Search results for "Cysteine"

showing 10 items of 550 documents

Fish tolerance to organophosphate-induced oxidative stress is dependent on the glutathione metabolism and enhanced by N-acetylcysteine

2003

Abstract Dichlorvos (2,2-dichlorovinyl dimethyl phosphate, DDVP) is an organophosphorus (OP) insecticide and acaricide extensively used to treat external parasitic infections of farmed fish. In previous studies we have demonstrated the importance of the glutathione (GSH) metabolism in the resistance of the European eel ( Anguilla anguilla L.) to thiocarbamate herbicides. The present work studied the effects of the antioxidant and glutathione pro-drug N -acetyl- l -cysteine (NAC) on the survival of a natural population of A. anguilla exposed to a lethal concentration of dichlorvos, focusing on the glutathione metabolism and the enzyme activities of acetylcholinesterase (AChE) and caspase-3 a…

InsecticidesAntioxidantHealth Toxicology and Mutagenesismedicine.medical_treatmentGlutathione reductaseMedizinApoptosisAquatic SciencePharmacologymedicine.disease_causeAcetylcysteinechemistry.chemical_compoundDichlorvosToxicity Tests AcutemedicineAnimalsProportional Hazards ModelsAnalysis of VarianceEelsDose-Response Relationship DrugMusclesOrganophosphateGlutathioneGlutathioneAcetylcysteineOxidative StressLiverchemistryBiochemistryDichlorvosToxicityNeurotoxicity SyndromesOxidative stressmedicine.drugAquatic Toxicology
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Increased recovery of brain acetylcholinesterase activity in dichlorvos-intoxicated European eels Anguilla anguilla by bath treatment with N-acetylcy…

2003

Organophosphate (OP) pesticides are widely used as antiparasitic chemicals in finfish aquaculture. However, current antidotes cannot be applied to treat intoxicated fish. We showed in previous studies the importance of glutathione (GSH) metabolism in pesticide resistance of the European eel Anguilla anguilla L. The present work studied the effects of the antioxidant and glutathione pro-drug N-acetyl-l-cysteine (NAC) on the recovery of European eels exposed for 96 h to a sublethal concentration (0.17 mg l^-1; 20% of its 96 h LC50) of the OP pesticide dichlorvos (2,2-dichlorovinyl dimethyl phosphate; DDVP). This insecticide and acaricide decreased muscular GSH content and increased oxidised g…

InsecticidesAntioxidantmedicine.medical_treatmentGlutathione reductaseMedizinmedicine.disease_causeAntioxidantsAcetylcysteinechemistry.chemical_compoundGlutathione metabolismUNESCO::CIENCIAS DE LA VIDAOrganophosphorus pesticideProdrugsUNESCO::CIENCIAS DE LA VIDA::Biología animal (Zoología):CIENCIAS DE LA VIDA::Biología animal (Zoología) [UNESCO]biologyOrganophosphateBrainCholinesterase inhibitorGlutathioneGlutathione ReductaseInactivation MetabolicAcetylcholinesteraseDetoxificationmedicine.drugEnvironmental Monitoringmedicine.medical_specialtyN-acetyl-l-cysteineAquatic Science:CIENCIAS DE LA VIDA [UNESCO]Internal medicineDichlorvosmedicineToxicity Tests AcuteAnimalsEcology Evolution Behavior and SystematicsCholinesteraseOrganophosphate poisoningAnalysis of VarianceDetoxification ; Organophosphorus pesticide ; Organophosphate poisoning ; Cholinesterase inhibitor ; Oxidative stress ; N-acetyl-l-cysteine ; AChE ; Glutathione metabolismDose-Response Relationship DrugBathsGlutathioneAnguillaAcetylcysteineEndocrinologychemistryOxidative stressDichlorvosbiology.proteinAChECholinesterase InhibitorsOxidative stressWater Pollutants Chemical
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Highly Efficient Removal of Neonicotinoid Insecticides by Thioether-Based (Multivariate) Metal–Organic Frameworks

2021

Circumventing the impact of agrochemicals on aquatic environments has become a necessity for health and ecological reasons. Herein, we report the use of a family of five eco-friendly water-stable isoreticular metal-organic frameworks (MOFs), prepared from amino acids, as adsorbents for the removal of neonicotinoid insecticides (thiamethoxam, clothianidin, imidacloprid, acetamiprid, and thiacloprid) from water. Among them, the three MOFs containing thioether-based residues show remarkable removal efficiency. In particular, the novel multivariate MOF {SrIICuII6[(S,S)-methox]1.5[(S,S)-Mecysmox]1.50(OH)2(H2O)}·36H2O (5), featuring narrow functional channels decorated with both -CH2SCH3 and -CH2…

