Search results for "phosphatases"

showing 10 items of 138 documents

Inhibition of B2 receptor internalization delays its dephosphorylation

1997

SucroseReceptor Bradykinin B2Immunoprecipitationmedia_common.quotation_subjectBradykininBradykininCell LineDephosphorylationRadioligand Assaychemistry.chemical_compoundOkadaic AcidConcanavalin APhosphoprotein PhosphatasesHumansEnzyme InhibitorsPhosphorylationInternalizationOxazolesBradykinin Receptor AntagonistsSkinmedia_commonPharmacologyChemistryReceptors BradykininOkadaic acidFibroblastsPrecipitinPrecipitin TestsRadioligand AssayBiochemistryCantharidinIrritantsAutoradiographyPhosphorylationElectrophoresis Polyacrylamide GelMarine ToxinsImmunopharmacology
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Kti12, a PSTK-like tRNA dependent ATPase essential for tRNA modification by Elongator

2019

Abstract Posttranscriptional RNA modifications occur in all domains of life. Modifications of anticodon bases are of particular importance for ribosomal decoding and proteome homeostasis. The Elongator complex modifies uridines in the wobble position and is highly conserved in eukaryotes. Despite recent insights into Elongator's architecture, the structure and function of its regulatory factor Kti12 have remained elusive. Here, we present the crystal structure of Kti12′s nucleotide hydrolase domain trapped in a transition state of ATP hydrolysis. The structure reveals striking similarities to an O-phosphoseryl-tRNA kinase involved in the selenocysteine pathway. Both proteins employ similar …

TRNA modificationSaccharomyces cerevisiae ProteinsProtein ConformationWobble base pairSaccharomyces cerevisiaeBiologyChaetomiumCrystallography X-Ray03 medical and health scienceschemistry.chemical_compound0302 clinical medicineRNA TransferATP hydrolysisGeneticsRNA and RNA-protein complexesAnticodonRNA Processing Post-TranscriptionalUridine030304 developmental biologyAdaptor Proteins Signal TransducingAdenosine Triphosphatases0303 health sciencesSelenocysteineRNATRNA bindingCell biologychemistryTransfer RNASelenocysteine incorporationCarrier ProteinsRibosomes030217 neurology & neurosurgery
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Regulation of stress response in Oenococcus oeni as a function of environmental changes and growth phase

2000

International audience; Oenococcus oeni is a lactic acid bacterium which is able to grow in wine and perform malolactic fermentation. To survive and grow in such a harsh environment as wine, O. oeni uses several mechanisms of resistance including stress protein synthesis. The molecular characterisation of three stress genes hsp18, clpX, trxA encoding for a small heat shock protein, an ATPase regulation component of ClpP protease and a thioredoxin, respectively, allow us to suggest the existence in O. oeni of multiple regulation mechanisms as is the case in Bacillus subtilis. One common feature of these genes is that they are expressed under the control of housekeeping promoters. The express…

Transcription Geneticmedicine.medical_treatment[SDV]Life Sciences [q-bio]bactérie lactiqueBacillus subtilisatpaseMicrobiologygène clppoenococcus oenicaractérisation moléculaire03 medical and health sciencesBacterial ProteinsHeat shock proteinOenococcus;Malolactic fermentation;Stress gene;ATPaseMalolactic fermentationmedicineprotéine de choc thermiquePromoter Regions GeneticGeneHeat-Shock ProteinsOenococcus030304 developmental biologyOenococcus oeniAdenosine Triphosphatases0303 health sciencesProteasebiology030306 microbiologyMalolactic fermentationStress genefood and beveragesGeneral MedicineHydrogen-Ion Concentrationbiology.organism_classificationGram-Positive CocciBiochemistryThioredoxinOenococcusLeuconostocFood Scienceexpression des gènes
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Dual effect of ceramide on human endothelial cells: induction of oxidative stress and transcriptional upregulation of endothelial nitric oxide syntha…

