysicsQRDrugsSulbactamCondensed Matter PhysicsBacterial PathogensChemistryBiochemistryMedical MicrobiologyPhysical SciencesCrystal StructureMedicinePathogensbeta-Lactamase InhibitorsResearch Articlemedicine.drugScienceIn silico030106 microbiologySulfonamideResearch and Analysis MethodsMicrobiologyMeropenemTazobactambeta-Lactamases03 medical and health sciencesBacterial ProteinsMicrobial ControlClavulanic acidmedicineSolid State PhysicsMicrobial PathogensPharmacologyLigand efficiencyChemical BondingBacteriaOrganic ChemistryChemical CompoundsOrganismsBiology and Life SciencesHydrogen Bondingbiochemical phenomena metabolism and nutritionbiology.organism_classificationbacterial infections and mycosesAmidesBiological Databases030104 developmental biologyAgricultural and Biological Sciences (all)
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H89 enhances the sensitivity of cancer cells to glyceryl trinitrate through a purinergic receptor-dependent pathway

2014

// Marion Cortier 1, 2, 3 , Rahamata Boina-Ali 1, 2, 3 , Cindy Racoeur 1, 2, 3 , Catherine Paul 1, 2, 3 , Eric Solary 2, 4, 5 , Jean-Francois Jeannin 1, 2, 3 , Ali Bettaieb 1, 2, 3 1 EPHE, Tumor Immunology and Immunotherapy Laboratory, Dijon, F-21000, France 2 Inserm U866, Dijon, F-21000, France 3 EA7269, University of Burgundy, Dijon, F-21000, France 4 Inserm UMR1009, Gustave Roussy Institute, Villejuif F-94805, France 5 University Paris-Sud, Faculty of Medicine, Le Kremlin-Bicetre, F-94800, France Correspondence to: Ali Bettaieb, e-mail: ali.bettaieb@u-bourgogne.fr Keywords: H89, GTN, cancer, purinergic receptors, cGMP Received: October 08, 2014      Accepted: January 09, 2015      Publis…

H89SuraminApoptosisPharmacologyBiologyNitric OxideTransfectionNitric oxideMiceNitroglycerinReceptors Purinergic P2Y1chemistry.chemical_compoundAdenosine TriphosphateCell Line TumorNeoplasmspurinergic receptorsmedicineAnimalsHumanscancerCytotoxic T cellReceptorProtein Kinase InhibitorsMembrane Potential MitochondrialSulfonamidesReceptors Purinergic P2Gene Expression ProfilingPurinergic receptorReceptors PurinergicDrug SynergismOligonucleotides AntisenseIsoquinolinescGMPOncologychemistryApoptosisColonic NeoplasmsCancer cellcardiovascular systemSignal transductionReactive Oxygen SpeciesGTNReceptors Purinergic P2X3circulatory and respiratory physiologySignal TransductionResearch Papermedicine.drugOncotarget
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Identification of biological markers of liver X receptor (LXR) activation at the cell surface of human monocytes.

2012

Background Liver X receptor (LXR) α and LXR β (NR1H3 and NR1H2) are oxysterol-activated nuclear receptors involved in the control of major metabolic pathways such as cholesterol homeostasis, lipogenesis, inflammation and innate immunity. Synthetic LXR agonists are currently under development and could find applications in various fields such as cardiovascular diseases, cancer, diabetes and neurodegenerative diseases. The clinical development of LXR agonists requires the identification of biological markers for pharmacodynamic studies. In this context, monocytes represent an attractive target to monitor LXR activation. They are easily accessible cells present in peripheral blood; they expres…

Hydrocarbons FluorinatedCD226Celllcsh:MedicineBiochemistryMonocytesDrug DiscoveryMolecular Cell Biologypolycyclic compoundsSignaling in Cellular Processeslcsh:ScienceLiver X ReceptorsSulfonamidesMultidisciplinarymedicine.diagnostic_testfood and beveragesCell DifferentiationOrphan Nuclear ReceptorsFlow CytometryNuclear SignalingCholesterolmedicine.anatomical_structureGene Knockdown Techniqueslipids (amino acids peptides and proteins)Research ArticleSignal TransductionAgonistmedicine.drug_classImmune CellsImmunologyContext (language use)Biologydigestive systemFlow cytometryAntigens CDDNA-binding proteinsmedicineHumansRNA MessengerLiver X receptorBiologyCluster of differentiationMacrophagesCell Membranelcsh:RProteinsLipid MetabolismMetabolismGene Expression RegulationNuclear receptorImmunologyCancer researchlcsh:QBiomarkersCytometryFoam CellsDevelopmental BiologyPLoS ONE
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Effect of a Rigid Sulfonamide Bond on Molecular Folding: A Case Study

2015

A disulfonamide compound with bulky aromatic side chains was prepared, and its properties as a potential building block for foldamers were evaluated. Two different solvate crystal forms of the compound were identified and compared to the structures of an analogous oligoamide and related disulfonamides. The disulfonamide is unfolded in one of the solvates, whereas in the other one, a loosely folded conformer stabilized by an intramolecular hydrogen bond is found. Density functional calculations indicated that the loosely folded conformer is slightly more stable than its unfolded isomer. The calculations also identified a third, more tightly folded and more extensively hydrogen bonded, confor…

HydrogenStereochemistrychemistry.chemical_elementmolecular foldingkonformeeritorgaaninen synteesiCrystalSide chainmolecular conformersGeneral Materials Sciencemolekyylien laskostuminenta116sulfonamidisidosConformational isomerismX-ray crystallographychemistry.chemical_classificationHydrogen bondsulfonamide bondGeneral Chemistryorganic synthesisCondensed Matter PhysicsSulfonamideFolding (chemistry)chemistryIntramolecular forceröntgenkristallografiaCrystal Growth & Design
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