Search results for "binding proteins"

showing 10 items of 911 documents

Common variants conferring risk of schizophrenia

2009

Schizophrenia is a complex disorder, caused by both genetic and environmental factors and their interactions. Research on pathogenesis has traditionally focused on neurotransmitter systems in the brain, particularly those involving dopamine. Schizophrenia has been considered a separate disease for over a century, but in the absence of clear biological markers, diagnosis has historically been based on signs and symptoms. A fundamental message emerging from genome-wide association studies of copy number variations (CNVs) associated with the disease is that its genetic basis does not necessarily conform to classical nosological disease boundaries. Certain CNVs confer not only high relative ris…

Pair 6/geneticsGenetics and epigenetic pathways of disease [NCMLS 6]Genome-wide association studyAetiology screening and detection [ONCOL 5]1Q21.1Major Histocompatibility Complex/geneticsMajor Histocompatibility ComplexTranscription Factor 40302 clinical medicineChemicals And Cas Registry NumbersPerception and Action [DCN 1]Copy-number variationPOPULATIONGeneticsPair 18/genetics0303 health scienceseducation.field_of_studyGenomeHuman/geneticsMultidisciplinaryBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsSchizophrenia/*genetics/immunologyGenetic Predisposition to Disease/*genetics3. Good healthDNA-Binding ProteinsNeurogranin/geneticsDISEASESChromosomes Human Pair 6Single Nucleotide/*geneticsFunctional Neurogenomics [DCN 2]Zinc finger protein 804AHumanGenetic MarkersPsychosisGenotypePopulationTranscription Factors/geneticsSingle-nucleotide polymorphismBiologyPolymorphism Single NucleotideChromosomesPair 11/geneticsArticleChromosomes; Human; Pair 11/genetics; Pair 18/genetics; Pair 6/genetics; DNA-Binding Proteins/genetics; Genetic Markers/genetics; Genetic Predisposition to Disease/*genetics; Genome; Human/genetics; Genome-Wide Association Study; Genotype; Humans; Major Histocompatibility Complex/genetics; Neurogranin/genetics; Polymorphism; Single Nucleotide/*genetics; Schizophrenia/*genetics/immunology; Transcription Factors/geneticsGenomic disorders and inherited multi-system disorders [IGMD 3]Molecular epidemiology [NCEBP 1]03 medical and health sciencesTranslational research [ONCOL 3]medicineHumansSNPGenetic Predisposition to DiseasePolymorphismGENOME-WIDE ASSOCIATIONeducation030304 developmental biologyGenetic associationGenetic Markers/geneticsHereditary cancer and cancer-related syndromes [ONCOL 1]Genome HumanChromosomes Human Pair 11MEMORYmedicine.diseaseGENENEUROGRANINDELETIONSSchizophreniabiology.proteinNeurograninChromosomes Human Pair 18DNA-Binding Proteins/geneticsMENTAL-RETARDATIONSCAN030217 neurology & neurosurgeryGenome-Wide Association StudyTranscription Factors
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The expression level of the orphan nuclear receptor GCNF (germ cell nuclear factor) is critical for neuronal differentiation.

2004

The germ cell nuclear factor (GCNF) is essential for normal embryonic development and gametogenesis. To test the prediction that GCNF is additionally required for neuronal differentiation, we used the mouse embryonal carcinoma cell line PCC7-Mz1, which represents an advantageous model to study neuronal cells from the stage of fate choice until the acquirement of functional competence. We generated stable transfectants that express gcnf sense or antisense RNA under the control of a tetracycline-regulated promoter. After retinoic acid-induced withdrawal from the cell cycle, sense clones developed a neuron network with changed properties, and the time course of neuron maturation was shortened.…

Patch-Clamp TechniquesGerm cell nuclear factorSynaptophysinDown-RegulationGene ExpressionReceptors Cytoplasmic and NuclearNerve Tissue ProteinsTretinoinBiologyNestinMiceEndocrinologyGAP-43 ProteinIntermediate Filament ProteinsNuclear Receptor Subfamily 6 Group A Member 1AnimalsRNA AntisenseMolecular BiologyNeuronsCell CycleCell PolarityCell DifferentiationGeneral MedicineCell cycleNestinCell biologyUp-RegulationNeuroepithelial cellDNA-Binding Proteinsnervous systemNeuron maturationSynaptophysinbiology.proteinNeuron differentiationStem cellMicrotubule-Associated ProteinsMolecular endocrinology (Baltimore, Md.)
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Modulation of Hedgehog target gene expression by the Fused serine-threonine kinase in wing imaginal discs

