Search results for "binding site"

showing 10 items of 856 documents

Guanosine-Mediated Anxiolytic-Like Effect: Interplay with Adenosine A1 and A2A Receptors

2020

Acute or chronic administration of guanosine (GUO) induces anxiolytic-like effects, for which the adenosine (ADO) system involvement has been postulated yet without a direct experimental evidence. Thus, we aimed to investigate whether adenosine receptors (ARs) are involved in the GUO-mediated anxiolytic-like effect, evaluated by three anxiety-related paradigms in rats. First, we confirmed that acute treatment with GUO exerts an anxiolytic-like effect. Subsequently, we investigated the effects of pretreatment with ADO or A1R (CPA, CCPA) or A2AR (CGS21680) agonists 10 min prior to GUO on a GUO-induced anxiolytic-like effect. All the combined treatments blocked the GUO anxiolytic-like effect, …

LightPharmacologyAnxietySettore BIO/09 - FisiologiaHippocampuslcsh:Chemistrychemistry.chemical_compound0302 clinical medicineReceptorlcsh:QH301-705.5Spectroscopycaffeine0303 health sciencesBehavior AnimalRGeneral MedicineDarkness3. Good healthComputer Science ApplicationsadenosineCCPA[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]A<sub>1</sub>RCaffeineA1Rmedicine.drugReceptor Adenosine A2A1GuanosineCatalysisArticleInorganic Chemistry03 medical and health sciencesAmedicineAnimals[SDV.NEU] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]Physical and Theoretical ChemistryBinding site2AMolecular Biology030304 developmental biologyDose-Response Relationship DrugReceptor Adenosine A1behaviorOrganic ChemistryCell MembraneAntagonistAdenosineAdenosine receptorRatsguanosineA<sub>2A</sub>Rlcsh:Biology (General)lcsh:QD1-999chemistryA2AR030217 neurology & neurosurgery
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Photoaffinity Labeling and Photoaffinity Cross-Linking of Phosphofructokinase-1 from Saccharomyces cerevisiae by 8-Azidoadeninenucleotides

2001

Phosphofructokinase-1 from Saccharomyces cerevisiae is composed of four alpha- and four beta-subunits, each of them carrying catalytic and regulatory bindings sites for MgATP. In this paper, various photoaffinity labels, such as 8-azidoadenosine 5'-triphosphate, 8-azido-1,N6-ethenoadenosine 5'-triphosphate, and 8-N3-3'(2')-O-biotinyl-8-azidoadenosine 5'-triphosphate have been used to study their interaction with the enzyme in the dark and during irradiation. All nucleotidetriphosphates function as phosphate donor forming fructose 1,6-bisphosphate from fructose 6-phosphate. However, the kinetic analysis revealed distinctly differences between them. Photolabeling causes a decrease in enzyme a…

LightPhosphofructokinase-1Blotting WesternSaccharomyces cerevisiaeBiophysicsPhotoaffinity LabelsSaccharomyces cerevisiaePhotoaffinity LabelsBiochemistryAdenosine TriphosphateFructosediphosphatesChymotrypsinMagnesiumPhosphofructokinase 1Molecular Biologychemistry.chemical_classificationGel electrophoresisBinding SitesAffinity labelingbiologyPhotoaffinity labelingFructosephosphatesDarknessbiology.organism_classificationEnzyme assayKineticsProtein SubunitsCross-Linking ReagentsEnzymechemistryBiochemistrybiology.proteinElectrophoresis Polyacrylamide GelArchives of Biochemistry and Biophysics
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Molybdenum Trioxide Nanoparticles with Intrinsic Sulfite Oxidase Activity

2014

Sulfite oxidase is a mitochondria-located molybdenum-containing enzyme catalyzing the oxidation of sulfite to sulfate in the amino acid and lipid metabolism. Therefore, it plays a major role in detoxification processes, where defects in the enzyme cause a severe infant disease leading to early death with no efficient or cost-effective therapy in sight. Here we report that molybdenum trioxide (MoO3) nanoparticles display an intrinsic biomimetic sulfite oxidase activity under physiological conditions, and, functionalized with a customized bifunctional ligand containing dopamine as anchor group and triphenylphosphonium ion as targeting agent, they selectively target the mitochondria while bein…

LightPhotochemistryMetal NanoparticlesGeneral Physics and AstronomyMolybdenum trioxidechemistry.chemical_compoundSulfiteSulfite oxidaseElectrochemistryNanotechnologyGeneral Materials ScienceBifunctionalAmino Acid Metabolism Inborn ErrorsElectrodesSulfite oxidase deficiencyMolybdenumchemistry.chemical_classificationPhotonsBinding SitesNanowiresSulfite OxidaseGeneral EngineeringOxidesAmino acidKineticsEnzymechemistryBiochemistryNanoparticlesEnzyme mimicElectronicsZinc OxideOxidation-ReductionACS Nano
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IL-9 and IL-13 production by activated mast cells is strongly enhanced in the presence of lipopolysaccharide: NF-kappa B is decisively involved in th…

