Search results for "Escher"

showing 10 items of 728 documents

Antibacterial activity of Mediterranean Oyster mushrooms, species of genus Pleurotus (higher Basidiomycetes).

2013

Extracts of the Mediterranean culinary-medicinal Oyster mushrooms Pleurotus eryngii var. eryngii, P. eryngii var. ferulae, P. eryngii var. elaeoselini, and P. nebrodensis were tested for their in vitro growth inhibitory activity against a group of bacterial reference strains of medical relevance: Staphylococcus aureus ATCC 25923, S. epidermidis RP62A, Pseudomonas aeruginosa ATCC 15442, and Escherichia coli ATCC10536. All of the Pleurotus species analyzed inhibited the tested microorganisms in varying degrees. The data included in this paper for P. nebrodensis and P. eryngii var. elaeoselinii are new reports.

OysterMicroorganismStaphylococcusHuman pathogenmedicine.disease_causePleurotusApplied Microbiology and BiotechnologySpecies Specificitybiology.animalDrug DiscoveryBotanymedicineEscherichia coliPleurotus eryngiiFood scienceEscherichia coliPharmacologyPleurotusBiological Productsbiologybiology.organism_classificationAnti-Bacterial AgentsStaphylococcus aureusSettore BIO/03 - Botanica Ambientale E ApplicataPseudomonas aeruginosamedicinal mushrooms antibacterial activity Pleurotus human pathogensAntibacterial activityAgaricalesInternational journal of medicinal mushrooms
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The cytoplasmic PASC domain of the sensor kinase DcuS of Escherichia coli : role in signal transduction, dimer formation, and DctA interaction

2013

The cytoplasmic PAS(C) domain of the fumarate responsive sensor kinase DcuS of Escherichia coli links the transmembrane to the kinase domain. PAS(C) is also required for interaction with the transporter DctA serving as a cosensor of DcuS. Earlier studies suggested that PAS(C) functions as a hinge and transmits the signal to the kinase. Reorganizing the PAS(C) dimer interaction and, independently, removal of DctA, converts DcuS to the constitutive ON state (active without fumarate stimulation). ON mutants were categorized with respect to these two biophysical interactions and the functional state of DcuS: type I-ON mutations grossly reorganize the homodimer, and decrease interaction with Dct…

PAS domainDicarboxylic Acid TransportersModels MolecularfumarateProtein ConformationEscherichia coli ProteinsDNA Mutational AnalysisDctAModels Biological570 Life sciencessignal transduction.Escherichia coliProtein Interaction Domains and MotifsProtein MultimerizationDcuS sensor kinaseProtein KinasesOriginal ResearchSignal Transduction570 Biowissenschaften
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The stability and functional properties of proteoliposomes mixed with dextran derivatives bearing hydrophobic anchor groups

1992

Liposomes composed of Escherichia coli phospholipid were coated with polysaccharides bearing hydrophobic palmitoyl anchors. The effect on the stability of liposomes without or with integral membrane proteins was investigated. A high concentration of hydrophobized dextrans protected the liposomes against detergent degradation, decreased the fluidity of the membranes, prevented fusion of the liposomes and enhanced their stability. Proteoliposomes containing beef heart cytochrome-c oxidase and the lactose transport carrier of E. coli were similarly affected by coating with the dextrans. Under these conditions both membrane proteins were still active. Long-term stability of the coated liposomes…

PROTEINMembrane FusionBiochemistryMembrane Potentialschemistry.chemical_compoundFUSIONINTEGRAL MEMBRANE PROTEINBINDINGIntegral membrane proteinLiposomeSymportersEscherichia coli ProteinsVesiclePROTEOLIPOSOMEDextransDEXTRAN DERIVATIVEBIOLOGICAL-MEMBRANESFluoresceinsMembraneCarbohydrate SequenceESCHERICHIA-COLIMonosaccharide Transport ProteinsCations DivalentMembrane FluidityProteolipidsMolecular Sequence DataBiophysicsPhospholipidFluorescence PolarizationLactose transportOXIDASECYTOCHROME-CVESICLESElectron Transport Complex IVHYDROPHOBIC ANCHOR GROUPEscherichia coliAnimalsKINETICSChromatographyMyocardiumMembrane ProteinsMembrane Transport ProteinsBiological membraneCell BiologyPROTON-MOTIVE FORCEMembrane proteinchemistryLiposomesCalciumCattleBiochimica et Biophysica Acta (BBA) - Biomembranes
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Confocal laser endomicroscopy is a new imaging modality for recognition of intramucosal bacteria in inflammatory bowel disease in vivo.

