Search results for "isoenzymes"

showing 10 items of 244 documents

A new pyrazolo pyrimidine derivative inhibitor of cyclooxygenase-2 with anti-angiogenic activity

2003

In a previous study, we reported a new pyrazolo pyrimidine derivative, N(4)-benzyl-N(6),N(6)-dimethyl-1-1(tert-butyl)-1H-pyrazolo[3,4-d]pyrimidine-6,4-diamine (DPP), which inhibited potently cyclooxygenase-2 activity in intact cell assays with minor activity against cyclooxygenase-1 (IC(50)=0.9 nM for cyclooxygenase-2 versus IC(50)=59.6 nM for cyclooxygenase-1). In the present work, this behaviour was confirmed in vivo by using the 24-h zymosan-injected mouse air pouch model (ID(50)=1.36 nM/pouch for prostaglandin E(2) level). We also studied the possible beneficial effect of DPP in the angiogenesis-dependent murine air pouch granuloma and rat paw carrageenan-induced hyperalgesia models. DP…

Pyrimidinemedicine.medical_treatmentAngiogenesis InhibitorsPharmacologyCarrageenanDinoprostoneMicechemistry.chemical_compoundIn vivomedicineAnimalsEdemaCyclooxygenase InhibitorsRats WistarProstaglandin E2IC50NitrobenzenesPharmacologySulfonamidesGranulomaCyclooxygenase 2 InhibitorsNeovascularization PathologicbiologyTumor Necrosis Factor-alphaZymosanRatsIsoenzymesPyrimidinesEicosanoidchemistryBiochemistryCyclooxygenase 2Prostaglandin-Endoperoxide SynthasesHyperalgesiabiology.proteinPyrazolesFemaleCyclooxygenasemedicine.symptomInterleukin-1Prostaglandin Emedicine.drugEuropean Journal of Pharmacology
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Pseudouridine: Still mysterious, but never a fake (uridine)!

2014

International audience; Pseudouridine () is the most abundant of >150 nucleoside modifications in RNA. Although was discovered as the first modified nucleoside more than half a century ago, neither the enzymatic mechanism of its formation, nor the function of this modification are fully elucidated. We present the consistent picture of synthases, their substrates and their substrate positions in model organisms of all domains of life as it has emerged to date and point out the challenges that remain concerning higher eukaryotes and the elucidation of the enzymatic mechanism.

RNA MitochondrialSaccharomyces cerevisiaeReviewBiologyModified nucleosidesPseudouridine03 medical and health scienceschemistry.chemical_compound0302 clinical medicineRNA modificationEscherichia coliHumansRNA Processing Post-Transcriptional[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Intramolecular TransferasesUridineMolecular Biology030304 developmental biology0303 health sciencesRNACell BiologyRNA Transfer Amino Acid-SpecificRibonucleoproteins Small NuclearUridineIsoenzymeschemistryBiochemistryRNA Ribosomal030220 oncology & carcinogenesisTransfer RNANucleic Acid ConformationRNARibosomesNucleosidePseudouridineSmall nuclear RNA[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologyRNA Guide Kinetoplastida
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Role of nitric oxide synthase isoforms for ophthalmic artery reactivity in mice.

2014

Abstract Nitric oxide synthases (NOS) are involved in regulation of ocular vascular tone and blood flow. While endothelial NOS (eNOS) has recently been shown to mediate endothelium-dependent vasodilation in mouse retinal arterioles, the contribution of individual NOS isoforms to vascular responses is unknown in the retrobulbar vasculature. Moreover, it is unknown whether the lack of a single NOS isoform affects neuron survival in the retina. Thus, the goal of the present study was to examine the hypothesis that the lack of individual nitric oxide synthase (NOS) isoforms affects the reactivity of mouse ophthalmic arteries and neuron density in the retinal ganglion cell (RGC) layer. Mice defi…

Retinal Ganglion CellsVasodilator AgentsNitric Oxide Synthase Type IIVideo microscopyVasodilationCell CountNitric Oxide Synthase Type IMuscle Smooth Vascularchemistry.chemical_compoundMiceOphthalmic ArteryPhenylephrineEnosEnzyme InhibitorsMice KnockoutbiologyAnatomySensory SystemsNitric oxide synthaseIsoenzymesVasodilationmedicine.anatomical_structureNG-Nitroarginine Methyl EsterRetinal ganglion cellKnockout mouseRetinal NeuronsNitroprussidemedicine.medical_specialtyNitric Oxide Synthase Type IIIEndothelial NOSNitric oxideCellular and Molecular NeuroscienceTonometry OcularInternal medicinemedicineAnimalsNitric Oxide DonorsIntraocular Pressurebusiness.industrybiology.organism_classificationAcetylcholineMice Inbred C57BLOphthalmologyEndocrinologychemistryVasoconstrictionbiology.proteinAdrenergic alpha-1 Receptor AgonistsEndothelium VascularbusinessExperimental eye research
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Relationships of gag-pol diversity between Ty3/Gypsy and Retroviridae LTR retroelements and the three kings hypothesis