2001

Abstract Mast cells, due to their ability to produce a large panel of mediators and cytokines, participate in a variety of processes in adaptive and innate immunity. Herein we report that in primary murine bone marrow-derived mast cells activated with ionomycin or IgE-Ag the bacterial endotoxin LPS strongly enhances the expression of IL-9 and IL-13, but not IL-4. This costimulatory effect of LPS is absent in activated mast cells derived from the LPS-hyporesponsive mouse strain BALB/c-LPSd, although in these cells the proinflammatory cytokine IL-1 can still substitute for LPS. The enhanced production of mast cell-derived IL-13 in the presence of IL-1 is a novel observation. Coactivation of m…

LipopolysaccharidesImmunologyInflammationBone Marrow CellsBiologyProinflammatory cytokinechemistry.chemical_compoundMiceMice CongenicAdjuvants ImmunologicmedicineImmunology and AllergyAnimalsMast CellsPromoter Regions GeneticCells CulturedReporter geneMice Inbred BALB CMice Inbred C3HInnate immune systemBinding SitesInterleukin-13Interleukin-9NF-kappa BNFKB1Cell biologyInterleukin 33chemistryGene Expression RegulationIonomycinInterleukin 13Immunologymedicine.symptomSignal TransductionJournal of immunology (Baltimore, Md. : 1950)
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Mice Expressing Only Covalent Dimeric Heparin Binding-deficient Lipoprotein Lipase

2004

Lipoprotein lipase (LpL) hydrolyzes triglycerides of circulating lipoproteins while bound as homodimers to endothelial cell surface heparan sulfate proteoglycans. This primarily occurs in the capillary beds of muscle and adipose tissue. By creating a mouse line that expresses covalent dimers of heparin-binding deficient LpL (hLpLHBM-Dimer) in muscle, we confirmed in vivo that linking two LpL monomers in a head to tail configuration creates a functional LpL. The hLpLHBM-Dimer transgene produced abundant activity and protein in muscle, and the LpL was the expected size of a dimer (approximately 110 kDa). Unlike the heparin-binding mutant monomer, hLpLHBM-Dimer had the same stability as nonmut…

Lipoprotein lipaseCOS cellsChemistryTransgenedigestive oral and skin physiologynutritional and metabolic diseasesAdipose tissueCell BiologyTransfectionBiochemistryMolecular biologyEndothelial stem cellBiochemistrylipids (amino acids peptides and proteins)SecretionBinding siteMolecular BiologyJournal of Biological Chemistry
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Interaction of Quinine with Model Lipid Membranes of Different Compositions

2002

The binding of a drug such as Quinine with neutral and negatively charged small unilamellar lipid vesicles at pH 7 and 37 degrees C was investigated. Changes in the fluorescence properties of the drug after association with the liposomes were used to obtain binding isotherms over a range of phospholipid compositions at different ionic strengths. Under such conditions, the association was strongly enhanced by the negative net charge of the bilayer but diminished by the increasing presence of electrolytes in the aqueous media. Binding data were analyzed in terms of a surface partition equilibrium without and after correcting for electrostatic effects by means of the Gouy-Chapman theory. The i…

LiposomeBinding SitesChromatographyQuinineChemistryBilayerLipid BilayersStatic ElectricityPhospholipidPharmaceutical ScienceMembranes ArtificialPhosphatidylglycerolsBinding constantPartition coefficientHydrophobic effectchemistry.chemical_compoundIonic strengthPartition equilibriumBiophysicsJournal of Pharmaceutical Sciences
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Triazolopyridopyrimidines: an emerging family of effective DNA photocleavers. DNA binding. Antileishmanial activity.

2015

Triazolopyridopyrimidines 3-phenyl-6,8-di(2-pyridyl)-[1,2,3]triazolo[5',1':6,1]pyrido[2,3-d]pyrimidine (1a), 6,8-di(pyridin-2-yl)-[1,2,3]triazolo[1',5':1,6]pyrido[2,3-d]pyrimidine (1b) and 3-methyl-6,8-di(2-pyridyl)-[1,2,3]triazolo[5',1':6,1]pyrido[2,3-d]pyrimidine (1c) were prepared and their electrochemical and luminescence properties were studied in depth. The DNA binding ability of this series of compounds has been investigated by means of UV-vis absorption and fluorescence titrations, steady-state emission quenching with ferrocyanide as well as viscosity measurements. Results have shown that triazolopyridopyrimidine 1a interacts strongly at DNA grooves. This compound also displays pref…