2011

International audience; BACKGROUND AND OBJECTIVES: Interaction of bacteria with the immune system within the intestinal mucosa plays a key role in the pathogenesis of inflammatory bowel disease (IBD). The aim of the current study was to develop a fluorescein-aided confocal laser endomicroscopy (CLE) method to visualise intramucosal enteric bacteria in vivo and to determine the involved mucosal area in the colon and ileum in patients with ulcerative colitis (UC) and Crohn's disease (CD). METHODS: Initially, E coli strains expressing enhanced green fluorescent protein (pEGFP) were endomicroscopically imaged in mice. In addition, ex vivo and in vivo imaging of fluorescent human enteric bacteri…

PathologyMESH : Escherichia colifluoresceinMESH : Retrospective StudiesColorectal cancerMESH : Prospective StudiesGastroenterologyInflammatory bowel disease[ SDV.CAN ] Life Sciences [q-bio]/Cancer0302 clinical medicineIntestinal mucosaMESH: Microscopy ConfocalMESH: AnimalsMESH : Colonoscopy1506MESH: In Situ Hybridization Fluorescenceintramucosal bacteria0303 health sciencesCrohn's diseaseMESH: Escherichia coliGastroenterologyMESH : EnterobacteriaceaeMESH : Colitis UlcerativeUlcerative colitisenteric bacterial microflora3. Good healthMESH : In Situ Hybridization FluorescenceCrohn's diseaseMESH: Colonoscopyconfocal laser endomicroscopyMESH: Intestinal MucosaMESH : Inflammatory Bowel Diseases030211 gastroenterology & hepatologymedicine.medical_specialtyMESH : MaleMESH: Colitis Ulcerative[SDV.CAN]Life Sciences [q-bio]/CancerMESH : Mice Inbred C57BLBiologyMESH : Intestinal MucosaMESH : Crohn Disease03 medical and health sciencesMESH: EnterobacteriaceaeFISHfluorescence endoscopyIn vivoMESH: Mice Inbred C57BLInternal medicineMESH : MicemedicineEndomicroscopyMESH: ColonMESH : Microscopy ConfocalMESH: Miceulcerative colitis030304 developmental biologyMESH : IleumMESH: HumansBacteriaMESH: Crohn Diseaseinfectious colitisMESH : HumansEndoscopyMESH: Retrospective Studiesmedicine.diseaseMESH: Inflammatory Bowel DiseasesMESH : ColonMESH: MaleMESH: Prospective StudiesMESH: IleumMESH : AnimalsEx vivo
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Surface Components of Escherichia coli That Mediate Resistance to the Bactericidal Activities of Serum and Phagocytes

1985

Microorganisms that enter the animal body, either actively or passively, encounter a battery of nonspecific and specific chemical and cellular defenses whose role is to inactivate and eliminate foreign materials. Successful pathogens have the ability to avoid, resist, or inactivate these defenses for at least the period necessary for initiation of the disease process.

PhagocytebiologyPhagocytosisBlood Bactericidal Activitymedicine.disease_causebiology.organism_classificationEnterobacteriaceaeBacterial geneticsMicrobiologymedicine.anatomical_structuremedicineAnimal bodyEscherichia coliBacteria
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One-step synthesis, crystallographic studies and antimicrobial activity of new 4-diazopyrazole derivatives

1996

Summary A number of new 4-diazopyrazole derivatives were prepared by the reaction of 1- R -3-methyl-5(R 1 -substituted)benzamidopyrazoles with a sevenfold excess of nitrous acid in acetic medium. The compounds were tested for activity against Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, Staphylococcus epidermidis, Streptococcus faecalis, Listeria monocytogenes, Candida albicans, Candida tropicalis and Paecilomyces varioti . The highest microbial susceptibility was shown by Gram-positive bacteria, with minimum inhibitory concentrations (MIC) in the range 0.5–12.5 μg/mL. For S aureus the R 1 substituents were screened utilizing the Topliss operational scheme. The 4-nitro g…

PharmacologybiologyStereochemistryChemistryOrganic ChemistryGeneral Medicinebiology.organism_classificationAntimicrobialmedicine.disease_causeCandida tropicalisStaphylococcus epidermidisStaphylococcus aureusDrug DiscoverymedicineCandida albicansAntibacterial activityEscherichia coliAntibacterial agentEuropean Journal of Medicinal Chemistry
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TiO2 Supported over Hβ and HZSM-5 Photocatalysts for Salmonelle and Escherichia Coli Disinfection

