Search results for "binding"

showing 10 items of 3896 documents

Species-specific mechanisms for cholesterol 7alpha-hydroxylase (CYP7A1) regulation by drugs and bile acids.

2005

The gene encoding cholesterol 7alpha-hydroxylase (CYP7A1) is tightly regulated in order to control intrahepatic cholesterol and bile acid levels. Ligands of the xenobiotic-sensing pregnane X receptor inhibit CYP7A1 expression. To retrace the evolution of the molecular mechanisms underlying CYP7A1 inhibition, we used a chicken hepatoma cell system that retains the ability to be induced by phenobarbital and other drugs. Whereas bile acids regulate CYP7A1 via small heterodimer partner and liver receptor homolog-1, mRNA expression of these nuclear receptors is unchanged by xenobiotics. Instead, drugs repress chicken hepatic nuclear factor 4alpha (HNF4alpha) transcript levels concomitant with a …

Receptors Steroidmedicine.drug_classMolecular Sequence DataBiophysicsReceptors Cytoplasmic and NuclearBiologyIn Vitro TechniquesCholesterol 7 alpha-hydroxylaseBiochemistryGene Expression Regulation EnzymologicBile Acids and SaltsMiceSpecies SpecificitymedicineAnimalsHumansRNA MessengerCholesterol 7-alpha-HydroxylaseMolecular BiologyCells CulturedMice KnockoutPregnane X receptorBile acidLiver receptor homolog-1Pregnane X ReceptorPhosphoproteinsRecombinant ProteinsDNA-Binding ProteinsBiochemistryNuclear receptorHepatocyte Nuclear Factor 4PhenobarbitalSmall heterodimer partnerHepatocytesFarnesoid X receptorSignal transductionChickensSignal TransductionTranscription FactorsArchives of biochemistry and biophysics
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Suppressor of fused links Fused and Cubitus interruptus on the Hedgehog signalling pathway

1998

0960-9822 doi: DOI: 10.1016/S0960-9822(98)70227-1; The Hedgehog (Hh) family of signalling proteins [1] mediate inductive interactions either directly or by controlling the transcription of other secreted proteins through the action of Gli transcription factors, such as Cubitus interruptus (Ci) [2]. In Drosophila, the transcription of Hh targets requires the activation of the protein kinase Fused (Fu) and the inactivation of both Suppressor of fused (Su(fu)) and Costal-2 (Cos-2) [3]. Fu is required for Hh signalling in the embryo and in the wing imaginal disc and acts also as an antitumorigen in ovaries [4]. All fu– phenotypes are suppressed by the loss of function of Su(fu) [5]. Fu, Cos-2 a…

Recombinant Fusion ProteinsBiologyProtein Serine-Threonine KinasesGeneral Biochemistry Genetics and Molecular Biologylaw.invention03 medical and health sciences0302 clinical medicinelawTranscription (biology)AnimalsDrosophila ProteinsHedgehog ProteinsProtein kinase AIntracellular partTranscription factorHedgehog030304 developmental biology0303 health sciencesAgricultural and Biological Sciences(all)Biochemistry Genetics and Molecular Biology(all)AnatomyCi proteinCell biologyDNA-Binding ProteinsRepressor ProteinsImaginal discSuppressorInsect ProteinsRabbitsGeneral Agricultural and Biological Sciences030217 neurology & neurosurgerySignal TransductionTranscription Factors
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Purification of a biologically active recombinant glyceraldehyde 3-phosphate dehydrogenase fromCandida albicans

1999

We report here the purification of a functionally active recombinant glyceraldehyde 3-phosphate dehydrogenase (GAPDH) from Candida albicans. The GAPDH protein encoded by the TDH1 gene was obtained as a glutathione S-transferase fusion protein by expression in the vector pGEX-4T-3, and purified by affinity chromatography and thrombin digestion. The purified protein displays GAPDH enzymatic activity (42 micromol NADH min(-1) mg(-1)) as well as the laminin and fibronectin binding activities previously described. In addition, the recombinant GAPDH is covalently modified by NAD linkage; this modification is stimulated by nitric oxide and probably involves a sulfhydryl group (cysteine) residue si…

Recombinant Fusion ProteinsDehydrogenaseBiologyMicrobiologyChromatography Affinitylaw.inventionchemistry.chemical_compoundstomatognathic systemAffinity chromatographylawGlyceraldehydeCandida albicansEscherichia coliGeneticsCloning MolecularMolecular BiologyGlyceraldehyde 3-phosphate dehydrogenaseGlutathione TransferaseThrombinGlyceraldehyde-3-Phosphate DehydrogenasesMolecular biologyRecombinant ProteinsKineticschemistryBiochemistryFibronectin bindingbiology.proteinRecombinant DNAGlyceraldehyde 3-phosphateCysteineFEMS Microbiology Letters
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6-mercaptopurine and 9-(2-phosphonyl-methoxyethyl) adenine (PMEA) transport altered by two missense mutations in the drug transporter gene ABCC4