2002

Background— Generation of the second-messenger molecule ceramide by stimulated sphingomyelinase activity has been implicated in the inflammatory processes contributing to the pathogenesis of atherosclerosis. However, reports of stimulatory effects of ceramide on endothelial NO production in animal models suggest antiatherosclerotic effects of the molecule. Therefore, we investigated long-term effects of ceramide on NO generation in human endothelial cells. Methods and Results— In human umbilical vein endothelial cells (HUVECs) and in HUVEC-derived EA.hy 926 endothelial cells, C6-ceramide ( N -hexanoyl- d -erythro-sphingosine) reduced the generation of bioactive NO (RFL-6 reporter-cell assa…

Transcriptional ActivationCeramideNitric Oxide Synthase Type IIIRNA StabilityBiologyCeramidesNitric OxideUmbilical veinCell Linechemistry.chemical_compoundDownregulation and upregulationEnosPhysiology (medical)Phosphoprotein PhosphatasesHumansEnzyme InhibitorsPromoter Regions GeneticCells CulturedDose-Response Relationship DrugLipid signalingbiology.organism_classificationCell biologyUp-RegulationNitric oxide synthaseEndothelial stem cellKineticsOxidative StressSphingomyelin PhosphodiesteraseBiochemistrychemistrybiology.proteinEndothelium VascularSignal transductionNitric Oxide SynthaseCardiology and Cardiovascular MedicineReactive Oxygen SpeciesCirculation
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Induction of rapid and reversible cytokeratin filament network remodeling by inhibition of tyrosine phosphatases

2002

The cytokeratin filament network is intrinsically dynamic, continuously exchanging subunits over its entire surface, while conferring structural stability on epithelial cells. However, it is not known how cytokeratin filaments are remodeled in situations where the network is temporarily and spatially restricted. Using the tyrosine phosphatase inhibitor orthovanadate we observed rapid and reversible restructuring in living cells, which may provide the basis for such dynamics. By examining cells stably expressing fluorescent cytokeratin chimeras, we found that cytokeratin filaments were broken down and then formed into granular aggregates within a few minutes of orthovanadate addition. After …

Tyrosine 3-MonooxygenaseRecombinant Fusion ProteinsGreen Fluorescent ProteinsIntermediate FilamentsFluorescent Antibody Techniquemacromolecular substancesBiologyCytoplasmic GranulesProtein filamentCytokeratinIntermediate Filament ProteinsKeratinTumor Cells CulturedEnzyme InhibitorsPhosphorylationCytoskeletonIntermediate filamentActinchemistry.chemical_classificationCell BiologyPlectinCell biologyLuminescent ProteinsMicroscopy ElectronEukaryotic Cells14-3-3 ProteinschemistryCytoplasmKeratinsPlectinTyrosineProtein Tyrosine PhosphatasesVanadatesJournal of Cell Science
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Oxidative stress, a new hallmark in the pathophysiology of Lafora progressive myoclonus epilepsy

2015

12 páginas, 4 figuras, 1 tabla

Ubiquitin-Protein LigasesFree radicalsBiologymedicine.disease_causeBiochemistryAntioxidantsLafora diseasechemistry.chemical_compoundLaforinPhysiology (medical)medicineHumansLafora diseaseProteostasis DeficienciesGlycogenAutophagyProtein Tyrosine Phosphatases Non-ReceptorMalinmedicine.diseaseOxidative StressProteostasisLafora DiseaseBiochemistrychemistryProteasomeOxidative stressMutationProteostasisUnfolded protein responseCarrier ProteinsLaforinGlycogenOxidative stressFree Radical Biology and Medicine
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Ubiquitin conjugating enzyme E2-N and sequestosome-1 (p62) are components of the ubiquitination process mediated by the malin-laforin E3-ubiquitin li…

2015

11 páginas, 9 figuras.

