Search results for "OxyR"

showing 10 items of 216 documents

The Topological Analysis of the ELFx Localization Function: Quantitative Prediction of Hydrogen Bonds in the Guanine–Cytosine Pair

2021

International audience; In this contribution, we recall and test a new methodology designed to identify the favorable reaction pathway between two reactants. Applied to the formation of the DNA guanine (G) –cytosine (C) pair, we successfully predict the best orientation between the base pairs held together by hydrogen bonds and leading to the formation of the typical Watson Crick structure of the GC pair. Beyond the global minimum, some local stationary points of the targeted pair are also clearly identified.

Models MolecularELF<sub>x</sub>Base pairGuaninePharmaceutical ScienceOrganic chemistryMolecular Structure of Nucleic Acids: A Structure for Deoxyribose Nucleic Acid010402 general chemistry01 natural sciencesArticleAnalytical ChemistryELFxchemistry.chemical_compoundQD241-441Nucleophilebase pair0103 physical sciencesDrug Discovery[CHIM]Chemical SciencesguaninePhysical and Theoretical Chemistrycytosinehydrogen bond010304 chemical physicsHydrogen bondHydrogen BondingDNA0104 chemical sciencesELF xelectrophilicCrystallographyELFchemistryChemistry (miscellaneous)ElectrophileMolecular MedicineNucleic Acid ConformationDNACytosinenucleophilicMolecules
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Copper-mediated DNA photocleavage by a tetrapyridoacridine (tpac) ligand.

2008

Abstract We have focused our interest on the tetrapyridoacridine ligand tetrapyrido[3,2- a :2′,3′- c :3′′,2″- h : 2‴,3‴- j ]acridine (tpac), as a model system for the preparation of novel copper-based artificial nucleases. The complex of copper(II)–tpac cleaves supercoiled pUC18 plasmid DNA in an oxidative manner by photoactivation with visible light, exhibiting maximum cleaving efficiency at 1:2 metal–ligand stoichiometric ratio. We propose an interaction of the copper–tpac complex with DNA through both major and minor grooves and a photocleavage mechanism via the formation of hydroxyl radicals and singlet oxygen or singlet oxygen-like species.

Models MolecularLightStereochemistryPhotochemistryRadicalClinical BiochemistryPharmaceutical Sciencechemistry.chemical_elementPhotochemistryLigandsBiochemistrychemistry.chemical_compoundPolycyclic compoundDrug DiscoveryPhotosensitizerSinglet stateMolecular Biologychemistry.chemical_classificationDeoxyribonucleasesMolecular StructureSinglet OxygenChemistrySinglet oxygenOrganic ChemistryDNACopperAcridineMolecular MedicineAcridinesDNACopperPhenanthrolinesBioorganicmedicinal chemistry letters
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Characterization of the pleiotropic LysR-type transcription regulator LeuO of Escherichia coli

2019

AbstractLeuO is a pleiotropic LysR-type transcriptional regulator (LTTR) and co-regulator of the abundant nucleoid-associated repressor protein H-NS in Gammaproteobacteria. As other LTTRs, LeuO is a tetramer that is formed by dimerization of the N-terminal DNA-binding domain (DBD) and C-terminal effector-binding domain (EBD). To characterize the Escherichia coli LeuO protein, we screened for LeuO mutants that activate the cas (CRISPR-associated/Cascade) promoter more effectively than wild-type LeuO. This yielded nine mutants carrying amino acid substitutions in the dimerization interface of the regulatory EBD, as shown by solving the EBD’s crystal structure. Superimposing of the crystal str…

Models MolecularProtein domainMutantRepressorPlasma protein bindingBiologymedicine.disease_cause03 medical and health sciencesProtein DomainsTranscription (biology)GeneticsConsensus sequencemedicinePromoter Regions GeneticEscherichia coli030304 developmental biologyGenetics0303 health sciences030306 microbiologyEscherichia coli ProteinsGene regulation Chromatin and EpigeneticsGenetic PleiotropyDNAGene Expression Regulation BacterialDNA-Binding ProteinsMutationNucleic Acid ConformationProtein MultimerizationDeoxyribonuclease IProtein BindingTranscription FactorsNucleic Acids Research
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The membrane distal half of gp130 is responsible for the formation of a ternary complex with IL-6 and the IL-6 receptor