2008

Abstract Background The origin of vertebrate retroviruses (Retroviridae) is yet to be thoroughly investigated, but due to their similarity and identical gag-pol (and env) genome structure, it is accepted that they evolve from Ty3/Gypsy LTR retroelements the retrotransposons and retroviruses of plants, fungi and animals. These 2 groups of LTR retroelements code for 3 proteins rarely studied due to the high variability – gag polyprotein, protease and GPY/F module. In relation to 3 previously proposed Retroviridae classes I, II and II, investigation of the above proteins conclusively uncovers important insights regarding the ancient history of Ty3/Gypsy and Retroviridae LTR retroelements. Resu…

RetroelementsEvolutionSequence analysisvirusesMolecular Sequence DataRetroviridae ProteinsTy3/Gypsy; Retroviridae; LTR retroelements; Gag-polGene Products gagGene Products polSequence alignmentRetrotransposonEvolution MolecularMonophylySequence Analysis ProteinPhylogeneticsbiology.animalQH359-425Amino Acid SequenceRetroviridae ProteinsPhylogenyEcology Evolution Behavior and SystematicsGenetics:CIENCIAS DE LA VIDA::Genética ::Otras [UNESCO]Polymorphism GeneticPhylogenetic treebiologyTerminal Repeat SequencesVertebratefood and beveragesUNESCO::CIENCIAS DE LA VIDA::Genética ::OtrasIsoenzymesGag-polPhenotypeTy3/GypsyRetroviridaeLTR retroelementsSequence AlignmentResearch Article
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Yeast contains multiple forms of histone acetyltransferase.

1989

We have assayed several methods to quantitatively recover yeast histone acetyltransferases in an attempt to study the multiplicity of enzymatic activities. Two methods, namely (NH4)2SO4 precipitation and salt dissociation of chromatin in 0.5 M NaCl, yielded convenient preparations of total histone acetyltransferases. DEAE-Sepharose chromatography of the crude extracts resulted in the separation of three peaks of activity when total yeast histones were used as substrate. However, the scanning of the enzymatic activity toward individual histones along the chromatography, achieved by determining the specific activity of the individual histones after incubating whole histones and [14C]acetyl-Co…

Saccharomyces cerevisiae ProteinsIon chromatographySaccharomyces cerevisiaeBiochemistryHistone DeacetylasesSubstrate SpecificityHistonesAcetyltransferasesEnzyme StabilityHistone octamerMolecular BiologyHistone AcetyltransferasesHistone AcetyltransferasesChromatographybiologyChemistryAcetylationCell BiologyHistone acetyltransferaseChromatography Ion ExchangeYeastChromatinChromatinIsoenzymesKineticsHistoneBiochemistryAcetylationbiology.proteinThe Journal of biological chemistry
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Site specificity of pea histone acetyltransferase B in vitro.

1993

Histone acetyltransferase B from pea embryonic axes has been purified approximately 300-fold by a combination of chromatographic procedures, including affinity chromatography on histone-agarose. The enzyme preparation has been used for the in vitro transfer of acetyl groups from [1-14C]acetyl-CoA to non-acetylated pea histone H4. Up to three acetyl groups can be introduced into the histone. The resulting mono-, di-, and triacetylated H4 isoforms were separated and sequenced to determine the acetylated sites. Only sites 5, 12, and 16 were used by histone acetyltransferase B, but no clear preference among them was observed. The absence of modification of other potentially acetylatable sites i…

Saccharomyces cerevisiae ProteinsLysineMolecular Sequence DataBiochemistryChromatography AffinitySubstrate SpecificityHistone H4HistonesAffinity chromatographyAcetyltransferasesHistone octamerAmino Acid SequenceMolecular BiologyHistone AcetyltransferasesPlants MedicinalbiologyAcetylationFabaceaeCell BiologyHistone acetyltransferaseMolecular biologyIsoenzymesHistoneBiochemistryAcetylationHistone methyltransferasebiology.proteinElectrophoresis Polyacrylamide GelThe Journal of biological chemistry
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The formation of hybrid complexes between isoenzymes of glyceraldehyde‐3‐phosphate dehydrogenase regulates its aggregation state, the glycolytic acti…

2019

The glycolytic enzyme glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH) has been traditionally considered a housekeeping protein involved in energy generation. However, evidence indicates that GAPDHs from different origins are tightly regulated and that this regulation may be on the basis of glycolysis‐related and glycolysis‐unrelated functions. In Saccharomyces cerevisiae, Tdh3 is the main GAPDH, although two other isoenzymes encoded by TDH1 and TDH2 have been identified. Like other GAPDHs, Tdh3 exists predominantly as a tetramer, although dimeric and monomeric forms have also been isolated. Mechanisms of Tdh3 regulation may thus imply changes in its oligomeric state or be based in its abil…