2008

Multiple drug resistance protein 4 (MRP4, ABCC4) belongs to the C subfamily of the ATP-binding cassette (ABC) transporter superfamily and participates in the transport of diverse antiviral and chemotherapeutic agents such as 6-mercaptopurine (6-MP) and 9-(2-phosphonyl methoxyethyl) adenine (PMEA). We have undertaken a comprehensive functional characterization of protein variants of MRP4 found in Caucasians and other ethnicities. A total of 11 MRP4 missense genetic variants (nonsynonymous SNPs), fused to green fluorescent protein (GFP), were examined in Xenopus laevis oocytes for their effect on expression, localization, and function of the transporter. Radiolabeled 6-MP and PMEA were chosen…

Recombinant Fusion ProteinsGreen Fluorescent ProteinsMutation MissenseOrganophosphonatesXenopusATP-binding cassette transporterABCC4BiologyGreen fluorescent proteinXenopus laevisGeneticsAnimalsHumansMissense mutationGenetics (clinical)DNA Primerschemistry.chemical_classificationBase SequenceMercaptopurineAdenineWild typebiology.organism_classificationMolecular biologyTransmembrane proteinAmino acidchemistryBiochemistryMutagenesis Site-Directedbiology.proteinMultidrug Resistance-Associated ProteinsHuman Mutation
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Human germ cell differentiation from fetal- and adult-derived induced pluripotent stem cells

2010

Historically, our understanding of molecular genetic aspects of human germ cell development has been limited, at least in part due to inaccessibility of early stages of human development to experimentation. However, the derivation of pluripotent stem cells may provide the necessary human genetic system to study germ cell development. In this study, we compared the potential of human induced pluripotent stem cells (iPSCs), derived from adult and fetal somatic cells to form primordial and meiotic germ cells, relative to human embryonic stem cells. We found that ∼5% of human iPSCs differentiated to primordial germ cells (PGCs) following induction with bone morphogenetic proteins. Furthermore, …

Recombinant Fusion ProteinsInduced Pluripotent Stem CellsEmbryoid bodyHaploidyBiologyCell LineDEAD-box RNA Helicases03 medical and health sciences0302 clinical medicineGeneticsmedicineHumansInduced pluripotent stem cellMolecular BiologyEmbryonic Stem CellsGenetics (clinical)030304 developmental biology0303 health sciences030219 obstetrics & reproductive medicineSynaptonemal ComplexGene Expression ProfilingGene Expression Regulation DevelopmentalRNA-Binding ProteinsCell DifferentiationArticlesGeneral MedicineEmbryonic stem cellMolecular biologyGerm Cellsmedicine.anatomical_structureBone Morphogenetic ProteinsGerm line developmentStem cellReprogrammingGerm cellAdult stem cellHuman Molecular Genetics
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In vivo Trafficking and Localization of p24 Proteins in Plant Cells

2008

p24 proteins constitute a family of putative cargo receptors that traffic in the early secretory pathway. p24 proteins can be divided into four subfamilies (p23, p24, p25 and p26) by sequence homology. In contrast to mammals and yeast, most plant p24 proteins contain in their cytosolic C-terminus both a dilysine motif in the -3, -4 position and a diaromatic motif in the -7, -8 position. We have previously shown that the cytosolic tail of Arabidopsis p24 proteins has the ability to interact with ARF1 and coatomer (through the dilysine motif) and with COPII subunits (through the diaromatic motif). Here, we establish the localization and trafficking properties of an Arabidopsis thaliana p24 pr…

Recombinant Fusion ProteinsMolecular Sequence DataArabidopsisGolgi ApparatusVacuoleProtein Sorting SignalsBiologyEndoplasmic ReticulumBiochemistrysymbols.namesakeStructural BiologyArabidopsisGeneticsAnimalsHumansProtein IsoformsAmino Acid SequenceMolecular BiologyCOPIISecretory pathwayArabidopsis ProteinsLysineEndoplasmic reticulumMembrane ProteinsCell BiologyCOPIGolgi apparatusbiology.organism_classificationActinsCell biologyDNA-Binding ProteinsProtein TransportBiochemistryCoatomerVacuolessymbolsCOP-Coated VesiclesCarrier ProteinsTranscription FactorsTraffic
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The yeast putative transcriptional repressor RGM1 is a proline-rich zinc finger protein.

1991

Abstract I have cloned a yeast gene, RGM1, which encodes a proline-rich zinc, finger protein. rgm1 mutants do not show any obvious phenotype but overexpression of RGM1 gene greatly impairs cell growth. The proline-rich region of RGM1 attached to a heterologous DNA binding domain is able to repress the expression of the target gene. RGM1 shares similar zinc finger motifs with the mammalian Egr (early growth response) proteins as well as proline-rich sequences with a high serine and threonine content, suggesting that RGM1 and Egr proteins could have functional similarities.