1995

AbstractGp130 is the signal transducing subunit of the interleukin-6 receptor. Signaling is initiated by the complex formation of gp130 with IL-6 bound to the IL-6 receptor (IL-6R). We have subdivided the extracellular domain of gp130 in two parts and expressed the mutant proteins as soluble IgG fusion proteins in COS-7 cells. By studying the formation of the ternary complex we show that the membrane distal half of gp130 which contains a cytokine receptor domain is responsible for the interaction with the IL-6/IL-6R complex. Interestingly this is the same region which is believed to be involved in specific recognition of the related cytokines LIF, OM, and probably also of CNTF and IL-11.

Molecular Sequence DataBiophysicsBiologyBiochemistryCytokine receptor domainCell Linegp130Structure-function analysisAntigens CDStructural BiologyCytokine Receptor gp130GeneticsAnimals5-HT5A receptorReceptorMolecular BiologyTernary complexMembrane GlycoproteinsBase SequenceInterleukin-6digestive oral and skin physiologyHaplorhiniReceptors InterleukinCell BiologyGlycoprotein 130Receptors Interleukin-6Fusion proteinbiological factorsCell biologyOligodeoxyribonucleotidesInterleukin-6 receptorCancer researchSignal transductionCytokine receptorProtein BindingSignal TransductionFEBS Letters
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Excessive CpG 1668 stimulation triggers IL-10 production by cDC that inhibits IFN-alpha responses by pDC.

2008

Upon stimulation with a wide range of concentrations of CpG oligodeoxynucleotide 2216 (CpG 2216), plasmacytoid DC are induced to produce type I IFN (IFN-alpha/beta). In contrast, CpG 1668 shows a bell-shaped dose-response correlation, i.e. only intermediate but not high doses of CpG 1668 induce IFN-alpha/beta. Interestingly, high-dose CpG 1668 completely inhibited IFN-alpha responses induced by CpG 2216. Experiments using supernatant of high-dose CpG-1668-treated cells indicated that secreted inhibitor(s) mediated the IFN-alpha shut-off. Among modulating cytokines, IL-10 turned out to be one important negative regulator. In line with this, supernatants of IL-10-deficient DC cultures stimula…

MuromegalovirusCpG OligodeoxynucleotideImmunologyStimulationmedicine.disease_causeNegative regulatorAutoimmunityMiceAdjuvants ImmunologicmedicineImmunology and AllergyAnimalsCells CulturedbiologyTLR9Interferon-alphaDendritic Cellsbiology.organism_classificationMolecular biologyInterleukin-10Interleukin 10CpG siteOligodeoxyribonucleotidesVesicular stomatitis virusToll-Like Receptor 9ImmunologyCytokinesEuropean journal of immunology
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Morphological determination of the phototrophic community composition of biological soil crusts in coastal sand dunes in northern Germany

2022

This dataset comprises the microbial community composition of biological soil crusts in north-German sand dunes. For this we obtained enrichment cultures of phototrophic microorganisms, by placing fragments of biocrusts of the same Petri dishes as used for sequencing, in Petri dishes with Bold Basal (1N BBM) agarized medium (Bischoff and Bold 1963). Cultures were grown under standard laboratory conditions: with a 12-hour alteration of light and dark phases and irradiation of 25 μmol photons m-2 s-1 at a temperature 20 ± 5 ºС. Microscopic study of these raw cultures began in the third week of cultivation. Morphological examinations were performed using Olympus BX53 light microscope with Noma…

