Search results for "Adenosine"

showing 10 items of 542 documents

ADENOSINE IS A MODULATOR OF THE CONTRACTILITY OF THE DUODENAL LONGITUDINAL MUSCLE IN MICE

2009

ADENOSINE DUODENUM CONTRACTILITYSettore BIO/09 - Fisiologia
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Nitensidine A, a guanidine alkaloid from Pterogyne nitens, is a novel substrate for human ABC transporter ABCB1.

2014

The Pterogyne nitens (Fabaceae) tree, native to South America, has been found to produce guanidine alkaloids as well as bioactive flavonols such as kaempferol, quercetin, and rutin. In the present study, we examined the possibility of interaction between human ATP-binding cassette (ABC) transporter ABCB1 and four guanidine alkaloids isolated from P. nitens (i.e., galegine, nitensidine A, pterogynidine, and pterogynine) using human T cell lymphoblast-like leukemia cell line CCRF-CEM and its multi-drug resistant (MDR) counterpart CEM/ADR5000. In XTT assays, CEM/ADR5000 cells were resistant to the four guanidine alkaloids compared to CCRF-CEM cells, although the four guanidine alkaloids exhibi…

ATP Binding Cassette Transporter Subfamily BLeukemia T-CellStereochemistryATPasePharmaceutical ScienceATP-binding cassette transporterGuanidineschemistry.chemical_compoundStructure-Activity RelationshipCell Line TumorDrug DiscoveryHumansheterocyclic compoundsBinding siteGuanidineCytotoxicityP-glycoproteinPharmacologyAdenosine TriphosphatasesbiologyPlant ExtractsAlkaloidFabaceaeFluoresceinsAntineoplastic Agents PhytogenicDrug Resistance MultipleMolecular Docking SimulationComplementary and alternative medicinechemistryBiochemistryVerapamilDrug Resistance Neoplasmbiology.proteinMonoterpenesMolecular MedicineATP-Binding Cassette TransportersKaempferolPhytotherapyPhytomedicine : international journal of phytotherapy and phytopharmacology
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Binding mode analysis of ABCA7 for the prediction of novel Alzheimer's disease therapeutics

2021

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ATP Adenosine-triphosphateNBD nucleotide binding domainGSH reduced glutathionePolypharmacologyAlzheimer’s disease (AD)ATP-binding cassette transporterHTS high-throughput screeningBiochemistryABCA7Structural BiologyPLIF protein ligand interactionMSD membrane spanning domainPDB protein data bankTM transmembrane helixABC ATP-binding cassetteMultitarget modulation (PANABC)RMSD root mean square distanceABC transporter (ABCA1 ABCA4 ABCA7)Computer Science ApplicationsMOE Molecular Operating EnvironmentPharmacophoreSNP single-nucleotide polymorphismBiotechnologyResearch ArticleBBB blood-brain barrierBiophysicsDrug designComputational biologyBiologyAD Alzheimer’s diseasePET positron emission tomographyIC intracellular helixAPP amyloid precursor proteincryo-EM cryogenic-electron microscopyGeneticsHomology modelingBinding siteRational drug design and developmentComputingMethodologies_COMPUTERGRAPHICSNBD-cholesterol 7-nitro-2-13-benzoxadiazol-4-yl-cholesterolTransporterPSO particle swarm optimizationPET tracer (PETABC)ECD extracellular domainR-domain/region regulatory domain/regionABCA1biology.proteinEH extracellular helixTP248.13-248.65BODIPY-cholesterol 44-difluoro-4-bora-3a4a-diaza-s-indacene-cholesterolComputational and Structural Biotechnology Journal
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Conversion of the Ca2+-ATPase from Rhodospirillum rubrum into a Mg2+-dependent enzyme by 1,N6-etheno ATP

1980

Nucleoside triphosphate hydrolysis of R.rubrum ATPase complexes can be changed from Ca2+-dependence to Mg2+-dependence by replacing ATP with 1,N6-etheno ATP. Four ATPase complexes which have been prepared by different procedures hydrolyze ATP and 1,N6-etheno ATP at different rates in dependence on the added metal ions. These differences allow an easy distinction of the various enzyme forms.

ATPaseBiophysicsPhotophosphorylationCalcium-Transporting ATPasesRhodospirillum rubrumBiochemistrychemistry.chemical_compoundAdenosine TriphosphateMagnesiumMolecular BiologyEdetic Acidchemistry.chemical_classificationbiologyATP synthaseChemiosmosisCell MembraneRhodospirillum rubrumCell Biologybiology.organism_classificationKineticsEnzymeBiochemistrychemistrybiology.proteinNucleoside triphosphateOligomycinsATP synthase alpha/beta subunitsEthenoadenosine TriphosphateProtein BindingBiochemical and Biophysical Research Communications
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The Arabidopsis heavy metal P-type ATPase HMA5 interacts with metallochaperones and functions in copper detoxification of roots

