Search results for "HEK293 Cell"

showing 10 items of 201 documents

Encephalitis with Autoantibodies against the Glutamate Kainate Receptors GluK2

2021

OBJECTIVE: The objective of this study was to report the identification of antibodies against the glutamate kainate receptor subunit 2 (GluK2-abs) in patients with autoimmune encephalitis, and describe the clinical-immunological features and antibody effects. METHODS: Two sera from 8 patients with similar rat brain immunostaining were used to precipitate the antigen from neuronal cultures. A cell-based assay (CBA) with GluK2-expressing HEK293 cells was used to assess 596 patients with different neurological disorders, and 23 healthy controls. GluK2-ab effects were determined by confocal microscopy in cultured neurons and electrophysiology in GluK2-expressing HEK293 cells. RESULTS: Patients'…

0301 basic medicinePathologymedicine.medical_specialtyAutoimmunityKainate receptor03 medical and health sciences0302 clinical medicineReceptors Kainic AcidAntigenCerebellummedicineAnimalsHumansReceptorencephalitis ; autoantibodies ; GluK2AutoantibodiesNeuronsAutoimmune encephalitisbiologyAutoimmunitatbusiness.industryAutoantibodyGlutamate receptorEncefalitismedicine.diseaseRatsHEK293 Cells030104 developmental biologyNeurologybiology.proteinEncephalitisNeurology (clinical)Antibodybusiness030217 neurology & neurosurgeryEncephalitisAnnals of Neurology
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Familial Central Hypothyroidism Caused by a Novel IGSF1 Gene Mutation.

2016

Congenital hypothyroidism of central origin (CH-C) is a rare disease in which thyroid hormone deficiency is caused by insufficient thyrotropin stimulation of a normal thyroid gland. A recently described syndrome of isolated CH-C and macroorchidism was attributed to loss-of-function mutations of the immunoglobulin superfamily, member 1 gene (IGSF1).CH-C was diagnosed in three siblings. The TRH, TRHR, and TSHB genes were sequenced followed by whole-exome sequencing in the proband. A mutation identified in IGSF1 was analyzed by direct PCR sequencing in family members. The effects of the mutation were assessed by in vitro studies in HEK293 cells.The index case was negative for mutations in TRH,…

0301 basic medicineProbandMaleendocrine systemEndocrinology Diabetes and MetabolismDNA Mutational AnalysisImmunoglobulinsThyrotropin030209 endocrinology & metabolismBiology03 medical and health sciences0302 clinical medicineEndocrinologyHypothyroidismmedicineCentral hypothyroidismCongenital HypothyroidismHumansInsertionThyrotropin-Releasing HormoneGeneticsMacroorchidismReceptors Thyrotropin-Releasing HormoneSiblingsThyroidInfant NewbornInfantMembrane Proteinsmedicine.diseaseMolecular biologyCongenital hypothyroidismIGSF1030104 developmental biologymedicine.anatomical_structureHEK293 CellsChild PreschoolMutation (genetic algorithm)MutationThyroid : official journal of the American Thyroid Association
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Discovery and Biological Evaluation of Potent and Selective N-Methylene Saccharin-Derived Inhibitors for Rhomboid Intramembrane Proteases

2017

Rhomboids are intramembrane serine proteases and belong to the group of structurally and biochemically most comprehensively characterized membrane proteins. They are highly conserved and ubiquitously distributed in all kingdoms of life and function in a wide range of biological processes, including epidermal growth factor signaling, mitochondrial dynamics, and apoptosis. Importantly, rhomboids have been associated with multiple diseases, including Parkinson's disease, type 2 diabetes, and malaria. However, despite a thorough understanding of many structural and functional aspects of rhomboids, potent and selective inhibitors of these intramembrane proteases are still not available. In this …

0301 basic medicineProteasesSerine Proteinase InhibitorsChemistryRhomboid proteaseRhomboidHEK 293 cellsRational designMembrane ProteinsBiochemistryIn vitroArticleSerine03 medical and health sciences030104 developmental biologyHEK293 CellsSaccharinBiochemistryMembrane proteinDrug DesignComputer-Aided DesignHumansSerine Proteases
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BAG3 regulates total MAP1LC3B protein levels through a translational but not transcriptional mechanism

2015

Autophagy is mainly regulated by post-translational and lipid modifications of ATG proteins. In some scenarios, the induction of autophagy is accompanied by increased levels of certain ATG mRNAs such as MAP1LC3B/LC3B, ATG5 or ATG12. However, little is known about the regulation of ATG protein synthesis at the translational level. The cochaperone of the HSP70 system BAG3 (BCL2-associated athanogene 3) has been associated to LC3B lipidation through an unknown mechanism. In the present work, we studied how BAG3 controls autophagy in HeLa and HEK293 cells. Our results showed that BAG3 regulates the basal amount of total cellular LC3B protein by controlling its mRNA translation. This effect was …