2008

Photocatalysis TiO2 HZSM-5 Salmonelle Escherichia Coli
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Functioning of DcuC as the C 4 -Dicarboxylate Carrier during Glucose Fermentation by Escherichia coli

1999

ABSTRACT The dcuC gene of Escherichia coli encodes an alternative C 4 -dicarboxylate carrier (DcuC) with low transport activity. The expression of dcuC was investigated. dcuC was expressed only under anaerobic conditions; nitrate and fumarate caused slight repression and stimulation of expression, respectively. Anaerobic induction depended mainly on the transcriptional regulator FNR. Fumarate stimulation was independent of the fumarate response regulator DcuR. The expression of dcuC was not significantly inhibited by glucose, assigning a role to DcuC during glucose fermentation. The inactivation of dcuC increased fumarate-succinate exchange and fumarate uptake by DcuA and DcuB, suggesting a…

Physiology and MetabolismMolecular Sequence DataMutantStimulationBiologymedicine.disease_causeMicrobiologyBacterial ProteinsFumaratesConsensus SequenceEscherichia colimedicineTranscriptional regulationDicarboxylic AcidsAnaerobiosisPromoter Regions GeneticMolecular BiologyEscherichia coliPsychological repressionDicarboxylic Acid TransportersBinding SitesBase SequenceEscherichia coli ProteinsSuccinatesGene Expression Regulation BacterialKineticsResponse regulatorGlucoseBiochemistryFermentationFermentationEffluxCarrier ProteinsRibosomesJournal of Bacteriology
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Regulation of aerobic and anaerobic D-malate metabolism of Escherichia coli by the LysR-type regulator DmlR (YeaT).

2010

ABSTRACT Escherichia coli K-12 is able to grow under aerobic conditions on d -malate using DctA for d -malate uptake and the d -malate dehydrogenase DmlA (formerly YeaU) for converting d -malate to pyruvate. Induction of dmlA encoding DmlA required an intact dmlR (formerly yeaT ) gene, which encodes DmlR, a LysR-type transcriptional regulator. Induction of dmlA by DmlR required the presence of d -malate or l - or meso -tartrate, but only d -malate supported aerobic growth. The regulator of general C 4 -dicarboxylate metabolism (DcuS-DcuR two-component system) had some effect on dmlA expression. The anaerobic l -tartrate regulator TtdR or the oxygen sensors ArcB-ArcA and FNR did not have a m…

Physiology and MetabolismRegulatorMalatesDehydrogenasemedicine.disease_causeMicrobiologyMalate dehydrogenaseMicrobiologyMalate DehydrogenasemedicineAnaerobiosisMolecular BiologyEscherichia coliTartratesChromatography High Pressure LiquidbiologyEscherichia coli K12Escherichia coli ProteinsMetabolismGene Expression Regulation Bacterialbiology.organism_classificationbeta-GalactosidaseAerobiosisBiochemistryMutationFermentationAnaerobic exerciseBacteriaJournal of bacteriology
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Thermostability of Two Cyanobacterial GrpE Thermosensors

2011

GrpE proteins act as co-chaperones for DnaK heat-shock proteins. The dimeric protein unfolds under heat stress conditions, which results in impaired interaction with a DnaK protein. Since interaction of GrpE with DnaK is crucial for the DnaK chaperone activity, GrpE proteins act as a thermosensor in bacteria. Here we have analyzed the thermostability and function of two GrpE homologs of the mesophilic cyanobacterium Synechocystis sp. PCC 6803 and of the thermophilic cyanobacterium Thermosynechococcus elongatus BP1. While in Synechocystis an N-terminal helix pair of the GrpE dimer appears to be the thermosensing domain and mainly mediates GrpE dimerization, the C-terminal four-helix bundle i…

PhysiologyMolecular Sequence DataProtein domainPlant SciencePlasma protein bindingCyanobacteriaProtein structureBacterial ProteinsHeat shock proteinEscherichia coliAmino Acid SequencePeptide sequenceHeat-Shock ProteinsThermostabilitySequence Homology Amino AcidbiologyProtein StabilityChemistryCircular DichroismGenetic Complementation TestSynechocystisSynechocystisTemperatureCell BiologyGeneral Medicinebiology.organism_classificationProtein Structure TertiaryCross-Linking ReagentsChaperone (protein)Biophysicsbiology.proteinbacteriaProtein MultimerizationProtein BindingPlant and Cell Physiology
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