Search results for "Erich"

showing 10 items of 805 documents

Structure-Function Relationship of Substituted Bromomethylcoumarins in Nucleoside Specificity of RNA Alkylation

2013

Selective alkylation of RNA nucleotides is an important field of RNA biochemistry, e.g. in applications of fluorescent labeling or in structural probing experiments, yet detailed structure-function studies of labeling agents are rare. Here, bromomethylcoumarins as reactive compounds for fluorescent labeling of RNA are developed as an attractive scaffold on which electronic properties can be modulated by varying the substituents. Six different 4-bromomethyl-coumarins of various substitution patterns were tested for nucleotide specificity of RNA alkylation using tRNA from Escherichia coli as substrate. Using semi-quantitative LC-MS/MS analysis, reactions at mildly acidic and slightly alkaline…

AlkylationStaining and LabelingScienceQRNucleosidesRNA BacterialStructure-Activity RelationshipRNA TransferCoumarinsEscherichia coliMedicine500 Natural sciences and mathematics500 NaturwissenschaftenResearch ArticleFluorescent DyesPLoS ONE
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CyaC, a redox-regulated adenylate cyclase of Sinorhizobium meliloti with a quinone responsive diheme-B membrane anchor domain.

2019

The nucleotide cyclase CyaC of Sinorhizobium meliloti is a member of class III adenylate cyclases (AC), a diverse group present in all forms of life. CyaC is membrane-integral by a hexahelical membrane domain (6TM) with the basic topology of mammalian ACs. The 6TM domain of CyaC contains a tetra-histidine signature that is universally present in the membrane anchors of bacterial diheme-B succinate-quinone oxidoreductases. Heterologous expression of cyaC imparted activity for cAMP formation from ATP to Escherichia coli, whereas guanylate cyclase activity was not detectable. Detergent solubilized and purified CyaC was a diheme-B protein and carried a binuclear iron-sulfur cluster. Single poin…

Amino Acid Transport SystemsAdenylate kinasemedicine.disease_causeMicrobiologyCyclase03 medical and health sciencesmedicineBenzoquinonesNucleotideHistidineAmino Acid SequenceMolecular BiologyEscherichia coliHistidine030304 developmental biologychemistry.chemical_classification0303 health sciencesSinorhizobium melilotibiology030306 microbiologyEscherichia coli ProteinsGuanylate cyclase activityQuinonesMembrane Proteinsbiology.organism_classificationchemistryBiochemistryGenes BacterialHeterologous expressionOxidation-ReductionAdenylyl CyclasesSinorhizobium melilotiMolecular microbiology
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Expression, purification, crystallization and preliminary X-ray analysis of strictosidine glucosidase, an enzyme initiating biosynthetic pathways to …

2005

Abstract Strictosidine β- d -glucosidase, a plant enzyme initiating biosynthetic pathways to about 2000 monoterpenoid indole alkaloids with an extremely large number of various carbon skeletons, has been functionally expressed in Escherichia coli and purified to homogeneity in mg scale. Crystals suitable for X-ray analysis were found by robot-mediated screening. Using the hanging-drop technique, optimum conditions were 0.3 M ammonium sulfate, 0.1 M sodium acetate, pH 4.6 and PEG 4000 (10%) as precipitant buffer. The crystals of strictosidine glucosidase belong to the space group P 42 1 2 with unit cell dimensions of a =157.63, c =103.59 A and diffract X-rays to 2.48-A resolution.

Ammonium sulfateCatharanthusStereochemistryBiophysicsCrystallography X-Raymedicine.disease_causeBiochemistryIndole AlkaloidsAnalytical Chemistrychemistry.chemical_compoundRauvolfia serpentinaPEG ratioEscherichia colimedicineCloning MolecularMolecular BiologyEscherichia colichemistry.chemical_classificationbiologyIndole alkaloidbiology.organism_classificationEnzymeBiochemistrychemistryStrictosidineCrystallizationSodium acetateGlucosidasesBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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Requirement for the Proton-Pumping NADH Dehydrogenase I of Escherichia Coli in Respiration of NADH to Fumarate and Its Bioenergetic Implications

1997

In Escherichia coli the expression of the nuo genes encoding the proton pumping NADH dehydrogenase I is stimulated by the presence of fumarate during anaerobic respiration. The regulatory sites required for the induction by fumarate, nitrate and O2 are located at positions around –309, –277, and downstream of –231 bp, respectively, relative to the transcriptional-start site. The fumarate regulator has to be different from the O2 and nitrate regulators ArcA and NarL. For growth by fumarate respiration, the presence of NADH dehydrogenase I was essential, in contrast to aerobic or nitrate respiration which used preferentially NADH dehydrogenase II. The electron transport from NADH to fumarate …

