Search results for "Fides"

showing 10 items of 123 documents

Headspace Volatile Composition of the Flowers of Caralluma europaea N.E.Br. (Apocynaceae)

2009

The volatile constituents of the flowers of Caralluma (Apteranthes) europaea (Guss.) N.E. Br. (Apocynaceae - Asclepiadoideae) from Lampedusa Island were analyzed by headspace method. The analyses allowed the identification and quantification of 41 compounds. The main components were, among the monoterpenoids, terpinolene (23.3%), a-terpinene (19.1%) and linalool (18.4%), whereas, among the carbonylic compounds the major constituents were heptanal (2.0%), octanoic acid (2.4%) and hexanoic acid (1.7%). It is worth to mention the presence of a nitrogen containing compound, indole (0.8%) and of a sulphur containing compound, dimethylsulphide (t). The compounds found in the flowers of C. europea…

IndolespollinationPharmaceutical ScienceHymenopteraAnalytical Chemistrychemistry.chemical_compoundLinaloolDrug Discovery<em>Caralluma europaea</em>; <em>Apteranthes europaea</em>; Diptera; pollination; sapromyiophily; volatilesHexanoic acidchemistry.chemical_classificationApocynaceaevolatilesChemistry (miscellaneous)Molecular MedicineComposition (visual arts)CaprylatesSettore BIO/07 - EcologiaChromatography GasAcyclic MonoterpenesCyclohexane MonoterpenesFlowersBiologySulfidesArticleSettore CHIM/12 - Chimica Dell'Ambiente E Dei Beni CulturaliLepidoptera genitalialcsh:QD241-441lcsh:Organic chemistryBotanyOrganic matterPhysical and Theoretical ChemistryCaproatesCaralluma europaea; Apteranthes europaea; Diptera; pollination; sapromyiophily; volatilesAldehydesVolatile Organic CompoundsPlant ExtractsTerpenesDipteraOrganic ChemistrySettore CHIM/06 - Chimica Organicabiology.organism_classificationApocynaceaechemistryOdorsapromyiophilyCaralluma europaeaSettore BIO/03 - Botanica Ambientale E ApplicataMonoterpenesApteranthes europaea
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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 &amp; interfaces
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Reduced Apo-Fumarate Nitrate Reductase Regulator (ApoFNR) as the Major Form of FNR in Aerobically Growing Escherichia coli▿

2008

ABSTRACT Under anoxic conditions, the Escherichia coli oxygen sensor FNR (fumarate nitrate reductase regulator) is in the active state and contains a [4Fe-4S] cluster. Oxygen converts [4Fe-4S]FNR to inactive [2Fe-2S]FNR. After prolonged exposure to air in vitro, apoFNR lacking a Fe-S cluster is formed. ApoFNR can be differentiated from Fe-S-containing forms by the accessibility of the five Cys thiol residues, four of which serve as ligands for the Fe-S cluster. The presence of apoFNR in aerobically and anaerobically grown E. coli was analyzed in situ using thiol reagents. In anaerobically and aerobically grown cells, the membrane-permeable monobromobimane labeled one to two and four Cys res…

Iron-Sulfur ProteinsAerobic bacteriamedicine.disease_causeNitrate reductaseMicrobiologymedicineEscherichia coliAnaerobiosisDisulfidesMolecular BiologyEscherichia colichemistry.chemical_classificationbiologySuccinate dehydrogenaseEscherichia coli Proteinsbiology.organism_classificationEnterobacteriaceaeEnzymes and ProteinsAerobiosisCulture MediaOxygenchemistryBiochemistryThiolbiology.proteinbacteriaAnaerobic bacteriaOxidation-ReductionBacteria
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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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Organization of the major and minor capsid proteins in human papillomavirus type 33 virus-like particles.