2005

*† ‡ § Summary Since copper (Cu) is essential in key physiological oxidation reactions, organisms have developed strategies for handling Cu while avoiding its potentially toxic effects. Among the tools that have evolved to cope with Cu is a network of Cu homeostasis factors such as Cu-transporting P-type ATPases that play a key role in transmembrane Cu transport. In this work we present the functional characterization of an Arabidopsis Cutransporting P-type ATPase, denoted heavy metal ATPase 5 (HMA5), and its interaction with Arabidopsis metallochaperones. HMA5 is primarily expressed in roots, and is strongly and specifically induced by Cu in whole plants. We have identified and characteriz…

ATPaseMolecular Sequence DataMutantArabidopsisPlant ScienceGenes PlantPlant RootsMetallochaperonesArabidopsisGeneticsAmino Acid SequenceRNA MessengerDNA PrimersAdenosine TriphosphatasesBase SequenceSequence Homology Amino AcidbiologyArabidopsis ProteinsCell BiologyCompartmentalization (fire protection)biology.organism_classificationTransmembrane proteinCell biologyBiochemistryChaperone (protein)biology.proteinP-type ATPaseCopperMolecular ChaperonesThe Plant Journal
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Acid sensitivity of neomycin-resistant mutants ofOenococcus oeni: a relationship between reduction of ATPase activity and lack of malolactic activity

1999

Mutants of Oenococcus oeni were isolated as spontaneous neomycin-resistant mutants. Three of these mutants harbored a significantly reduced ATPase activity that represented 50% of that of the wild-type strain. Their growth rates were also impaired at pH 5.3 (46-86% of the wild-type level). However, the profiles of sugar consumption appeared identical to those of the parental strain. At pH 3.2, all the mutant strains failed to grow and a drastic decrease in viability was observed after an acid shock. Surprisingly, all the isolated mutants were devoid of malolactic activity. These results suggest that the ATPase and malolactic activities of O. oeni are linked to each other and play a crucial …

ATPaseMutantMalatesMicrobiologyMicrobiologyGeneticsmedicineMalolactic fermentationLactic AcidMolecular BiologyHeat-Shock ProteinsOenococcus oeniAdenosine Triphosphataseschemistry.chemical_classificationbiologyStrain (chemistry)Drug Resistance MicrobialNeomycinNeomycinHydrogen-Ion Concentrationbiology.organism_classificationAnti-Bacterial AgentsGram-Positive CocciEnzymeBiochemistrychemistrybiology.proteinHeat-Shock ResponseLeuconostocBacteriamedicine.drugFEMS Microbiology Letters
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Metabolic shift of polyphosphate-accumulating organisms with different levels of polyphosphate storage

2012

Previous studies have shown that polyphosphate-accumulating organisms (PAOs) are able to behave as glycogen-accumulating organisms (GAOs) under different conditions. In this study we investigated the behavior of a culture enriched with Accumulibacter at different levels of polyphosphate (poly-P) storage. The results of stoichiometric ratios Gly degraded/HAc uptake, PHB synthesized/HAc uptake, PHV synthesized/HAc uptake and P release/HAc uptake confirmed a metabolic shift from PAO metabolism to GAO metabolism: PAOs with high poly-P content used the poly-P to obtain adenosine tri-phosphate (ATP), and glycogen (Gly) to obtain nicotinamide adenine dinucleotide (NADH) and some ATP. In a test whe…

Accumulibacter Type IIWaste component removalUnclassified drugPhysiologyChemical compositionMicrobial metabolismStorageWastewaterNicotinamide adenine dinucleotidePolyhydroxyalkanoic acidchemistry.chemical_compoundBacteriumBioreactorsPolyphosphatesGlycolysisAnaerobiosisBiomassPolyphosphate-accumulating organismsWaste Management and DisposalAccumulibacter Type IGlycogen accumulating organismPriority journalWater Science and TechnologyFluorescence microscopyPolyhydroxyvalerateSewageGlycogenHydrolysisFluorescence in situ hybridizationEcological ModelingPhosphorusHydrogen-Ion ConcentrationBioaccumulationPollutionStoichiometryWaste treatmentPolyphosphate-accumulating organismsBiodegradation EnvironmentalEnhanced biological phosphorus removalBiochemistryGlycogen-accumulating metabolism (GAM)Nicotinamide adenine dinucleotideAccumulibacter type 1Accumulibacter type 2GlycolysisGlycogenMetabolic Networks and PathwaysAccumulibacterAdenosine triphosphateEnvironmental EngineeringBiologyAcetic acidArticleAssociative storagePolyphosphate-accumulating metabolism (PAM)PolyphosphateGlycogen-accumulating organismsGlycogen-accumulating metabolismsTECNOLOGIA DEL MEDIO AMBIENTEPolyphosphate accumulating organismCivil and Structural EngineeringPolyphosphate-accumulating organisms (PAO)BacteriaPolyphosphateMetabolismIn situ measurementGlycogen-accumulating organisms (GAO)Polyphosphate-accumulating metabolismsNonhumanAmidesCarbonMetabolismchemistryPolyphosphate (poly-P)Bacterial metabolismCell cultureVolatilizationWater Research
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Modeling ATP protonation and activity coefficients in NaClaq and KClaq by SIT and Pitzer equations.