Anaerobic respirationAcetatesmedicine.disease_causeBiochemistryElectron TransportFumaratesEscherichia colimedicineDimethyl SulfoxideNADH NADPH OxidoreductasesAnaerobiosisEscherichia colichemistry.chemical_classificationElectron Transport Complex IEthanolbiologyNADH dehydrogenaseGene Expression Regulation BacterialProton PumpsElectron acceptorFumarate reductaseNADElectron transport chainGlycerol-3-phosphate dehydrogenaseBiochemistrychemistryElectron Transport Complex Ibiology.proteinEnergy MetabolismEuropean Journal of Biochemistry
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Transport of C(4)-dicarboxylates in Wolinella succinogenes.

2000

ABSTRACT C 4 -dicarboxylate transport is a prerequisite for anaerobic respiration with fumarate in Wolinella succinogenes , since the substrate site of fumarate reductase is oriented towards the cytoplasmic side of the membrane. W. succinogenes was found to transport C 4 -dicarboxylates (fumarate, succinate, malate, and aspartate) across the cytoplasmic membrane by antiport and uniport mechanisms. The electrogenic uniport resulted in dicarboxylate accumulation driven by anaerobic respiration. The molar ratio of internal to external dicarboxylate concentration was up to 10 3 . The dicarboxylate antiport was either electrogenic or electroneutral. The electroneutral antiport required the prese…

Anaerobic respirationAntiporterPhysiology and MetabolismMutantMalatesBiologymedicine.disease_causeMicrobiologyCell membraneElectron TransportOxygen ConsumptionBacterial ProteinsFumaratesRespirationmedicineDicarboxylic AcidsAnaerobiosisMolecular BiologyEscherichia coliDicarboxylic Acid TransportersAspartic AcidNitratesEscherichia coli ProteinsCell MembraneSodiumMembrane ProteinsBiological TransportSuccinatesFumarate reductaseElectron transport chainWolinellamedicine.anatomical_structureBiochemistryMutagenesisCarrier ProteinsGene DeletionJournal of bacteriology
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Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors

1997

AbstractThe electron-transport chains of Escherichia coli are composed of many different dehydrogenases and terminal reductases (or oxidases) which are linked by quinones (ubiquinone, menaquinone and demethylmenaquinone). Quinol:cytochrome c oxido-reductase (`bc1 complex') is not present. For various electron acceptors (O2, nitrate) and donors (formate, H2, NADH, glycerol-3-P) isoenzymes are present. The enzymes show great variability in membrane topology and energy conservation. Energy is conserved by conformational proton pumps, or by arrangement of substrate sites on opposite sides of the membrane resulting in charge separation. Depending on the enzymes and isoenzymes used, the H+/e− rat…

Anaerobic respirationTranscription GeneticCellular respirationFNRBiophysicsBiochemistryElectron TransportOxygen sensorOxygen ConsumptionBacterial Proteins(Escherichia coli)Escherichia coliProtein phosphorylationAnaerobiosischemistry.chemical_classificationbiologyCytochrome cQuinonesArcAGene Expression Regulation BacterialCell BiologyElectron acceptorElectron transport chainAerobiosisAerobic electron transportResponse regulatorAnaerobic electron transportBiochemistrychemistrybiology.proteinCarrier ProteinsEnergy MetabolismOxidoreductasesFlux (metabolism)RegulationBiochimica et Biophysica Acta (BBA) - Bioenergetics
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Anionic Lipids Modulate the Activity of the Aquaglyceroporin GlpF

2015

AbstractThe structure and composition of a biological membrane can severely influence the activity of membrane-embedded proteins. Here, we show that the E. coli aquaglyceroporin GlpF has only little activity in lipid bilayers formed from native E. coli lipids. Thus, at first glance, GlpF appears to not be optimized for its natural membrane environment. In fact, we found that GlpF activity was severely affected by negatively charged lipids regardless of the exact chemical nature of the lipid headgroup, whereas GlpF was not sensitive to changes in the lateral membrane pressure. These observations illustrate a potential mechanism by which the activity of an α-helical membrane protein is modula…