InsecticidesMaterials science02 engineering and technologySulfides010402 general chemistry01 natural sciencesAcetamipridWater PurificationNeonicotinoidschemistry.chemical_compoundMethionineAdsorptionThioetherOrganic chemistryGeneral Materials ScienceCysteineMetal-Organic FrameworksSolid Phase ExtractionNeonicotinoidClothianidin021001 nanoscience & nanotechnologyThiacloprid0104 chemical scienceschemistryMetal-organic frameworkAdsorptionThiamethoxam0210 nano-technologyWater Pollutants Chemicalacs applied materials & interfaces
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Combining Hexanoic Acid Plant Priming with Bacillus thuringiensis Insecticidal Activity against Colorado Potato Beetle

2013

Interaction between insect herbivores and host plants can be modulated by endogenous and exogenous compounds present in the source of food and might be successfully exploited in Colorado potato beetle (CPB) pest management. Feeding tests with CPB larvae reared on three solanaceous plants (potato, eggplant and tomato) resulted in variable larval growth rates and differential susceptibility to Bacillus thuringiensis Cry3Aa toxin as a function of the host plant. An inverse correlation with toxicity was observed in Cry3Aa proteolytic patterns generated by CPB midgut brush-border membrane vesicles (BBMV) from Solanaceae-fed larvae, being the toxin most extensively proteolyzed on potato, followed…

Insecticidesmedicine.disease_causeMass Spectrometrylcsh:Chemistrychemistry.chemical_compoundHemolysin ProteinsPlant Growth RegulatorsCysteine ProteasesBacillus thuringiensisPlant defense against herbivoryColorado potato beetleElectrophoresis Gel Two-Dimensionallcsh:QH301-705.5SpectroscopySolanaceaeHexanoic acidbiologyfood and beveragesGeneral MedicineComputer Science ApplicationsColeopterasurgical procedures operativeBiochemistryLarvaHost-Pathogen Interactionsplant hormonesInsect ProteinsSolanaceaeproteolysisColoradoMolecular Sequence DataBacillus thuringiensisCatalysisArticleMicrobiologyCry3Aa toxinInorganic Chemistryintestain proteasesBacterial Proteinsplant defensemedicineAnimalsAmino Acid SequencePhysical and Theoretical ChemistryprimingMolecular BiologyCaproatesSolanum tuberosumBacillus thuringiensis ToxinsToxinOrganic ChemistryColorado potato beetlefungiBody WeightMidgutColorado potato beetle;<i> Bacillus thuringiensis</i>; Cry3Aa toxin; intestain proteases; proteolysis; Solanaceae; hexanoic acid; priming; plant defense; plant hormonesFeeding Behaviorbiology.organism_classificationDietEndotoxinsPapainchemistrylcsh:Biology (General)lcsh:QD1-999hexanoic acidPeptidesDigestive SystemSequence AlignmentInternational Journal of Molecular Sciences
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Stimulation of Fe-S cluster insertion into apoFNR by Escherichia coli glutaredoxins 1, 2 and 3 in vitro.

2004

Abstract The oxygen sensor fumarate nitrate reductase regu-lator (FNR) of Escherichia coli contains in the active (anaerobic)state a [4Fe–4S] 2þ cluster which is lost after exposure to O 2 .Inaerobically prepared apoFNR, or in FNR obtained by treatmentof [4Fe–4S] FNR with O 2 in vitro, intramolecular cysteinedisulfides are found, including the cysteine residues which serveas ligands for the Fe–S cluster. It is shown here that thereconstitution of [4Fe–4S] FNR from this form of aerobicapoFNR was preceded by a long lag phase when glutathione wasused as the reducing agent. Addition of E. coli glutaredoxins(Grx) 1, 2 or 3 decreased the lag phase greatly and stimulatedthe reconstitution rate slig…

Iron-Sulfur ProteinsTime FactorsReducing agentFNRGlutaredoxinBiophysicsBiologyReductaseSulfidesmedicine.disease_causeNitrate reductaseBiochemistryOxygen sensorchemistry.chemical_compoundStructural BiologyGlutaredoxinGeneticsmedicineEscherichia coliCysteineDisulfidesThioredoxinMolecular BiologyEscherichia coliGlutaredoxinsDisulfide reductaseEscherichia coli ProteinsProteinsCell BiologyGlutathioneGlutathioneOxygenBiochemistrychemistryMultigene FamilyThioredoxinOxidoreductasesCysteineTranscription FactorsFEBS letters
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Response of the oxygen sensor NreB to air in vivo: Fe-S-containing NreB and apo-NreB in aerobically and anaerobically growing Staphylococcus carnosus.