1998

0925-4773 doi: DOI: 10.1016/S0925-4773(98)00130-0; The Fused (Fu) serine–threonine kinase and the Suppressor of fused (Su(fu)) product are part of the Hedgehog (Hh) signalling pathway both in embryos and in imaginal discs. In wing imaginal discs, the Hh signal induces Cubitus interruptus (Ci) accumulation and activates patched (ptc) and decapentaplegic (dpp) expression along the anterior/posterior (A/P) boundary. In this paper, we have examined the role of the Fu and Su(fu) proteins in the regulation of Hh target gene expression in wing imaginal discs, by using different classes of fu alleles and an amorphic Su(fu) mutation. We show that, at the A/P boundary, Fu kinase activity is involved …

PatchedEmbryologyanimal structuresReceptors Cell SurfaceBiologyProtein Serine-Threonine KinasesSignal transductionCubitus interruptusImaginal disc developmentMorphogenesisAnimalsDrosophila ProteinsWings AnimalHedgehog ProteinsKinase activitySuppressor of fusedGeneticsSerine/threonine-specific protein kinaseHomeodomain ProteinsDecapentaplegicFusedGene Expression Regulation DevelopmentalMembrane ProteinsCi proteinHedgehog signaling pathwayCell biologyDNA-Binding ProteinsRepressor ProteinsImaginal discDrosophila melanogasterInsect ProteinsDrosophilaHedgehogMorphogenTranscription FactorsDevelopmental Biology
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Endothelial Wnt/β-catenin signaling inhibits glioma angiogenesis and normalizes tumor blood vessels by inducing PDGF-B expression

2012

Wnt modulates glioma vascularization by regulating PDGF-B expression.

PathologyAngiogenesisCentral Nervous System NeoplasmsMice0302 clinical medicineImmunology and AllergyWnt Signaling Pathwaybeta Catenin0303 health sciencesbiologyNeovascularization PathologicBrain NeoplasmsWnt signaling pathwayIntracellular Signaling Peptides and ProteinsForkhead Transcription FactorsGliomaProto-Oncogene Proteins c-sis3. Good healthmedicine.anatomical_structureBlood-Brain Barrier030220 oncology & carcinogenesiscardiovascular systemIntercellular Signaling Peptides and ProteinsFemalemedicine.medical_specialtyBeta-cateninEndotheliumImmunologyNotch signaling pathwayMice NudeWnt1 ProteinMural cellArticle03 medical and health sciencesGliomamedicineAnimalsHumansddc:610neoplasms030304 developmental biologyAdaptor Proteins Signal TransducingCalcium-Binding ProteinsMembrane Proteinsmedicine.diseaseXenograft Model Antitumor Assaysnervous system diseasesDKK1Cancer researchbiology.proteinEndothelium VascularNeoplasm Grading
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The analysis of modified peroxisome proliferator responsive elements of the peroxisomal bifunctional enzyme in transfected HepG2 cells reveals two re…

1995

AbstractPeroxisome proliferators (PPs) are non-genotoxic carcinogens in rodents. They can induce the expression of numerous genes via the heterodimerization of two members of the steroid hormone receptor superfamily, called the peroxisome proliferator-activated receptor (PPAR) and the 9-cis retinoic acid receptor (RXR). Many of the PP responsive genes possess a peroxisome proliferator response element (PPRE) formed by two TGACCT-related motifs. The bifunctional enzyme (HD) PPRE contains 3 such motifs, creating DR1 and DR2 sequences. PPAR and RXR regulate transcription via the DR1 element while DR2 modulates the expression of the gene via auxiliary factors in HepG2 cells.