0301 basic medicineProteasome Endopeptidase ComplexTranscription GeneticATG8ATG5BiologyBAG3ATG1203 medical and health sciences0302 clinical medicineProtein biosynthesisHumansRNA MessengerMolecular BiologyAdaptor Proteins Signal TransducingGeneticsGene knockdownAutophagyCell BiologyLipidsBasic Research PaperCell biologyHEK293 Cells030104 developmental biologyProtein BiosynthesisProteolysisApoptosis Regulatory ProteinsLysosomesMicrotubule-Associated ProteinsMAP1LC3B030217 neurology & neurosurgeryHeLa Cells
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Direct Visualization of the Conformational Dynamics of Single Influenza Hemagglutinin Trimers

2018

Influenza hemagglutinin (HA) is the canonical type I viral envelope glycoprotein and provides a template for the membrane-fusion mechanisms of numerous viruses. The current model of HA-mediated membrane fusion describes a static "spring-loaded" fusion domain (HA2) at neutral pH. Acidic pH triggers a singular irreversible conformational rearrangement in HA2 that fuses viral and cellular membranes. Here, using single-molecule Förster resonance energy transfer (smFRET)-imaging, we directly visualized pH-triggered conformational changes of HA trimers on the viral surface. Our analyses reveal reversible exchange between the pre-fusion and two intermediate conformations of HA2. Acidification of p…

0301 basic medicineProtein ConformationHemagglutinin (influenza)Hemagglutinin Glycoproteins Influenza VirusBiologyArticleGeneral Biochemistry Genetics and Molecular BiologyReaction coordinate03 medical and health sciencesViral envelopeInfluenza HumanFluorescence Resonance Energy TransferHumansDynamic equilibriumFusionCell MembraneLipid bilayer fusionHydrogen-Ion ConcentrationVirus InternalizationSingle Molecule ImagingHEK293 CellsHemagglutinins030104 developmental biologyMembraneFörster resonance energy transferA549 CellsInfluenza A virusBiophysicsbiology.proteinProtein BindingCell
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The Crystal Structure of Gurmarin, a Sweet Taste–Suppressing Protein: Identification of the Amino Acid Residues Essential for Inhibition

2018

International audience; Gurmarin is a highly specific sweet-taste suppressing protein in rodents that is isolated from the Indian plant Gymnemasylvestre. Gurmarin consists of 35 amino acid residues containing three intramolecular disulfide bridges that form a cystine knot. Here, we report the crystal structure of gurmarin at a 1.45 Å resolution and compare it with previously reported NMR solution structures. The atomic structure at this resolution allowed us to identify a very flexible region consisting of hydrophobic residues. Some of these amino acid residues had been identified as a putative binding site for the rat sweet taste receptor in a previous study. By combining alanine-scanning …

0301 basic medicineProtein ConformationPhysiologyCrystal structureCrystallography X-Ray03 medical and health sciencesBehavioral NeuroscienceGPCRsweet tastetaste receptorPhysiology (medical)goût sucréAnimalsHumansG protein-coupled receptorAmino AcidsBinding siteReceptorNuclear Magnetic Resonance BiomolecularPlant ProteinsGurmarininhibiteur030102 biochemistry & molecular biologybiologyChemistryMutagenesisCystine knotGymnema sylvestreSweet tastebiology.organism_classificationRecombinant ProteinsSensory SystemsRats3. Good healthinhibitorHEK293 Cells030104 developmental biologyBiochemistryGymnema sylvestreknottin[SDV.AEN]Life Sciences [q-bio]/Food and NutritionHydrophobic and Hydrophilic InteractionsChemical Senses
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Quantitative Proteomics Reveals Changes Induced by TIMP-3 on Cell Membrane Composition and Novel Metalloprotease Substrates

2021

Ectodomain shedding is a key mechanism of several biological processes, including cell-communication. Disintegrin and metalloproteinases (ADAMs), together with the membrane-type matrix metalloproteinases, play a pivotal role in shedding transmembrane proteins. Aberrant shedding is associated to several pathological conditions, including arthritis. Tissue inhibitor of metalloproteases 3 (TIMP-3), an endogenous inhibitor of ADAMs and matrix metalloproteases (MMPs), has been proven to be beneficial in such diseases. Thus, strategies to increase TIMP-3 bioavailability in the tissue have been sought for development of therapeutics. Nevertheless, high levels of TIMP-3 may lead to mechanism-based …