2009

ABSTRACT The sensor kinase NreB from Staphylococcus carnosus contains an O 2 -sensitive [4Fe-4S] 2+ cluster which is converted by O 2 to a [2Fe-2S] 2+ cluster, followed by complete degradation and formation of Fe-S-less apo-NreB. NreB·[2Fe-2S] 2+ and apoNreB are devoid of kinase activity. NreB contains four Cys residues which ligate the Fe-S clusters. The accessibility of the Cys residues to alkylating agents was tested and used to differentiate Fe-S-containing and Fe-S-less NreB. In a two-step labeling procedure, accessible Cys residues in the native protein were first labeled by iodoacetate. In the second step, Cys residues not labeled in the first step were alkylated with the fluorescent…

Iron-Sulfur ProteinsbiologyAerobic bacteriaStaphylococcusGene Expression Regulation BacterialAlkylationbiology.organism_classificationMicrobiologyModels BiologicalAerobiosisOxygenBiochemistryBacterial ProteinsSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationNative stateImmunoprecipitationAnaerobic bacteriaAnaerobiosisCysteineKinase activityMolecular BiologyBacteriaCysteineStaphylococcus carnosusSignal TransductionJournal of bacteriology
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Peptidyl Vinyl Ketone Irreversible Inhibitors of Rhodesain: Modifications of the P2 Fragment.

2020

In this paper, we report the design, synthesis and biological investigation of a series of peptidyl vinyl ketones obtained by modifying the P2 fragment of previously reported highly potent inhibitors of rhodesain, the main cysteine protease of Trypanosoma brucei rhodesiense. Investigation of the structure-activity relationship led us to identify new rhodesain inhibitors endowed with an improved selectivity profile (a selectivity index of up to 22 000 towards the target enzyme), and/or an improved antitrypanosomal activity in the sub-micromolar range.

KetoneStereochemistryTrypanosoma brucei bruceiTrypanosoma bruceiCysteine Proteinase Inhibitors01 natural sciencesBiochemistrycathepsin LCathepsin LStructure-Activity RelationshipParasitic Sensitivity TestsDrug DiscoveryTrypanosoma bruceiGeneral Pharmacology Toxicology and PharmaceuticsPharmacologychemistry.chemical_classificationrhodesainbiologyDose-Response Relationship DrugMolecular Structure010405 organic chemistryOrganic ChemistryselectivityTrypanosoma brucei rhodesienseKetonesbiology.organism_classificationCysteine proteaseTrypanocidal Agents0104 chemical sciences010404 medicinal & biomolecular chemistryCysteine EndopeptidasesEnzymechemistrybiology.proteinMolecular MedicineMichael acceptorSelectivityPeptidesChemMedChem
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Identification of HSP90 as a new GABARAPL1 (GEC1)-interacting protein

2011

GABARAPL1 belongs to the small family of GABARAP proteins (including GABARAP, GABARAPL1 and GABARAPL2/GATE-16), one of the two subfamilies of the yeast Atg8 orthologue. GABARAPL1 is involved in the intracellular transport of receptors, via an interaction with tubulin and GABA(A) or kappa opioid receptors, and also participates in autophagy and cell proliferation. In the present study, we identify the HSP90 protein as a novel interaction partner for GABARAPL1 using GST pull-down, mass spectrometry and coimmunoprecipitation experiments. GABARAPL1 and HSP90 partially colocalize in MCF-7 breast cancer cells overexpressed Dsred-GABARAPL1 and in rat brain. Moreover, treatment of MCF-7 cells overe…

LeupeptinsLactams MacrocyclicGABARAPATG8Blotting WesternLactacystinCysteine Proteinase InhibitorsBiologyBiochemistryMass SpectrometryCell Linechemistry.chemical_compoundCell Line TumorMG132BenzoquinonesAnimalsHumansImmunoprecipitationHSP90 Heat-Shock ProteinsReceptorAdaptor Proteins Signal TransducingMicroscopy ConfocalHEK 293 cellsGeneral MedicineHsp90RatsBiochemistrychemistryProteasomebiology.proteinMicrotubule-Associated ProteinsBiochimie
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eNOS S-nitrosylates β-actin on Cys374 and regulates PKC-θ at the immune synapse by impairing actin binding to profilin-1.