Nostoc cf linckiaNodosilinea cf. epilithicaTetracystis cf. sarcinalisCylindrocystis cf crassaPtychostomum moravicumElliptochloris subsphaericaThin layer chromatographyAsterococcus spCylindrocystis cf. crassaCladonia phyllophoraChloroidium cf ellipsoideumChlorolobion sp.Hypnum cupressiforme var lacunosumHypogymnia physodesStichococcus cf. bacillarisEremochloris spCrustsParmelia sulcataStenomitos sp.algaeBracteacoccus sp.Chlorococcum spPtychostomum capillarewith Nomarski DIC opticsCladonia chlorophaeaCladonia foliaceaBiospheric SciencesMyrmecia cf irregularisField experimentNodosilinea cf epilithicaBacidina etayanaPolytrichum juniperinumCoccomyxa sp.Placynthiella uliginosaLeptolyngbya spPohlia nutansCladonia furcataPeltigera extenuataWatanabea cf. acidophilaGeosciencesChloroidium cf. ellipsoideumLongitude of eventWatanabea cf acidophilaParietochloris cf. alveolarisPtychostomum imbricatulumSiteLight microscope Olympus Ltd BX53 with Nomarski DIC opticsDicranum scopariumSyntrichia ruraliformisBX53Pseudochlorella spKlebsormidium cf flaccidumOlympus LtdCladonia novochlorophaeaDATE TIMECladonia cocciferaCladonia conistaNostoc cf. linckiaDiplosphaera chodatii16S rRNAOxyrrhynchium praelongumTetracystis cf sarcinalisChlorokybus atmophyticusNostoc sp.Interfilum cf. massjukiaeMicarea misellaCoelastrella spStenomitos spNostoc spEvent labelLecanora hageniiPolytrichum piliferumTetradesmus arenicolaElevation of eventPlanophila spChlorococcum sp.Campylopus introflexusCladonia ramulosaCephaloziella divaricataPseudochlorella sp.Nostoc cf. communeChlorolobion spNannochloris spCladonia rangiformisMacrochloris spNannochloris sp.Cladonia fimbriataEvernia prunastriCaloplaca cerinellaLecania cyrtellaLecanora persimilisCladonia subulataPseudoscleropodium purumStichococcus cf bacillarisLatitude of eventLight microscopeInterfilum terricolaCladonia glaucaCladonia portentosaPlanophila sp.Spongiochloris spCladonia reisediment analysisCladonia gracilisHypnum cupressiformeTolypothrix cf. byssoideaCeratodon purpureusEcologyCladonia uncialis ssp biuncialisPseudomuriella cf. aurantiacaCylindrocystis sp.Klebsormidium cf. subtileRacomitrium canescensMicrocoleus vaginatusCoccomyxa spCylindrocystis spLobochlamys sp.soil ecologyXanthoria parietinaCladonia ciliataHypnum cupressiforme var. lacunosumActinochloris terrestrisInterfilum cf massjukiaeNatural SciencesChlorella vulgarisMacrochloris sp.Coelastrella sp.Bracteacoccus spRacomitrium elongatumCladonia scabriusculaNostoc cf. edaphicumStichococcus allasLocationNostoc cf edaphicumKlebsormidium cf. flaccidumLophozia bicuspidataPseudomuriella cf aurantiacaKlebsormidium crenulatumduneNostoc cf communeLeptolyngbya sp.Ptilidium ciliatumCladonia macilentaMyrmecia cf. irregularisPtychostomum compactumLobochlamys spPleurozium schreberiCladonia arbusculaPhyscia tenellaBrachythecium albicansPeltigera hymeniaAmandinea punctataTimaviella sp.Scoliciosporum galluraeParietochloris cf alveolarisAsterococcus sp.Hennediella heimiiTimaviella spDATE/TIMECladonia humilisBryum capillareTolypothrix cf byssoideaKlebsormidium cf subtileEremochloris sp.Cladonia floerkeanaSpongiochloris sp.Cladonia uncialis ssp. biuncialisHypnum jutlandicum
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Radiolabeled DNase, a potential indicator for noninvasive detection of tissue damage

1983

Pancreatic DNase I was labeled with 131I or fluorescamine and injected IV into NMRI mice bearing a sarcoma 180. Of the injected tracer, 1.5%-2% was found to accumulate per g tumor. In sections of tumor tissue DNase was localized in damaged cells in solid and necrotic tumor regions. This binding is most probably due to specific interaction of DNase with actin, an ubiquitous cytoskeletal protein. Two-component blood clearance with a rapid first component (two-thirds of applied radioactivity) was observed. The labeled tumor could easily be visualized by gamma camera imaging. The findings suggest DNase to be a potent radiopharmaceutical for imaging damaged tissue, occurring in malignant tumors …

