Search results for "Coenzymes"

showing 10 items of 101 documents

Bacteriophage GIL01 gp7 interacts with host LexA repressor to enhance DNA binding and inhibit RecA-mediated auto-cleavage

2015

The SOS response in Eubacteria is a global response to DNA damage and its activation is increasingly associated with the movement of mobile genetic elements. The temperate phage GIL01 is induced into lytic growth using the host's SOS response to genomic stress. LexA, the SOS transcription factor, represses bacteriophage transcription by binding to a set of SOS boxes in the lysogenic promoter P1. However, LexA is unable to efficiently repress GIL01 transcription unless the small phage-encoded protein gp7 is also present. We found that gp7 forms a stable complex with LexA that enhances LexA binding to phage and cellular SOS sites and interferes with RecA-mediated auto-cleavage of LexA, the ke…

Gene Expression Regulation ViralSOS responsebacteriophagesTranscription GeneticvirusesRepressorBacillus PhagesBiologybakteriofagitBacteriophage03 medical and health sciencesSOS Response (Genetics)Viral ProteinsBacterial ProteinsLysogenic cycleGeneticsSOS responsePromoter Regions GeneticSOS Response GeneticsTranscription factor030304 developmental biologyGenetics0303 health sciences030306 microbiologyLexA repressorGene regulation Chromatin and EpigeneticsSerine Endopeptidasesta1182DNAbiochemical phenomena metabolism and nutritionbiology.organism_classification3. Good healthCell biologyRepressor Proteinsenzymes and coenzymes (carbohydrates)Rec A RecombinasesLytic cyclebacteriaRepressor lexAProtein BindingNucleic Acids Research
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Interaction mechanism of endogenous PP2A inhibitor protein ENSA with PP2A

2022

The vast diversity of protein phosphatase 2A (PP2A) holoenzyme composition ensures its multifaceted role in the regulation of cellular growth and signal transduction. In several pathological conditions, such as cancer, PP2A is inhibited by endogenous inhibitor proteins. Several PP2A inhibitor proteins have been identified, one of which is α-endosulfine (ENSA). ENSA inhibits PP2A activity when it is phosphorylated at Ser67 by Greatwall (Gwl) kinase. The role of ENSA in PP2A inhibition is rather well characterized, but knowledge of the mechanism of inhibition is scarce. In this study, we have performed comprehensive structural characterization of ENSA, and its interaction with PP2A A- and var…

Gene isoformMitosisEndogenymacromolecular substancesProtein Serine-Threonine KinasesPP2A inhibitor protein010402 general chemistry01 natural sciencesBiochemistryenvironment and public health03 medical and health sciencesX-Ray DiffractionNeoplasmsScattering Small AngleHumansProtein Phosphatase 2DPsPhosphorylationNMR-spektroskopiaMolecular BiologyNuclear Magnetic Resonance Biomolecular030304 developmental biologyinhibiittoritsoluviestintä0303 health sciencesChemistryKinaseCell growthCell CycleCell BiologyProtein phosphatase 2Inhibitor proteinSAXSPhosphoproteinsNMR3. Good health0104 chemical sciencesCell biologyPP2Aenzymes and coenzymes (carbohydrates)ENSAPhosphorylationIntercellular Signaling Peptides and ProteinsproteiinitSignal transductionMicrotubule-Associated ProteinsProtein Processing Post-TranslationalSignal TransductionFEBS Journal
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Docosahexaenoic acid inhibits cancer cell growth via p27Kip1, CDK2, ERK1/ERK2, and retinoblastoma phosphorylation

2006

Docosahexaenoic acid (DHA), a PUFA of the n-3 family, inhibited the growth of FM3A mouse mammary cancer cells by arresting their progression from the late-G(1) to the S phase of the cell cycle. DHA upregulated p27(Kip1) levels by inhibiting phosphorylation of mitogen-activated protein (MAP) kinases, i.e., ERK1/ERK2. Indeed, inhibition of ERK1/ERK2 phosphorylation by DHA, U0126 [chemical MAPK extracellularly signal-regulated kinase kinase (MEK) inhibitor], and MEK(SA) (cells expressing dominant negative constructs of MEK) resulted in the accumulation of p27(Kip1). MAP kinase (MAPK) inhibition by DHA did not increase p27(Kip1) mRNA levels. Rather, this fatty acid stabilized p27(Kip1) contents…