2017

The actin cytoskeleton coordinates the organization of signaling microclusters at the immune synapse (IS); however, the mechanisms involved remain poorly understood. We show here that nitric oxide (NO) generated by endothelial nitric oxide synthase (eNOS) controls the coalescence of protein kinase C-¿ (PKC-¿) at the central supramolecular activation cluster (c-SMAC) of the IS. eNOS translocated with the Golgi to the IS and partially colocalized with F-actin around the c-SMAC. This resulted in reduced actin polymerization and centripetal retrograde flow of ß-actin and PKC-¿ from the lamellipodium-like distal (d)-SMAC, promoting PKC-¿ activation. Furthermore, eNOS-derived NO S-nitrosylated ß-…

Life Sciences & Biomedicine - Other Topics0301 basic medicinePOLARIZATIONIMMUNOLOGICAL SYNAPSEImmunological SynapsesT-LymphocytesPROTEINGolgi ApparatusCYTOSKELETONRetrograde FlowBiochemistryARP2/3 COMPLEXT-CELL-ACTIVATIONProfilinsWhite Blood CellsContractile ProteinsFluorescence MicroscopyAnimal CellsMedicine and Health SciencesPseudopodiaBiology (General)Post-Translational ModificationCells CulturedProtein Kinase CMicroscopyT CellsGeneral NeuroscienceLight MicroscopyNeurochemistryRecombinant Proteins3. Good healthIsoenzymesPOLYMERIZATIONProtein TransportCell ProcessesRNA InterferenceCellular TypesNeurochemicalsGeneral Agricultural and Biological SciencesLife Sciences & BiomedicineResearch ArticleBiochemistry & Molecular BiologyNitric Oxide Synthase Type IIIQH301-705.5Imaging TechniquesRecombinant Fusion ProteinsImmune CellsImmunologyLibrary scienceAntigen-Presenting Cellsmacromolecular substancesBiologyNitric OxideResearch and Analysis MethodsGeneral Biochemistry Genetics and Molecular BiologyCell Line03 medical and health sciencesFluorescence ImagingHumansCysteineNITRIC-OXIDE SYNTHASEBiologyScience & TechnologyBlood CellsRECEPTORGeneral Immunology and MicrobiologyBiology and Life SciencesProteinsCell BiologyActinsS-NitrosylationEnzyme ActivationLuminescent ProteinsCytoskeletal Proteins030104 developmental biologyAmino Acid SubstitutionRETROGRADE FLOWProtein Kinase C-thetaMutationProtein Processing Post-TranslationalNeuroscienceActin PolymerizationPLoS biology
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In situ synthesis of lipopeptides as versatile receptors for the specific binding of nanoparticles and liposomes to solid-supported membranes.

2008

A detailed study of the in situ coupling of small peptides such as CGGH6 (H6) and CGWK8 (K8) to maleimide functionalized phospholipid bilayers is presented. Individually addressable microstructured membranes are employed to unequivocally probe the conjugation. The in situ coupling of peptides via a terminal cysteine moiety to maleimide functionalized phospholipids is shown to be a convenient and versatile way to selectively fabricate peptide-modified phospholipid bilayers serving as specific receptor platforms for functionalized vesicles and nanoparticles. Specific binding of functional vesicles to the peptide-modified bilayers is achieved by either histidine complexation with Ni-NTA-DOGS c…

Lipid BilayersStatic ElectricityPhospholipidBiomaterialsDiffusionMaleimideschemistry.chemical_compoundMoietyOrganic chemistryNanotechnologyGeneral Materials ScienceCysteineLipid bilayerMaleimidePOPCMicellesPhospholipidsLiposomeMicroscopy ConfocalChemistryVesicleLysineWaterGeneral ChemistryMembraneModels ChemicalLiposomesBiophysicsNanoparticlesPeptidesBiotechnologySmall (Weinheim an der Bergstrasse, Germany)
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