Search results for "Erich"

showing 10 items of 805 documents

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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Synthesis of recombinant atrial natriuretic peptide (rANP) using hybrid fusion protein-phage fr coat/ANP (CP/ANP).

1997

Abstract Baumanis, V., I. Jansone, A. Skangals, I. Mandrika and V. Berzins. Synthesis of recombinant atrial natriuretic peptide (rANP) using hybrid fusion protein-phage fr coat/ANP (CP/ANP). Peptides 18(8) 1229–1235, 1997.—Recombinant atrial natriuretic peptide (rANP) was expressed in and isolated from E. coli. rANP was purified using HPLC. Amino acid analysis, partial sequencing, and molecular mass were determined. Fused protein was used to rise polyclonal antibodies and to develop of immunoenzymatic assays of rANP and CP/ANP. Experiments were designed to study rANP effects on isolated rabbit aortic strips and to examine hypotensive, diuretic, and natriuretic activity, as well as renal cre…

PhysiologyMuscle RelaxationRecombinant Fusion ProteinsRenal functionEnzyme-Linked Immunosorbent AssayIn Vitro TechniquesBiochemistryMuscle Smooth Vascularlaw.inventionCellular and Molecular NeuroscienceEndocrinologyCapsidAtrial natriuretic peptideIn vivolawEscherichia coliAnimalsAntihypertensive AgentsAortaChromatography High Pressure LiquidbiologyMolecular massChemistryMetalloendopeptidasesFusion proteinNPR2DiuresisRatsBiochemistryPolyclonal antibodiescardiovascular systembiology.proteinRecombinant DNACapsid ProteinsRabbitshormones hormone substitutes and hormone antagonistsAtrial Natriuretic Factorcirculatory and respiratory physiologyGlomerular Filtration RatePeptides
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Identification of the Weevil immune genes and their expression in the bacteriome tissue

2008

Abstract Background Persistent infections with mutualistic intracellular bacteria (endosymbionts) are well represented in insects and are considered to be a driving force in evolution. However, while pathogenic relationships have been well studied over the last decades very little is known about the recognition of the endosymbionts by the host immune system and the mechanism that limits their infection to the bacteria-bearing host tissue (the bacteriome). Results To study bacteriome immune specificity, we first identified immune-relevant genes of the weevil Sitophilus zeamais by using suppressive subtractive hybridization (SSH) and then analyzed their full-length coding sequences obtained b…

PhysiologyPlant Scienceprotéines et peptides de signalisation intracellulaireStructural BiologyGene expressionlcsh:QH301-705.5Genetics0303 health sciencesAgricultural and Biological Sciences(all)EndosymbiosisReverse Transcriptase Polymerase Chain ReactionMicrobiology and ParasitologyIntracellular Signaling Peptides and ProteinsMicrobiologie et ParasitologielarveLarva1-1-1 Article périodique à comité de lectureInsect ProteinsGeneral Agricultural and Biological SciencesResearch ArticleBiotechnologyexpression géniquecharanconMolecular Sequence DatamuramidaseBiologyGeneral Biochemistry Genetics and Molecular BiologyMicrobiology03 medical and health sciencesAposymbioticcurculionidaeImmune systemEscherichia coliAnimalsGeneEcology Evolution Behavior and SystematicsAlphaproteobacteria030304 developmental biologyBiochemistry Genetics and Molecular Biology(all)030306 microbiologyTOLLIPIntracellular parasitefungiBacteriomeCell Biologybiochemical phenomena metabolism and nutritionGene Expression Regulationlcsh:Biology (General)WeevilsbacteriaCarrier ProteinsAntimicrobial Cationic Peptides[SDV.EE.IEO]Life Sciences [q-bio]/Ecology environment/SymbiosisDevelopmental BiologyBMC Biology
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Identification of a plasminogen-binding motif in PAM, a bacterial surface protein.