MAPK/ERK pathwayDocosahexaenoic AcidsMammary Neoplasms AnimalQD415-436fatty acidsenvironment and public healthBiochemistryMiceEndocrinologyCyclin-dependent kinaseCyclin EAnimalsRNA MessengerPhosphorylationCells CulturedCell ProliferationMAPK14biologyKinaseCyclin-dependent kinase 4Cyclin-Dependent Kinase 2Cyclin-dependent kinase 2Retinoblastomafood and beveragesCell BiologyUp-RegulationCell biologyenzymes and coenzymes (carbohydrates)cyclin-dependent kinaseCyclin-dependent kinase complexbiology.proteinPhosphorylationcell cyclelipids (amino acids peptides and proteins)Mitogen-Activated Protein KinasesCyclin-Dependent Kinase Inhibitor p27Journal of Lipid Research
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p42 MAPK phosphorylates 80 kDa MARCKS at Ser-113.

1996

Abstract It is demonstrated here that p42 MAPKinase (p42 MAPK) phosphorylates the M yristoylated A lanine- R ich C - K inase S ubstrate (MARCKS) at Ser-113. In permeabilised Swiss 3T3 cells activation of protein kinase C (PKC) leads to p42 MAPK activation, but only the protein kinase C sites in MARCKS become phosphorylated and not Ser-113. The mitogen platelet-derived growth factor (PDGF) elicits the same response. These results demonstrate that while Ser-113 is a substrate for p42 MAPK in vitro and can be phosphorylated in vivo as shown by Taniguchi et al. [(1994) J. Biol. Chem. 269, 18299–18302], its phosphorylation is not subject to acute regulation by p42 MAPK in Swiss 3T3 cells.

MAPK/ERK pathwayMARCKSmedicine.medical_treatmentMitogen-activated protein kinase kinaseBiochemistryenvironment and public healthSubstrate SpecificityMiceStructural BiologySerinep42MAPKinasePhosphorylationMyristoylated Alanine-Rich C Kinase SubstrateCells CulturedProtein Kinase CMitogen-Activated Protein Kinase 1Platelet-Derived Growth FactorbiologyChemistryIntracellular Signaling Peptides and Proteins3T3 CellsProtein-Tyrosine KinasesCell biologyBiochemistryMitogen-activated protein kinasePhosphorylationTetradecanoylphorbol Acetatebiological phenomena cell phenomena and immunityPlatelet-derived growth factor receptorhormones hormone substitutes and hormone antagonistsendocrine systemRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsGeneticsmedicineAnimalsAmino Acid SequenceMARCKSMolecular BiologyProtein kinase CGrowth factorMembrane ProteinsProteinsCell BiologyPeptide FragmentsEnzyme ActivationMolecular Weightenzymes and coenzymes (carbohydrates)Calcium-Calmodulin-Dependent Protein Kinasesbiology.proteinMutagenesis Site-DirectedMitogensFEBS letters
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Thapsigargin-stimulated MAP kinase phosphorylation via CRAC channels and PLD activation: inhibitory action of docosahexaenoic acid.

2004

AbstractThis study was conducted on human Jurkat T-cells to investigate the role of depletion of intracellular Ca2+ stores in the phosphorylation of two mitogen-activated protein kinases (MAPKs), i.e. extracellular signal-regulated kinase (ERK) 1 and ERK2, and their modulation by a polyunsaturated fatty acid, docosahexaenoic acid (DHA). We observed that thapsigargin (TG) stimulated MAPK activation by store-operated calcium (SOC) influx via opening of calcium release-activated calcium (CRAC) channels as tyrphostin-A9, a CRAC channel blocker, and two SOC influx inhibitors, econazole and SKF-96365, diminished the action of the former. TG-stimulated ERK1/ERK2 phosphorylation was also diminished…