LuminescencePyrimidineStereochemistryGuaninePyridinesUltraviolet RaysRadicalTriazoleSubstituentAntiprotozoal AgentsBiochemistrychemistry.chemical_compoundStructure-Activity RelationshipParasitic Sensitivity TestsStructure–activity relationshipPhysical and Theoretical ChemistryBinding siteDNA CleavageLeishmaniaBinding SitesDose-Response Relationship DrugMolecular StructureOrganic ChemistryDNAPhotochemical ProcesseschemistryHeterocyclic Compounds 3-RingDNAOrganicbiomolecular chemistry
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Transcription factor NRF2 regulates miR-1 and miR-206 to drive tumorigenesis

2013

The mechanisms by which deregulated nuclear factor erythroid-2–related factor 2 (NRF2) and kelch-like ECH-associated protein 1 (KEAP1) signaling promote cellular proliferation and tumorigenesis are poorly understood. Using an integrated genomics and 13C-based targeted tracer fate association (TTFA) study, we found that NRF2 regulates miR-1 and miR-206 to direct carbon flux toward the pentose phosphate pathway (PPP) and the tricarboxylic acid (TCA) cycle, reprogramming glucose metabolism. Sustained activation of NRF2 signaling in cancer cells attenuated miR-1 and miR-206 expression, leading to enhanced expression of PPP genes. Conversely, overexpression of miR-1 and miR-206 decreased the exp…

Lung NeoplasmsCell SurvivalNF-E2-Related Factor 2Citric Acid CycleMice NudeBiologymedicine.disease_causeMiceRNA interferenceCarcinoma Non-Small-Cell LungCell Line TumormicroRNAGene expressionmedicineAnimalsHumansTranscription factor3' Untranslated RegionsCell ProliferationOligonucleotide Array Sequence AnalysisRegulation of gene expressionBinding SitesBase SequenceGeneral MedicineMolecular biologyHDAC4Cell biologyTumor BurdenGene Expression Regulation NeoplasticMicroRNAsCell Transformation NeoplasticGlucoseRNA InterferenceHistone deacetylaseCarcinogenesisTranscriptomeOxidation-ReductionNeoplasm TransplantationResearch Article
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Analysis of cell-free human alpha1 integrin with a monoclonal antibody to the I-domain: detection in ocular fluid and function as an adhesion substra…

2002

The alpha1 beta1 integrin, an inserted (1) domain containing collagen receptor, is expressed in the cell surface membrane of normal and malignant cells, and may play a role in their migration through tissues or in metastatic spread. Here we report that a functional anti-human alpha1beta1 integrin monoclonal antibody (mAb) (1B3.1) directly and specifically binds plastic bound recombinant human alpha1 I-domain protein containing the collagen binding site. Detection was diminished by acidification of the I-domain protein but was enhanced by increasing concentrations of Mg2+ cation. Furthermore, we detected binding of the mAb to proteins from the ocular fluids of 6 patients, with the highest co…

Lung Neoplasmsmedicine.drug_classClinical BiochemistryIntegrinIntegrin alpha1Enzyme-Linked Immunosorbent AssayAdenocarcinomaMonoclonal antibodyCD49bCataractCollagen receptorlaw.inventionIntegrin alpha1beta1Aqueous HumorlawCationsmedicineHumansBinding sitebiologyCell-Free SystemChemistryEye NeoplasmsAntibodies MonoclonalCell BiologyGeneral MedicineAdhesionMolecular biologyProtein Structure TertiaryIntegrin alpha Mbiology.proteinRecombinant DNACell Adhesion MoleculesCell communicationadhesion
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Neuroglobin and Other Hexacoordinated Hemoglobins Show a Weak Temperature Dependence of Oxygen Binding

2004

AbstractMouse and human neuroglobins, as well as the hemoglobins from Drosophila melanogaster and Arabidopsis thaliana, were recombinantly expressed in Escherichia coli, and their ligand-binding properties were studied versus temperature. These globins have a common feature of being hexacoordinated (via the distal histidine) under deoxy conditions, as evidenced by a large amplitude for the alpha absorption band at 560nm and the Soret band at 426nm. The transition from the hexacoordinated form to the CO bound species is slow, as expected for a replacement reaction Fe-His → Fe → FeCO. The intrinsic binding rates would indicate a high oxygen affinity for the pentacoordinated form, due to rapid…

Macromolecular SubstancesProtein ConformationBiophysicschemistry.chemical_elementNeuroglobinNerve Tissue ProteinsBiologyLigandsOxygenDissociation (chemistry)HemoglobinsMiceSpecies SpecificityAnimalsDrosophila ProteinsHumansGlobinBinding siteBinding SitesArabidopsis ProteinsTemperatureProteinsLigand (biochemistry)GlobinsOxygenCrystallographyKineticsBiochemistrychemistryNeuroglobinOxygen bindingProtein ligandProtein BindingBiophysical Journal
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