Ubiquitin-Protein LigasesUbiquitin-conjugating enzymeBiochemistryLafora diseaseSequestosome 1UbiquitinE2-conjugaseLaforinPhagosomesSequestosome-1 ProteinmedicineAutophagyLC3HumanseducationE3-ubiquitin ligaseAdaptor Proteins Signal Transducingchemistry.chemical_classificationDNA ligaseeducation.field_of_studybiologyUbiquitinationAutophagosomesCell Biologymedicine.diseaseProtein Tyrosine Phosphatases Non-ReceptorMalinUbiquitin ligaseCell biologyp62 (SQSTM1)UBE2NHEK293 CellschemistryBiochemistryGene Knockdown TechniquesUbiquitin-Conjugating Enzymesbiology.proteinCarrier ProteinsLaforinUbiquitin-Conjugating Enzyme E2 NProtein Binding
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Light-induced resistance of the keratin network to the filament-disrupting tyrosine phosphatase inhibitor orthovanadate.

2003

Epidermal keratinocytes respond to low-dose light irradiation by inducing signaling cascades that lead to long-term effects on gene transcription thereby protecting cells against damage. In contrast, little is known about immediate light-induced alterations of structural proteins. We have made the intriguing observation that light produces fundamental changes in the properties of the keratin filament system of cultured epidermoid A-431 cells. A short light exposure (1–10 min) causes the keratin cytoskeleton to become immediately resistant to the tyrosine phosphatase inhibitor orthovanadate, which otherwise disrupts the keratin filament network completely in just a few minutes. This protecti…

Ultraviolet Raysultraviolet lightDrug ResistanceIntermediate FilamentsDermatologyProtein tyrosine phosphatasemacromolecular substancesBiologyBiochemistryProtein filamentKeratinUltraviolet lightTumor Cells CulturedHumansVanadatePhosphorylationIntermediate filamentMolecular Biologychemistry.chemical_classificationintermediate filamentKeratin Filamentintegumentary systemVulvar NeoplasmsvanadateCell BiologyMolecular biologyCell biologychemistryEpidermal CellsPhosphorylationKeratinsFemaleProtein Tyrosine PhosphatasesVanadatescytokeratinThe Journal of investigative dermatology
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Evidence for essential primary amino groups in a bacterial coupling factor F1ATPase.

1980

Abstract We have found that the binding of pyridoxal-5′-phosphate to 6 primary amino groups leads to the inactivation of the enzyme. A preferential reaction of pyridoxal-5′-phosphate with the α-subunits of this enzyme can be demonstrated. The reactivity of the amino groups is influenced by various effectors. In the presence of ATP the inhibition of the ATPase activity is noncompetitive.

chemistry.chemical_classificationAdenosine TriphosphatasesPrimary (chemistry)Binding SitesChemistryStereochemistryEffectorCell MembraneBiophysicsCell BiologyBiochemistryMicrococcusCoupling (electronics)Structure-Activity RelationshipEnzymeBiochemistrySolubilityPyridoxal PhosphateAtpase activityReactivity (chemistry)Amino AcidsMolecular BiologyBiochemical and biophysical research communications
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Higher plants possess two different types of ATX1-like copper chaperones.

2007

Abstract Copper (Cu) chaperones constitute a family of small Cu+-binding proteins required for Cu homeostasis in eukaryotes. The ATX1 family of Cu chaperones specifically delivers Cu to heavy metal P-type ATPases. The plant Arabidopsis thaliana expresses the ATX1-like Cu chaperone CCH, which exhibits a plant-specific carboxy-terminal domain (CTD) with unique structural properties. We show that CCH homologues from other higher plants contain CTDs with structural properties similar to Arabidopsis CCH. Furthermore, we identify a new ATX1-like Cu chaperone in Arabidopsis, AtATX1, which functionally complements yeast atx1Δ and sod1Δ associated phenotypes, and localizes to the cytosol of Arabidop…

endocrine systemATPaseTwo-hybrid screeningBiophysicsArabidopsischemistry.chemical_elementBiochemistryArabidopsisMolecular BiologyAdenosine TriphosphatasesbiologyArabidopsis ProteinsCell BiologyHistone-Lysine N-Methyltransferasebiology.organism_classificationPhenotypeCopperYeastProtein Structure TertiaryCytosolBiochemistrychemistryChaperone (protein)biology.proteinCopperGenome PlantMolecular ChaperonesTranscription FactorsBiochemical and biophysical research communications
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