MAPK/ERK pathwayThapsigarginDocosahexaenoic AcidsBiophysicschemistry.chemical_elementCalciumBiochemistryDiglycerideschemistry.chemical_compoundJurkat CellsStructural BiologyGeneticsPhospholipase DHumansPhosphorylationMolecular BiologyProtein kinase CProtein Kinase CDiacylglycerol kinaseMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Phospholipase CChemistryKinasePhospholipase DRyanodine Receptor Calcium Release ChannelCell BiologyJurkat T-cellCell biologyEnzyme Activationenzymes and coenzymes (carbohydrates)Docosahexaenoic acidFatty Acids UnsaturatedThapsigarginlipids (amino acids peptides and proteins)CalciumMitogen-Activated Protein KinasesFEBS letters
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Use of CDC2 from etoposide-treated cells as substrate to assay CDC25 phosphatase activity

1999

International audience; Cyclin-dependent kinases (CDKs) regulate the key transition of the cell cycle in all organisms. In response to Etoposide (VP-16) induced DNA damage, cells undergo a G2-phase arrest resulting in the accumulation of inactive CDK1 (CDC2) kinase complexes. Here we report that upon Etoposide treatment CDC2 is phosphorylated on tyrosine 15 and is dephosphorylated and activated in vitro by recombinant CDC25 phosphatase. We also show that inactive CDC2 kinase from Etoposide-treated cells can be used as a substrate in a sensitive two-step assay of CDC25 phosphatase. This assay, which is very simple to set-up, is based on the monitoring of CDC2 kinase activity after CDC25-depe…

MESH: HumansMESH: Phosphorylation[SDV]Life Sciences [q-bio]Cell Cycle Proteins[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]MESH: CDC2 Protein KinaseMESH: Tyrosine[SDV] Life Sciences [q-bio]AGENT ANTITUMORALenzymes and coenzymes (carbohydrates)MESH: Cell Cycle ProteinsMESH: cdc25 PhosphatasesCDC2 Protein KinaseMESH: HeLa CellsMESH: Phosphoprotein PhosphatasesPhosphoprotein PhosphatasesHumansTyrosinecdc25 PhosphatasesPhosphorylationbiological phenomena cell phenomena and immunityEtoposideHeLa CellsMESH: Etoposide
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The nutrigenetic influence of the interaction between dietary vitamin E and TXN and COMT gene polymorphisms on waist circumference: a case control st…

2015

Background Abdominal obesity (AO) is a common modifiable risk factor for certain non-communicable diseases associated with enhanced oxidative stress (OS). The objective of this work was to investigate whether the interaction between antioxidant vitamin intake and OS-related polymorphisms modulates gene-associated anthropometry in a Spanish population. Methods A total of 246 subjects with AO, and 492 age and gender matched non-AO subjects were included in the study. Anthropometric, biochemical, and OS parameters, and antioxidant dietary intake data were assessed using validated procedures. DNA from white blood cells was isolated and the genotype of seven polymorphisms from genes involved in …