0301 basic medicineProteomicsADAM15ProteomeCellMatrix metalloproteinaseMass SpectrometryCell membranelcsh:Chemistryanalysis [Proteome]lcsh:QH301-705.5proteomicSpectroscopybiologyChemistrytissue inhibitor of metalloproteases 3 (TIMP-3)General MedicineTransmembrane proteinComputer Science ApplicationsCell biologymedicine.anatomical_structureEctodomainddc:540TIMP3 protein humanmetalloproteinaseectodomain sheddingmetabolism [Tissue Inhibitor of Metalloproteinase-3]Quantitative proteomicsADAM15 protein humanchemistry [Cell Membrane]Catalysismetabolism [Cell Membrane]ArticlemetalloproteinasesInorganic Chemistry03 medical and health sciencestissue inhibitor of metalloproteases 3 (TIMP-3).medicineDisintegrinHumansPhysical and Theoretical ChemistryMolecular BiologyTissue Inhibitor of Metalloproteinase-3030102 biochemistry & molecular biologyOrganic ChemistryCell MembraneMembrane Proteinsmetabolism [Proteome]ADAM Proteins030104 developmental biologyHEK293 Cellslcsh:Biology (General)lcsh:QD1-999metabolism [ADAM Proteins]biology.proteinmetabolism [Membrane Proteins]International Journal of Molecular Sciences
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DICER- and MMSET-catalyzed H4K20me2 recruits the nucleotide excision repair factor XPA to DNA damage sites

2017

The endoribonuclease DICER facilitates chromatin decondensation during lesion recognition following UV exposure. Chitale and Richly show that DICER mediates the recruitment of the methyltransferase MMSET, which catalyzes the dimethylation of histone H4 at lysine 20 and facilitates the recruitment of the nucleotide excision repair factor XPA.

0301 basic medicineRibonuclease IIIDNA RepairDNA damageDNA repairUltraviolet Raysgenetic processes27Article24DEAD-box RNA HelicasesHistones03 medical and health sciencesCell Line TumorHumansResearch ArticlesbiologyLysinefungiEndoribonuclease Dicerfood and beverages37Cell BiologyDNA Repair PathwayHistone-Lysine N-MethyltransferaseCell biologyChromatinXeroderma Pigmentosum Group A ProteinRepressor Proteinsenzymes and coenzymes (carbohydrates)030104 developmental biologyHistoneHEK293 Cellsbiology.proteinBiocatalysisDicerNucleotide excision repairDNA DamageThe Journal of Cell Biology
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A protein-RNA interaction atlas of the ribosome biogenesis factor AATF

2018

AbstractAATF is a central regulator of the cellular outcome upon p53 activation, a finding that has primarily been attributed to its function as a transcription factor. Recent data showed that AATF is essential for ribosome biogenesis and plays a role in rRNA maturation. AATF has been implicated to fulfil this role through direct interaction with rRNA and was identified in several RNA-interactome capture experiments. Here, we provide a first comprehensive analysis of the RNA bound by AATF using CLIP-sequencing. Interestingly, this approach shows predominant binding of the 45S pre-ribosomal RNA precursor molecules. Furthermore, AATF binds to mRNAs encoding for ribosome biogenesis factors as …

0301 basic medicineRibosomal ProteinsRegulatorRibosome biogenesisProteomic analysislcsh:MedicineInteractomeArticleCell Line03 medical and health sciencesMice0302 clinical medicineRNA PrecursorsAnimalsHumansSmall nucleolar RNABinding sitelcsh:ScienceTranscription factor030304 developmental biologyRNA metabolism0303 health sciencesMultidisciplinaryBinding SitesChemistrylcsh:RRNARibosomal RNACell biologyRibosome Subunits SmallRepressor Proteins030104 developmental biologyHEK293 Cells030220 oncology & carcinogenesisRNAlcsh:QApoptosis Regulatory ProteinsRibosomes030217 neurology & neurosurgeryProtein BindingScientific Reports
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Sox8 and Sox10 jointly maintain myelin gene expression in oligodendrocytes

2017

In Schwann cells of the vertebrate peripheral nervous system, induction of myelination and myelin maintenance both depend on the HMG-domain-containing transcription factor Sox10. In oligodendrocytes of the central nervous system, Sox10 is also essential for the induction of myelination. Its role in late phases of myelination and myelin maintenance has not been studied so far. Here, we show that these processes are largely unaffected in mice that lack Sox10 in mature oligodendrocytes. As Sox10 is co-expressed with the related Sox8, we also analyzed oligodendrocytes and myelination in Sox8-deficient mice. Again, we could not detect any major abnormalities. Expression of many myelin genes was …

0301 basic medicineSOX10Central nervous systemGene ExpressionBiologyMice03 medical and health sciencesCellular and Molecular NeuroscienceMyelin0302 clinical medicineGene expressionmedicineAnimalsHumansCell LineageGeneMyelin SheathMice KnockoutSOXE Transcription FactorsHEK 293 cellsOligodendrocyteOligodendrogliaHEK293 Cells030104 developmental biologymedicine.anatomical_structurenervous systemNeurologyMyelin maintenanceembryonic structuresSchwann CellsNeuroscience030217 neurology & neurosurgeryHeLa CellsGlia
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