2006

Abstract The acid–base properties of Adenosine 5′-triphosphate (ATP) in NaCl and KCl aqueous solutions at different ionic strengths (0  I  / mol L − 1  ≤ 5 for NaCl aq , 0  I  / mol L − 1  ≤ 3 for KCl aq ) and at t  = 25 °C were investigated. A selection of literature data on ATP protonation constants and on activity isopiestic coefficients was performed, together with new potentiometric measurements (by ISE-H + , glass electrode). Both literature and new experimental data were used to model the dependence on ionic strength and ionic medium of ATP protonation by SIT (Specific ion Interaction Theory) and Pitzer equations. In addition to values of first and second ATP protonation constants in…

Activity coefficientMolar concentrationactivity coefficientsActivity coefficientPotentiometric titrationInorganic chemistryBiophysicsIonic bondingProtonationProtonationATP; protonation; activity coefficients; Dependence on medium and ionic strength; SIT model; Pitzer modelSodium ChlorideBiochemistryPotassium ChlorideAdenosine TriphosphateElectrochemistrySettore CHIM/01 - Chimica AnaliticaChemistryOrganic ChemistryOsmolar ConcentrationPitzer modelSIT modelATPSpecific ion interaction theoryIonic strengthDependence on medium and ionic strengthPhysical chemistryPitzer equationsBiophysical chemistry
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Novel mutations of the MET proto-oncogene in papillary renal carcinomas.

1999

Hereditary papillary renal carcinoma (HPRC) is characterized by multiple, bilateral papillary renal carcinomas. Previously, we demonstrated missense mutations in the tyrosine kinase domain of the MET proto-oncogene in HPRC and a subset of sporadic papillary renal carcinomas. In this study, we screened a large panel of sporadic papillary renal carcinomas and various solid tumors for mutations in the MET proto-oncogene. Summarizing these and previous results, mutations of the MET proto-oncogene were detected in 17/129 sporadic papillary renal carcinomas but not in other solid tumors. We detected five novel missense mutations; three of five mutations were located in the ATP-binding region of t…

AdenomaModels MolecularCancer ResearchProtein ConformationDNA Mutational AnalysisMolecular Sequence DataHereditary Papillary Renal Cell CarcinomaBiologymedicine.disease_causeTransfectionProto-Oncogene MasReceptor tyrosine kinaseMiceAdenosine TriphosphateNeoplastic Syndromes HereditaryProto-OncogenesGeneticsCarcinomamedicineMissense mutationAnimalsHumansPoint MutationAmino Acid SequencePhosphorylationCodonMolecular BiologyKidneyMutationBinding SitesSequence Homology Amino AcidPoint mutation3T3 CellsDNA NeoplasmProto-Oncogene Proteins c-metmedicine.diseaseCarcinoma PapillaryKidney NeoplasmsNeoplasm Proteinsmedicine.anatomical_structureCell Transformation NeoplasticCancer researchbiology.proteinMutagenesis Site-DirectedTyrosine kinaseProtein Processing Post-TranslationalSequence AlignmentOncogene
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Customised next-generation sequencing multigene panel to screen a large cohort of individuals with chromatin-related disorder

2020

BackgroundThe regulation of the chromatin state by epigenetic mechanisms plays a central role in gene expression, cell function, and maintenance of cell identity. Hereditary disorders of chromatin regulation are a group of conditions caused by abnormalities of the various components of the epigenetic machinery, namely writers, erasers, readers, and chromatin remodelers. Although neurological dysfunction is almost ubiquitous in these disorders, the constellation of additional features characterizing many of these genes and the emerging clinical overlap among them indicate the existence of a community of syndromes. The introduction of high-throughput next generation sequencing (NGS) methods f…

Adenosine TriphosphataseAdultMaleCCCTC-Binding FactorTranscription FactorDNA-Binding Proteinchromatin disorderComputational biologyBiologyDNA HelicaseDNA sequencingEpigenesis GeneticMendelian chromatin disordersLocus heterogeneityDe Lange SyndromeGeneticsmedicineCoffin-Lowry SyndromeHumansGenetic Predisposition to DiseaseEpigeneticsGenetic TestingChildGeneGenetics (clinical)Adenosine Triphosphatasesnext generation sequencingepigeneticsGenetic heterogeneityDNA HelicasesMendelian chromatin disorderHistone-Lysine N-Methyltransferasemedicine.diseaseChromatinChromatinDNA-Binding ProteinsMendelian chromatin disorders; epigenetics; next generation sequencingCohortMutationRelated disorderFemaleMyeloid-Lymphoid Leukemia ProteinepigeneticTranscription FactorsHuman
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