MaleAntioxidantPolimorphismmedicine.medical_treatment:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::Thioredoxins [Medical Subject Headings]Antioxidantes:Analytical Diagnostic and Therapeutic Techniques and Equipment::Investigative Techniques::Epidemiologic Methods::Statistics as Topic::Probability::Risk::Risk Factors [Medical Subject Headings]AntioxidantsVitamin E intakeObesidad abdominalchemistry.chemical_compoundNutrigenomicsThioredoxinsPolymorphism (computer science):Anatomy::Cells::Blood Cells::Leukocytes [Medical Subject Headings]Risk FactorsGenotypeVitamin E:Chemicals and Drugs::Nucleic Acids Nucleotides and Nucleosides::Nucleosides::Deoxyribonucleosides::Deoxyguanosine [Medical Subject Headings]:Chemicals and Drugs::Chemical Actions and Uses::Pharmacologic Actions::Physiological Effects of Drugs::Growth Substances::Micronutrients::Vitamins [Medical Subject Headings]:Phenomena and Processes::Metabolic Phenomena::Metabolism::Oxidative Stress [Medical Subject Headings]Abdominal obesityNutrigenómicaMedicine(all)AnthropometryAge FactorsGeneral MedicineAbdominal obesity:Phenomena and Processes::Physiological Phenomena::Body Constitution::Body Weights and Measures::Body Size::Body Weight::Overweight::Obesity::Obesity Abdominal [Medical Subject Headings]Middle Aged:Analytical Diagnostic and Therapeutic Techniques and Equipment::Investigative Techniques::Epidemiologic Methods::Statistics as Topic::Models Statistical::Logistic Models [Medical Subject Headings]Waist circumferenceDietaFemale:Phenomena and Processes::Genetic Phenomena::Genotype [Medical Subject Headings]medicine.symptomFactores de riesgoVitaminAdultmedicine.medical_specialtyGenotypeVitamina ECatechol-O-methyltransferaseBiology:Phenomena and Processes::Physiological Phenomena::Nutritional Physiological Phenomena::Diet [Medical Subject Headings]:Phenomena and Processes::Genetic Phenomena::Genetic Structures::Genome::Genome Components::Genes::Genes Reporter [Medical Subject Headings]Catechol O-Methyltransferase:Chemicals and Drugs::Biological Factors::Pigments Biological::Carotenoids::Retinoids::Vitamin A [Medical Subject Headings]Polymorphism Single NucleotideGeneral Biochemistry Genetics and Molecular BiologySex FactorsInternal medicine:Chemicals and Drugs::Inorganic Chemicals::Oxygen Compounds::Reactive Oxygen Species [Medical Subject Headings]:Chemicals and Drugs::Chemical Actions and Uses::Pharmacologic Actions::Physiological Effects of Drugs::Protective Agents::Antioxidants [Medical Subject Headings]medicinePerímetro abdominal:Phenomena and Processes::Physiological Phenomena::Body Constitution::Body Weights and Measures::Body Size::Waist Circumference [Medical Subject Headings]:Chemicals and Drugs::Heterocyclic Compounds::Heterocyclic Compounds 2-Ring::Benzopyrans::Vitamin E [Medical Subject Headings]HumansObesityPolymorphismThioredoxinAgedCatechol-O-methyl transferaseBiochemistry Genetics and Molecular Biology(all)Vitamin EResearchCase-control studyGenes informadores:Disciplines and Occupations::Natural Science Disciplines::Biological Science Disciplines::Biology::Genetics::Genomics::Nutrigenomics [Medical Subject Headings]DietOxidative StressEndocrinologychemistrySpainOxidative stressCase-Control Studies:Chemicals and Drugs::Enzymes and Coenzymes::Enzymes::Transferases::One-Carbon Group Transferases::Methyltransferases::Catechol O-Methyltransferase [Medical Subject Headings]:Chemicals and Drugs::Nucleic Acids Nucleotides and Nucleosides::Nucleic Acids::DNA [Medical Subject Headings]Genotipo
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Oxidation of tienilic acid by human yeast-expressed cytochromes P-450 2C8, 2C9, 2C18 and 2C19. Evidence that this drug is a mechanism-based inhibitor…

1996

Oxidation of tienilic acid by human cytochromes P-450 (CYP) 2C9, 2C18, 2C8 and 2C19 was studied using recombinant enzymes expressed in yeast. CYP 2C9 was the best catalyst for 5-hydroxylation of tienilic acid (K(m) = 5 +/- 1 microM, kcat = 1.7 +/- 0.2 min-1), 30-fold more potent in terms of kcat/K(m) than CYP 2C18 (K(m) = 150 +/- 15 microM, kcat = 1.8 +/- 0.2 min-1) and 300-fold more potent than CYP 2C8 (K(m) = 145 +/- 15 microM, kcat = 0.2 +/- 0.1 min-1). CYP 2C19 was unable to catalyze this hydroxylation under our experimental conditions. During this study, a marked effect of the ionic strength on the activities (hydroxylations of tienilic acid and tolbutamide) of these cytochromes P-450 …