Recombinant Fusion ProteinsMolecular Sequence DataRestriction MappingGene ExpressionSaccharomyces cerevisiaeBiologyZIC2TransfectionSequence Homology Nucleic AcidGene expressionGeneticsAmino Acid SequenceCloning MolecularLIM domainSIN3BZinc fingerBase SequenceZinc FingersDNA-binding domainZinc finger nucleaseRING finger domainbody regionsRepressor ProteinsBiochemistryMutagenesisCarbohydrate MetabolismPlasmidsNucleic acids research
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The polypyrimidine tract-binding protein (PTB) is involved in the post-transcriptional regulation of human inducible nitric oxide synthase expression.

2006

Human inducible nitric oxide synthase (iNOS) expression is regulated by transcriptional and post-transcriptional mechanisms. We have recently shown that the multifunctional RNA-binding proteins KH-type splicing regulatory protein and tristetraprolin are critically involved in the post-transcriptional regulation of human iNOS expression. Several reports have shown that KH-type splicing regulatory protein colocalizes with the polypyrimidine tract-binding protein (PTB), and both RNA-binding proteins seem to interact with the same mRNAs. Therefore we analyzed the involvement of PTB in human iNOS expression. In human DLD-1 cells, cytokine incubation necessary to induce iNOS expression did not ch…

Recombinant Fusion ProteinsTristetraprolinGreen Fluorescent ProteinsNitric Oxide Synthase Type IImacromolecular substancesBiologyIn Vitro TechniquesTransfectionenvironment and public healthBiochemistryGene Expression Regulation EnzymologicCell LineCell Line TumorHumansPolypyrimidine tract-binding proteinRNA MessengerEnzyme InhibitorsPromoter Regions GeneticMolecular BiologyPost-transcriptional regulationRegulation of gene expressionMessenger RNAintegumentary systemCarcinomaEpithelial CellsCell BiologyTransfectionMolecular biologyNitric oxide synthaseRNA splicingColonic Neoplasmsbiology.proteinCytokinesRNA InterferenceProtein Processing Post-TranslationalDichlororibofuranosylbenzimidazolePolypyrimidine Tract-Binding ProteinThe Journal of biological chemistry
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Specific Binding of Baculoviruses Displaying gp64 Fusion Proteins to Mammalian Cells

2001

Viral vectors displaying specific ligand binding moieties have raised an increasing interest in the area of targeted gene therapy. In this report, we describe baculovirus vectors displaying either a functional single chain antibody fragment (scFv) specific for the carcinoembryonic antigen (CEA) or the synthetic IgG binding domains (ZZ) derived from protein A of Staphylococcus aureus. In addition, the vectors were engineered to incorporate a reporter gene encoding the enhanced green fluorescent protein (EGFP) under the transcriptional regulation of the cytomegalovirus (CMV) IE promoter. Display of the targeting moieties on the viral surface was achieved through fusion to the N-terminus of gp…

Recombinant Fusion ProteinsvirusesGenetic VectorsGreen Fluorescent ProteinsImmunoglobulin Variable RegionBiophysicsSpodopteraTransfectionBiochemistryCell LineGreen fluorescent proteinViral vector03 medical and health sciencesGenes ReporterTransduction GeneticCricetinaeTumor Cells CulturedAnimalsStaphylococcal Protein AMolecular Biology030304 developmental biology0303 health sciencesReporter genebiology030302 biochemistry & molecular biologyAntibodies MonoclonalGenetic TherapyCell BiologyTransfectionFusion proteinMolecular biologyCarcinoembryonic Antigen3. Good healthLuminescent ProteinsMicroscopy FluorescenceIgG bindingbiology.proteinAntibodyProtein ABaculoviridaeViral Fusion ProteinsBiochemical and Biophysical Research Communications
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The Tobacco mosaic virus movement protein associates with but does not integrate into biological membranes

2014

Plant positive-strand RNA viruses require association with plant cell endomembranes for viral translation and replication, as well as for intra- and intercellular movement of the viral progeny. The membrane association and RNA binding of the Tobacco mosaic virus (TMV) movement protein (MP) are vital for orchestrating the macromolecular network required for virus movement. A previously proposed topological model suggests that TMV MP is an integral membrane protein with two putative -helical transmembrane (TM) segments. Here we tested this model using an experimental system that measured the efficiency with which natural polypeptide segments were inserted into the ER membrane under conditions…

Recombinant Fusion ProteinsvirusesMolecular Sequence DataImmunologyGene ExpressionMicrobiologiaBiologyEndoplasmic ReticulumMicrobiologyCell membraneGenes ReporterPlant CellsVirologymedicineTobacco mosaic virusAmino Acid SequenceMovement proteinIntegral membrane proteinStructure and AssemblyCell MembraneViral translationfungifood and beveragesBiological membraneVirologyTransmembrane proteinTransport proteinCell biologyVirusPlant Viral Movement ProteinsTobacco Mosaic VirusProtein Transportmedicine.anatomical_structureInsect ScienceHydrophobic and Hydrophilic InteractionsProtein Binding
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