Peroxisome proliferator-activated receptor gammaReceptors Retinoic AcidSteroid hormone receptorMolecular Sequence DataResponse elementBiophysicsReceptors Cytoplasmic and NuclearPeroxisome proliferator-activated receptorchemical and pharmacologic phenomenaIn Vitro TechniquesRegulatory Sequences Nucleic AcidRetinoid X receptorBiologyPeroxisomal Bifunctional EnzymeTransfectionMicrobodiesBiochemistryGene Expression Regulation EnzymologicTranscriptional activationPeroxisomal Bifunctional EnzymeMultienzyme ComplexesStructural BiologyPeroxisome proliferator response element9-cis Retinoic acid receptor alphaTumor Cells CulturedGeneticsHumansRNA MessengerIsomerasesEnoyl-CoA HydrataseMolecular Biologychemistry.chemical_classificationBinding SitesBase Sequence3-Hydroxyacyl CoA DehydrogenasesPeroxisome proliferator-activated receptorCell BiologyDNA-Binding ProteinsRetinoic acid receptorRetinoid X ReceptorsLiverOligodeoxyribonucleotidesBiochemistrychemistryRat peroxisomal enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenaseEnzyme InductionPeroxisome proliferator-activated receptor alphaTranscription FactorsFEBS Letters
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Functional characterization of a peroxisome proliferator response-element located in the intron 3 of rat peroxisomal thiolase B gene.

2003

Expression of the rat peroxisomal 3-ketoacyl-CoA thiolase gene B is induced by peroxisome proliferators. Although a sequence element like a peroxisome proliferator-activated receptor (PPAR)-binding site is located in the promoter region of this gene, we previously found that this element is competent for the activation by hepatocyte nuclear factor-4, but not functional with PPARalpha. We describe here a new peroxisome proliferator-response element located in the intron 3 (+1422/+1434) that binds in vitro the PPARalpha/retinoid X receptor alpha heterodimer and confers the induction by PPARalpha in transfection assays. We propose a model of regulation of the rat thiolase B gene involving thos…

Peroxisome proliferator-activated receptor gammaResponse elementBiophysicsPeroxisome proliferator-activated receptorReceptors Cytoplasmic and NuclearRetinoid X receptorBiochemistryGene Expression Regulation EnzymologicStructure-Activity RelationshipPeroxisomesAnimalsAcetyl-CoA C-AcetyltransferaseMolecular BiologyCells Culturedchemistry.chemical_classificationThiolaseChemistryCell BiologyPhosphoproteinsMolecular biologyIntronsRatsDNA-Binding ProteinsBiochemistryHepatocyte Nuclear Factor 4LiverPeroxisome proliferator-activated receptor deltaPeroxisome ProliferatorsPeroxisome proliferator-activated receptor alphaPPARGC1BTranscription FactorsBiochemical and biophysical research communications
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Muscarinic acetylcholine receptor trafficking in streptolysin O-permeabilized MDCK cells.

1996

We investigated the validity of streptolysin O (SLO)-permeabilized Madin-Darbin canine kidney (MDCK) cells which express muscarinic acetylcholine receptors (mAChRs) coupled to pertussis toxin-sensitive guanine nucleotide-binding proteins (G proteins) for the study of the molecular machinery that regulated mAChR internalization and recycling. Exposure of SLO-permeabilized cells to carbachol-reduced cell surface receptor number by up to 40% without changing total receptor number. The kinetics and maximal extent of receptor internalization as well as the potency of carbachol to induce receptor internalization were almost identical in SLO-permeabilized and non-permeabilized cells. Using this se…

PharmacologyG protein-coupled receptor kinasemedia_common.quotation_subjectB-cell receptorMuscarinic acetylcholine receptor M3General MedicineMuscarinic acetylcholine receptor M1BiologyKidneyReceptors MuscarinicPermeabilityCell biologyAdenosine TriphosphateDogsBacterial ProteinsCell surface receptorGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Muscarinic acetylcholine receptor M5StreptolysinsEnzyme-linked receptorAnimalsInternalizationCells Culturedmedia_commonNaunyn-Schmiedeberg's archives of pharmacology
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In Vitro Analysis of the Two-Component System MtrB-MtrA from Corynebacterium glutamicum▿ †

2007

ABSTRACT The two-component system MtrBA is involved in the osmostress response of Corynebacterium glutamicum . MtrB was reconstituted in a functionally active form in liposomes and showed autophosphorylation and phosphatase activity. In proteoliposomes, MtrB activity was stimulated by monovalent cations used by many osmosensors for the detection of hypertonicity. Although MtrB was activated by monovalent cations, they lead in vitro to a general stabilization of histidine kinases and do not represent the stimulus for MtrB to sense hyperosmotic stress.