MaleCytochromeTolbutamideTicrynafenSaccharomyces cerevisiaeurologic and male genital diseasesHydroxylationBiochemistryMixed Function OxygenasesHydroxylationchemistry.chemical_compoundCytochrome P-450 Enzyme SystemMicrosomesmedicineCytochrome P-450 Enzyme InhibitorsHumansheterocyclic compoundsEnzyme InhibitorsCytochrome P-450 Enzyme Inhibitorschemistry.chemical_classificationbiologyChemistryorganic chemicalsMembrane ProteinsGlutathionerespiratory systemRecombinant ProteinsIsoenzymesenzymes and coenzymes (carbohydrates)EnzymeBiochemistrySteroid 16-alpha-HydroxylaseTienilic acidSuicide inhibitionbiology.proteinMicrosomeMicrosomes LiverAryl Hydrocarbon HydroxylasesOxidation-Reductionmedicine.drugEuropean journal of biochemistry
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BRAF-V600E expression in precursor versus differentiated dendritic cells defines clinically distinct LCH risk groups.

2014

BRAF-V600E expression is identified in hematopoietic progenitor and precursor myeloid dendritic cells in patients with high-risk LCH, and enforced expression of BRAF-V600E in CD11c+ cells recapitulates a high-risk LCH-like phenotype in mice.

MalePathologyendocrine system diseasesCellular differentiationCD34Antigens CD34Mice0302 clinical medicineLangerhans cell histiocytosisBone MarrowRisk FactorsImmunology and Allergyskin and connective tissue diseasesChild0303 health sciencesCell Differentiation3. Good healthHistiocytosismedicine.anatomical_structurePhenotypeTreatment Outcome030220 oncology & carcinogenesisChild PreschoolAntigens Surface2723 Immunology and AllergyFemaleProto-Oncogene Proteins B-rafmedicine.medical_specialtyImmunologyCD11c610 Medicine & healthBiologyArticle03 medical and health sciencesGermline mutationmedicineAnimalsHumansCell LineageGenetic Predisposition to DiseaseLectins C-TypeProgenitor cellneoplasms030304 developmental biology2403 ImmunologyHistocompatibility Antigens Class II302InfantCorrectionDendritic Cellsmedicine.diseaseHematopoietic Stem Cellsdigestive system diseasesCD11c Antigenenzymes and coenzymes (carbohydrates)Histiocytosis Langerhans-CellMannose-Binding Lectins10032 Clinic for Oncology and HematologyMutationBone marrowThe Journal of experimental medicine
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The clinical significance of CDK1 expression in oral squamous cell carcinoma

2014

Objectives: To evaluate the clinical significance of cyclin-dependent kinase 1 (CDK 1 ) in 77 oral squamous cell carcinomas (OSCC) using immunohistochemical methods. Study Design: Immunohistochemical expression of CDK 1 was compared with various clinicopathological features in 77 OSCC and 60 controlled epithelia adjacent to the tumours. In addition, correlation of CDK 1 expression and prognostic and the 5-year accumulative survival rate of OSCC were investigated. Results: The CDK 1 protein was expressed in 52 cases of 77 tumor tissues (67.5%), compared with 21 cases of 60 controlled (35.0%). The expression of CDK 1 was significantly correlated with the histological grade of OSCC ( P <0.05).…

MalePathologymedicine.medical_specialtyCellOdontologíaenvironment and public healthCDC2 Protein KinaseHumansMedicineClinical significanceGeneral DentistrySurvival rateMouth neoplasmCyclin-dependent kinase 1Oral Medicine and Pathologybusiness.industryKinaseCell growthResearchMiddle Aged:CIENCIAS MÉDICAS [UNESCO]Ciencias de la saludImmunohistochemistrySurvival Rateenzymes and coenzymes (carbohydrates)stomatognathic diseasesmedicine.anatomical_structureOtorhinolaryngologyUNESCO::CIENCIAS MÉDICASCarcinoma Squamous CellCancer researchImmunohistochemistryFemaleMouth NeoplasmsSurgerybiological phenomena cell phenomena and immunitybusinessMedicina Oral Patología Oral y Cirugia Bucal
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