1995

Surface-associated plasmin(ogen) may contribute to the invasive properties of various cells. Analysis of plasmin(ogen)-binding surface proteins is therefore of interest. The N-terminal variable regions of M-like (ML) proteins from five different group A streptococcal serotypes (33, 41, 52, 53 and 56) exhibiting the plasminogen-binding phenotype were cloned and expressed in Escherichia coli. The recombinant proteins all bound plasminogen with high affinity. The binding involved the kringle domains of plasminogen and was blocked by a lysine analogue, 6-aminohexanoic acid, indicating that lysine residues in the M-like proteins participate in the interaction. Sequence analysis revealed that the…

PlasminStreptococcus pyogenesMolecular Sequence DataPlasma protein bindingBiologyMicrobiologyKringle domainBacterial ProteinsKringlesmedicineEscherichia coliAmino Acid SequenceBinding siteCloning MolecularMolecular BiologyPeptide sequenceBinding SitesBase SequenceLysinePlasminogenFusion proteinMolecular biologyRecombinant ProteinsPhenotypeBiochemistryCarrier ProteinsPlasminogen activatorSequence AlignmentBinding domainmedicine.drugProtein BindingMolecular microbiology
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Self-reporting hydrogels rapidly differentiate among enterohemorrhagic Escherichia coli (EHEC) and non-virulent Escherichia coli (K12)

2016

Abstract We report on the development of an autonomously reporting indicator hydrogel for the rapid and selective detection of enzymes secreted by the food-borne biosafety level 3 pathogen enterohemorrhagic Escherichia coli (E. coli) O157:H7 (EHEC) and the differentiation of this pathogen from the non-virulent E. coli strain K12. To introduce the sensing functionality, chitosan hydrogel films were equipped with fluorogenic substrates for the detection of α-galactosidase (α-Gal) and β-galactosidase (β-Gal), which are secreted by E. coli O157:H7, and β-glucuronidase (β-GUS), which is produced by the non-virulent E. coli K12 strain, but not by E. coli O157:H7, respectively. In the presence of …

Polymers and PlasticsGeneral Physics and AstronomyVirulence02 engineering and technology010402 general chemistrymedicine.disease_cause01 natural sciencesChitosanchemistry.chemical_compoundMaterials ChemistrymedicineEscherichia coliPathogenchemistry.chemical_classificationStrain (chemistry)biologyOrganic Chemistry021001 nanoscience & nanotechnologybiology.organism_classification0104 chemical sciencesEnzymechemistryBiochemistrySelf-healing hydrogels0210 nano-technologyBacteriaEuropean Polymer Journal
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Straightforward Approach for Preparing Durable Antibacterial ZnO Nanoparticle Coatings on Flexible Substrates

2022

Flexible antibacterial materials have gained utmost importance in protection from the distribution of bacteria and viruses due to the exceptional variety of applications. Herein, we demonstrate a readily scalable and rapid single-step approach for producing durable ZnO nanoparticle antibacterial coating on flexible polymer substrates at room temperature. Substrates used are polystyrene, poly(ethylene-co-vinyl acetate) copolymer, poly(methyl methacrylate), polypropylene, high density polyethylene and a commercial acrylate type adhesive tape. The deposition was achieved by a spin-coating process using a slurry of ZnO nanoparticles in toluene. A stable modification layer was obtained when tolu…

PolymersnanoparticleOrganic ChemistryE. coliPharmaceutical Sciencecoating:NATURAL SCIENCES::Physics [Research Subject Categories]S. aureus540ZnO; nanoparticle; coating; flexible substrate; antibacterial; <i>E. coli</i>; <i>S. aureus</i>Anti-Bacterial AgentsAnalytical Chemistryantibacterialflexible substrateChemistry (miscellaneous)Drug DiscoveryEscherichia coliSolventsZnOPolystyrenesMolecular MedicineZinc OxidePhysical and Theoretical ChemistryToluene
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