PhosphataseCorynebacteriumEnzyme ActivatorsMicrobiologyCorynebacterium glutamicumEnzyme activatorBacterial ProteinsOsmotic PressurePhosphorylationMolecular BiologyHistidinebiologyAutophosphorylationRNA-Binding ProteinsCations Monovalentbiology.organism_classificationAdaptation PhysiologicalTwo-component regulatory systemPhosphoric Monoester HydrolasesCorynebacterium glutamicumBiochemistryLiposomesPhosphorylationATP-Binding Cassette TransportersSignal TransductionTranscription Factors
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Tyrosine-phosphorylation-dependent and Rho-protein-mediated control of cellular phosphatidylinositol 4,5-bisphosphate levels

1998

The polyphosphoinositide PtdIns(4,5)P2, best known as a substrate for phospholipase C isozymes, has recently been recognized to be involved in a variety of other cellular processes. The aim of this study was to examine whether the cellular levels of this versatile phospholipid are controlled by tyrosine phosphorylation. The studies were performed in human embryonic kidney (HEK)-293 cells stably expressing the M3 muscarinic acetylcholine receptor. Inhibition of tyrosine phosphatases by pervanadate induced an up-to-approx.-2.5-fold increase in the total cellular level of PtdIns(4,5)P2, which was both time- and concentration-dependent. In contrast, the tyrosine kinase inhibitors, genistein and…

Phosphatidylinositol 45-DiphosphateBacterial ToxinsBiologyBiochemistryCell LineGTP Phosphohydrolaseschemistry.chemical_compoundEnzyme activatorBacterial ProteinsGTP-Binding ProteinsPhospholipase DHumansPhosphorylationTyrosinerhoB GTP-Binding ProteinMolecular BiologyPhospholipase CADP-Ribosylation FactorsClostridioides difficilePhospholipase DMembrane ProteinsTyrosine phosphorylationCell BiologyTyrphostinsGenisteinCell biologyEnzyme ActivationBiochemistryPhosphatidylinositol 45-bisphosphatechemistryTyrosinePhosphorylationVanadatesTyrosine kinaseResearch ArticleBiochemical Journal
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A role for Rho in receptor- and G protein-stimulated phospholipase C Reduction in phosphatidylinositol 4,5-bisphosphate by Clostridium difficile toxi…

1996

Receptors coupled to heterotrimeric guanine nucleotide-binding proteins (G proteins) activate phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2)-hydrolyzing phospholipase C (PLC) enzymes by activated alpha of free beta gamma subunits of the relevant G proteins. To study whether low molecular weight G proteins of the Rho family are involved in receptor signaling to PLC, we examined the effect of Clostridium difficile toxin B, which glucosylates and thereby inactivates Rho proteins, on the regulation of PLC activity in human embryonic kidney (HEK) cells stably expressing the m3 muscarinic acetylcholine receptor (mAChR) subtype. Toxin B treatment of HEK cells did not affect basal PLC activi…

Phosphatidylinositol 45-DiphosphateBotulinum ToxinsG proteinBacterial ToxinsClostridium difficile toxin AClostridium difficile toxin BBiologychemistry.chemical_compoundBacterial ProteinsGTP-Binding ProteinsHeterotrimeric G proteinHumansPhosphatidylinositolCells CulturedADP Ribose TransferasesPharmacologyPhospholipase CHEK 293 cellsGeneral MedicineReceptors MuscarinicMolecular biologyCell biologychemistryPhosphatidylinositol 45-bisphosphateType C PhospholipasesrhoA GTP-Binding ProteinNaunyn-Schmiedeberg's Archives of Pharmacology
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