AnionsLiposomeMembranesEscherichia coli ProteinsBiophysicsAquaporinBiological membraneBiologyAquaporinsLipidsCell biologyMembraneMembrane proteinNegative chargeLiposomesEscherichia colilipids (amino acids peptides and proteins)Lipid bilayerPotential mechanismBiophysical Journal
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Anthemis wiedemanniana essential oil prevents LPS-induced production of NO in RAW 264.7 macrophages and exerts antiproliferative and antibacterial ac…

2012

Anthemis wiedemanniana is known in folk medicine for the treatment of microbial infections, cancer and also urinary and pulmonary problems. In this study, the chemical composition of the essential oil from A. wiedemanniana was evaluated and its antibacterial activity was tested against 10 bacterial strains. The oil was also tested for its potentiality to inhibit nitric oxide production in RAW 264.7 macrophages and for its cytotoxicity against four human cancer cell lines. A. wiedemanniana oil, rich of oxygenated monoterpenes (25.4%), showed a good antibacterial activity against Gram-positive bacteria and a good activity against the two Gram-negative bacteria, Escherichia coli and Proteus vu…

Anthemis wiedemanniana essential oil antiproliferative activity antibacterial activityLipopolysaccharidesProteus vulgarisPlant ScienceMicrobial Sensitivity Testsmedicine.disease_causeGram-Positive BacteriaBiochemistryAnalytical ChemistryNitric oxideMicrobiologylaw.inventionCell Linechemistry.chemical_compoundMicelawCell Line TumormedicineEscherichia coliOils VolatileAnimalsHumansAnthemisSettore BIO/15 - Biologia FarmaceuticaCytotoxicityEscherichia coliEssential oilNitritesCell ProliferationbiologyOrganic ChemistrySettore CHIM/06 - Chimica Organicabiology.organism_classificationProteusAntineoplastic Agents PhytogenicAnti-Bacterial AgentschemistryMonoterpenesAnthemisAntibacterial activityBacteriaNatural product research
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Anti-Pseudomonas aeruginosa activity of hemlock (Conium maculatum, Apiaceae) essential oil

2018

Conium maculatum is a nitrophilous weed belonging to the Apiaceae family and occurring in hedgerows, pastures, waste ground, along rivers and roadsides. Little is known on the chemistry and bioactivity of other secondary metabolites occurring in the plant. In the present work, we have analysed the chemical composition and antimicrobial activity of the essential oils hydrodistilled from leaves and inflorescenes of C. maculatum growing in Sicily, Italy. The composition of essential oils was achieved by gas chromatography-mass spectrometry (GC-MS) analysis, whereas the inhibitory effects on the growth of two Gram negative strains, namely Escherichia coli and Pseudomonas aeruginosa were assesse…

Anti-Infective AgentAlkeneved/biology.organism_classification_rank.speciesPlant Sciencemedicine.disease_cause01 natural sciencesBiochemistryConium maculatumessential oilGas Chromatography-Mass SpectrometryAnalytical Chemistrylaw.inventionchemistry.chemical_compoundPiperidinelawBotanymedicineEscherichia coliOils Volatilechemical compositionSicilyEssential oilDistillationAcyclic MonoterpeneApiaceaeantimicrobial activitybiology010405 organic chemistryved/biologyPseudomonas aeruginosaMicrobial Sensitivity TestOrganic ChemistryConium maculatumAntimicrobialbiology.organism_classificationHemlock0104 chemical sciences010404 medicinal & biomolecular chemistrychemistryMyrcenePseudomonas aeruginosaComposition (visual arts)WeedPlant LeaveApiaceae
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CrELISA: a fast and robust enzyme-linked immunosorbent assay bypassing the need for purification of recombinant protein

2004

A multitude of antigens has been recently identified by screening of cDNA expression libraries derived from human tumors with autologous sera. Using a phage autoantibody assay and small panels of sera derived from cancer patients or controls it has been shown that some of these antigens display cancer-associated autoantibody responses. The diagnostic and prognostic significance of these potentially cancer-related autoantibodies remains unclear until large-scale assays are developed and serological data are available for hundreds of cancer patients and controls. The major bottleneck for the development of large-scale assays are the cloning, expression and the purification of each of the resp…

Antibodies NeoplasmImmunologyEnzyme-Linked Immunosorbent AssayBiologyAutoantigensSerologylaw.inventionAntigenAntigens NeoplasmlawEscherichia colimedicineHumansImmunology and AllergyAutoantibodiesCloningchemistry.chemical_classificationAutoantibodyMembrane ProteinsCancermedicine.diseaseVirologyMolecular biologyRecombinant ProteinsTumor antigenEnzymechemistryRecombinant DNAJournal of Immunological Methods
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