1995

The organization of the major (L1) and minor (L2) proteins in the human papillomavirus capsid is still largely unknown. In this study we analysed the disulphide bonding between L1 proteins and the association of L2 proteins with capsomers using virus-like particles obtained in insect cells by co-expression of the L1 and L2 genes of human papillomavirus type 33. About 50% of the L1 protein molecules in these particles (1.29 g/cm3) formed disulphide-bonded trimers. Reduction of the intermolecular disulphide bonds by dithiothreitol (DTT) treatment caused disassembly of virus-like particles into capsomers. This indicates that disulphide bonds between capsomers at the threefold symmetry position…

L1virusesCapsomereVirionOncogene Proteins ViralBiologyVirologyVirusDithiothreitolCell Linechemistry.chemical_compoundMonomerCapsidchemistryCapsidVirologyMoleculeAnimalsHumansCapsid ProteinsDisulfidesGenePapillomaviridaeThe Journal of general virology
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Nonheme Fe(IV) Oxo Complexes of Two New Pentadentate Ligands and Their Hydrogen-Atom and Oxygen-Atom Transfer Reactions.

2015

Two new pentadentate {N5} donor ligands based on the N4Py (N4Py = N,N-bis(2-pyridylmethyl)-N-bis(2-pyridyl)methylamine) framework have been synthesized, viz. [N-(1-methyl-2-benzimidazolyl)methyl-N-(2-pyridyl)methyl-N-(bis-2-pyridyl methyl)amine] (L1) and [N-bis(1-methyl-2-benzimidazolyl)methyl-N-(bis-2-pyridylmethyl)amine] (L2), where one or two pyridyl arms of N4Py have been replaced by corresponding (N-methyl)benzimidazolyl-containing arms. The complexes [FeII(CH3CN)(L)]2+ (L = L1 (1); L2 (2)) were synthesized, and reaction of these ferrous complexes with iodosylbenzene led to the formation of the ferryl complexes [FeIV(O)(L)]2+ (L = L1 (3); L2 (4)), which were characterized by UV–vis spe…

Ligand field theoryModels MolecularStereochemistryPyridinesIronMolecular ConformationSulfidesIron compoundsLigandsMedicinal chemistryRedoxReaccions químiquesInorganic Chemistrychemistry.chemical_compoundChemical reactionsMössbauer spectroscopyElectrochemistryOrganometallic Compoundspentadentate ligandsPhysical and Theoretical ChemistrySpectroscopyta116LigandChemistryMethylamineFerro -- CompostosHydrogen atomOxygeniron complexesAmine gas treatingOxidation-ReductionHydrogenInorganic chemistry
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Bio serves nano: biological light-harvesting complex as energy donor for semiconductor quantum dots.

2012

Light-harvesting complex (LHCII) of the photosynthetic apparatus in plants is attached to type-II core-shell CdTe/CdSe/ZnS nanocrystals (quantum dots, QD) exhibiting an absorption band at 710 nm and carrying a dihydrolipoic acid coating for water solubility. LHCII stays functional upon binding to the QD surface and enhances the light utilization of the QDs significantly, similar to its light-harvesting function in photosynthesis. Electronic excitation energy transfer of about 50% efficiency is shown by donor (LHCII) fluorescence quenching as well as sensitized acceptor (QD) emission and corroborated by time-resolved fluorescence measurements. The energy transfer efficiency is commensurable …

Light-Harvesting Protein ComplexesSulfidesPhotochemistryAbsorptionLight-harvesting complexQuantum DotsElectrochemistryCadmium CompoundsGeneral Materials ScienceAbsorption (electromagnetic radiation)Selenium CompoundsSpectroscopyFluorescent Dyesbusiness.industryChemistryPeasSurfaces and InterfacesCondensed Matter PhysicsFluorescenceAcceptorNanocrystalEnergy TransferSemiconductorsAbsorption bandQuantum dotZinc CompoundsOptoelectronicsTelluriumbusinessVisible spectrumLangmuir : the ACS journal of surfaces and colloids
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Molecular structures of Se(SCH3)2 and Te(SCH3)2 using gas-phase electron diffraction and ab initio and DFT geometry optimisations

2005

The molecular structures of Se(SCH3)2 and Te(SCH3)2 were investigated using gas-phase electron diffraction (GED) and ab initio and DFT geometry optimisations. While parameters involving H atoms were refined using flexible restraints according to the SARACEN method, parameters that depended only on heavy atoms could be refined without restraints. The GED-determined geometric parameters (rh1) are: rSe-S 219.1(1), rS-C 183.2(1), rC-H 109.6(4) pm; S-Se-S 102.9(3), Se-S-C 100.6(2), S-C-H (mean) 107.4(5), S-Se-S-C 87.9(20), Se-S-C-H 178.8(19)° for Se(SCH3)2, and rTe-S 238.1(2), rS-C 184.1(3), rC-H 110.0(6) pm; S-Te-S 98.9(6), Te-S-C 99.7(4), S-C-H (mean) 109.2(9), S-Te-S-C 73.0(48), Te-S-C-H 180.…