Pathologymedicine.medical_specialtyDeoxyribonucleasesPancreatic DNaseGeneral MedicineFluorescaminemedicine.diseaseFluorescamineIodine RadioisotopesMicechemistry.chemical_compoundchemistryNmri miceTissue damagemedicineAnimalsFemaleTissue DistributionRadiology Nuclear Medicine and imagingNecrotic tumorSarcomaRadionuclide ImagingSarcoma 180CytoskeletonActinEuropean Journal of Nuclear Medicine
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Standardized staining methods: Feulgen-Rossenbeck reaction for desoxyribonucleic acid and periodic acid-Schiff (PAS) procedure

2002

A project group working under the European Confederation of Laboratory Medicine (ECLM) presents recommendations for standardized procedures for the Feulgen-Rossenbeck-Schiff and the periodic acid-Schiff (PAS) reactions on cytological and histological material. The advantages and disadvantages of such standardized procedures are presented here in a preamble. Both users and manufacturers are encouraged to give their opinions with a view to achieving consensus on these procedures and on how further work on these lines may proceed.

Pathologymedicine.medical_specialtyHistologyColoring agentsGeneral MedicinePeriodic acid–Schiff stainBiologyStainingMedical Laboratory TechnologymedicineMedical physicsFeulgen stainProject groupDesoxyribonucleic acidBiotechnic &amp; Histochemistry
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The analysis of modified peroxisome proliferator responsive elements of the peroxisomal bifunctional enzyme in transfected HepG2 cells reveals two re…

1995

AbstractPeroxisome proliferators (PPs) are non-genotoxic carcinogens in rodents. They can induce the expression of numerous genes via the heterodimerization of two members of the steroid hormone receptor superfamily, called the peroxisome proliferator-activated receptor (PPAR) and the 9-cis retinoic acid receptor (RXR). Many of the PP responsive genes possess a peroxisome proliferator response element (PPRE) formed by two TGACCT-related motifs. The bifunctional enzyme (HD) PPRE contains 3 such motifs, creating DR1 and DR2 sequences. PPAR and RXR regulate transcription via the DR1 element while DR2 modulates the expression of the gene via auxiliary factors in HepG2 cells.

Peroxisome proliferator-activated receptor gammaReceptors Retinoic AcidSteroid hormone receptorMolecular Sequence DataResponse elementBiophysicsReceptors Cytoplasmic and NuclearPeroxisome proliferator-activated receptorchemical and pharmacologic phenomenaIn Vitro TechniquesRegulatory Sequences Nucleic AcidRetinoid X receptorBiologyPeroxisomal Bifunctional EnzymeTransfectionMicrobodiesBiochemistryGene Expression Regulation EnzymologicTranscriptional activationPeroxisomal Bifunctional EnzymeMultienzyme ComplexesStructural BiologyPeroxisome proliferator response element9-cis Retinoic acid receptor alphaTumor Cells CulturedGeneticsHumansRNA MessengerIsomerasesEnoyl-CoA HydrataseMolecular Biologychemistry.chemical_classificationBinding SitesBase Sequence3-Hydroxyacyl CoA DehydrogenasesPeroxisome proliferator-activated receptorCell BiologyDNA-Binding ProteinsRetinoic acid receptorRetinoid X ReceptorsLiverOligodeoxyribonucleotidesBiochemistrychemistryRat peroxisomal enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenaseEnzyme InductionPeroxisome proliferator-activated receptor alphaTranscription FactorsFEBS Letters
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Purification of a nuclease from human serum.

1981

The purification procedure for a nuclease from human serum is described. It includes ammonium sulfate precipitation, chromatography on DEAE-Sephadex and on Sephacryl-S 200, and preparative electrophoresis. The enzyme, purified about 2000-fold, is homogeneous in a sodium dodecyl sulfate electrophoretic system, where it has a mol. wt of 78,000. The pH optimum lies around pH 6.5; it is a sugar-nonspecific endonuclease.

Pharmacologychemistry.chemical_classificationNucleaseChromatographyDeoxyribonucleasesbiologyCell BiologyCellular and Molecular NeuroscienceElectrophoresischemistry.chemical_compoundEndonucleaseKineticsEnzymechemistrybiology.proteinMolecular MedicineHumansAmmoniumSodium dodecyl sulfateSulfateMolecular BiologyAmmonium sulfate precipitationExperientia
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