Saccharomyces cerevisiae Proteinslcsh:BiotechnologySaccharomyces cerevisiaeMicrobiologiaBioengineeringDehydrogenaseSaccharomyces cerevisiaeProtein aggregationApplied Microbiology and BiotechnologyBiochemistryIsozyme03 medical and health scienceslcsh:TP248.13-248.65Tdh2Tdh1Tdh3Ceramide synthaseResearch ArticlesGlyceraldehyde 3-phosphate dehydrogenase030304 developmental biologySphingolipids0303 health sciencesbiology030306 microbiologyChemistryGlyceraldehyde-3-Phosphate Dehydrogenasesbiology.organism_classificationLipidsSphingolipidYeastIsoenzymesMetabolismBiochemistrybiology.proteinGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)Protein aggregationEnzimsGlycolysisFlux (metabolism)Research ArticleBiotechnologyMicrobial Biotechnology
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Novel Glutamate–Putrescine Ligase Activity in Haloferax mediterranei: A New Function for glnA-2 Gene

2021

This article belongs to the Section Cellular Biochemistry.

Salmonella typhimuriumTranscription GeneticNitrogen assimilationHaloferax mediterraneiGene ExpressionBiochemistryGlutamate-putrescine ligase activitySubstrate SpecificityLigasesAdenosine TriphosphateputrescineCloning MolecularPhylogenyhaloarchaeachemistry.chemical_classification0303 health sciencesbiologyChemistryHaloarchaeaEscherichia coli Proteinsglutamine synthetaseBioquímica y Biología MolecularQR1-502Recombinant ProteinsNitrogen assimilationHaloferax mediterraneiIsoenzymesBiochemistryArchaeal ProteinsGenetic VectorsGlutamic AcidGlutamate–putrescine ligaseMicrobiologyArticleglutamate–putrescine ligaseGlutamine synthetase03 medical and health sciencesAmmoniaGlutamine synthetaseNitrogen FixationEscherichia coliPutrescineAmino Acid SequenceMolecular Biology030304 developmental biologyDNA ligaseSequence Homology Amino Acid030306 microbiologyComputational Biologynitrogen assimilationbiology.organism_classificationMetabolic pathwayEnzymeProtein BiosynthesisHaloarchaeaGene Expression Regulation ArchaealSequence AlignmentBiomolecules
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Raloxifene increases the capacity of serum to promote prostacyclin release in human endothelial cells: implication of COX-1 and COX-2.

2004

OBJECTIVE Prostacyclin is a potent vasodilator synthesized by two isoforms of cyclooxygenase in endothelium. The aim of this study was to investigate the effect of serum from postmenopausal women treated with raloxifene on prostacyclin production by human umbilical vein endothelial cells and on cyclooxygenases-1 and -2. DESIGN Serum was collected from 21 women receiving 60 mg/day of raloxifene, at baseline and at 3 and 6 months. Human umbilical vein endothelial cells were exposed to serum for 24 hours, and prostacyclin production was evaluated in supernatants. Selective inhibitors of cyclooxygenases-1 and -2 (SC-560 and NS-398) were used to investigate the relative contribution of each enzy…

Selective Estrogen Receptor Modulatorsmedicine.medical_specialtyUmbilical VeinsEndotheliumCell SurvivalProstacyclinVasodilationUmbilical veinWestern blotInternal medicinemedicineHumansRaloxifeneCyclooxygenase InhibitorsCells CulturedNitrobenzeneschemistry.chemical_classificationSulfonamidesbiologymedicine.diagnostic_testCyclooxygenase 2 Inhibitorsbusiness.industryObstetrics and GynecologyEndothelial CellsMembrane ProteinsMiddle AgedEpoprostenolImmunohistochemistryIsoenzymesPostmenopausemedicine.anatomical_structureEnzymeEndocrinologychemistryCyclooxygenase 2Prostaglandin-Endoperoxide SynthasesRaloxifene Hydrochloridecardiovascular systembiology.proteinCyclooxygenase 1PyrazolesFemaleCyclooxygenasebusinessmedicine.drugMenopause (New York, N.Y.)
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Ribonuclease H levels in herpes simplex virus-infected cells.

1980

Two forms of ribonuclease H (RNase H) have been identified both in uninfected and Herpes Simplex virus (HSV-)infected BHK cells. Identical RNase H species were detected in control- as well as in infected cells. RNase H I and II have not been found to be associated both with host cell DNA polymerase alpha and beta and HSV-induced DNA polymerase. Infection of BHK cells with HSV type 1 does not lead to a pronounced alteration of RNase H II activity but to an increase (3-fold) of the extractable RNase H I activity. RNase H I activity increases to a maximum between 8-10 hours p.i.; the bulk of HSV-DNA synthesis occurs between 6-8 hours p.i. From these experiments we draw the preliminary conclusi…

Simplexvirusfood.ingredientDNA polymerasevirusesPolynucleotidesmedicine.disease_causeKidneyIsozymeCell LineSubstrate SpecificityfoodRibonucleasesVirologyCricetinaeBaby hamster kidney cellmedicineAnimalsSimplexvirusRNase HbiologyGeneral MedicineVirologyMolecular biologyIsoenzymesMolecular WeightHerpes simplex virusCell culturePolynucleotideEthylmaleimideDNA Viralbiology.proteinArchives of virology
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