MAIN-GROUP ELEMENTSCRYSTALLINE PHASESPopulationAb initioElectronsGeometrySulfidesATOMSInorganic ChemistryBI3RD-ROWMoleculeORBITAL METHODSPOLARIZATION FUNCTIONSSelenium CompoundseducationVALENCE BASIS-SETSConformational isomerismBasis seteducation.field_of_studyValence (chemistry)Molecular StructureChemistry2ND-ROW ELEMENTSCrystallographyMain group elementDENSITYExcited stateTelluriumDalton Transactions
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Reversibly stable thiopolyplexes for intracellular delivery of genes.

2006

Novel polyaspartamide non-viral carriers for gene therapy were synthesized by introducing, on the same polymer backbone, positively charged groups, for electrostatic interactions with DNA, and thiol groups for the formation of disulfide bridges between polymer chains. The introduction of thiols was aimed to have a vector with low redox potential sensitivity: disulfide crosslinking in fact, being stable in extracellular environment, allowed either to have stable complexes in plasma, that can protect DNA from metabolism, or to be reduced inside the cell, where the excess of glutathion in reduced form maintains a low redox potential. The consequent destabilization of the complex after disulfid…

Magnetic Resonance SpectroscopyLightStereochemistryCell SurvivalPolymersPharmaceutical ScienceElectrophoretic Mobility Shift AssayGene deliveryTransfectionchemistry.chemical_compoundGene DeliveryMiceDynamic light scatteringGenes ReporterCell Line TumorAnimalsScattering RadiationElectrophoretic mobility shift assayDisulfidesSulfhydryl CompoundsLuciferaseschemistry.chemical_classificationthiopolycationsEndodeoxyribonucleasesLuminescent AgentsGenetic transferCationic polymerizationProteinsDNAChromatography Ion ExchangeCombinatorial chemistrychemistrypolyaspartammideAgarose gel electrophoresisThiolPeptidesOxidation-ReductionDNAJournal of controlled release : official journal of the Controlled Release Society
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Disulfide-crosslinked hyaluronan-gelatin hydrogel films: a covalent mimic of the extracellular matrix for in vitro cell growth

2003

A new disulfide crosslinking method was developed for the preparation of blended hyaluronan (HA)-gelatin hydrogels to form a synthetic, covalently linked mimic of the extracellular matrix (ECM). The HA and gelatin were chemically modified using 3,3′-dithiobis(propionic hydrazide) (DTP). After reduction with dithiothreitol (DTT), the thiol derivatives of HA (HA-DTPH) and gelatin (gelatin-DTPH) were obtained and characterized. To minimize interference with biological function, the degree of substitution of HA-DTPH and gelatin-DTPH was kept below 50%. Solutions of HA-DTPH and gelatin-DTPH in varying blends (20%, 40%, 60%, 80% gelatin) were prepared in 1% w/v NaCl and crosslinked by disulfide b…

Magnetic Resonance SpectroscopyTime FactorsBiocompatible MaterialsSodium ChlorideGelatinHydrogel Polyethylene Glycol DimethacrylateDithiothreitolCell growthMicechemistry.chemical_compoundHyaluronic acidDisulfidesHyaluronic Acidchemistry.chemical_classificationMice Inbred BALB CBiomaterialHydrogels3T3 CellsMethylgalactosidesExtracellular MatrixCross-Linking ReagentsMechanics of MaterialsCovalent bondSelf-healing hydrogelsThiolCell DivisionBiotechnologyfood.ingredientMaterials scienceCell SurvivalBiomedical EngineeringBiophysicsHyaluronoglucosaminidaseBioengineeringmacromolecular substancesIn Vitro TechniquesHydrazideBiomaterialsDisulfidefoodPolymer chemistryCell AdhesionAnimalsSulfhydryl Compoundstechnology industry and agricultureFibroblastsBiomaterialDithiothreitolModels ChemicalchemistryCeramics and CompositesGelatinPolystyrenesBiomaterials
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