2016
Mood, stress and longevity: convergence on ANK3
Rangaraju S, Levey DF, Nho K, Jain N, Andrews KD, Le-Niculescu H, Salomon DR, Saykin AJ, Petrascheck M, Niculescu AB. Mood, stress and longevity: convergence on ANK3. Molecular Psychiatry 2016, 21: 1037-1049. PMID: 27217151, PMCID: PMC9798616, DOI: 10.1038/mp.2016.65.Peer-Reviewed Original ResearchConceptsSignificant single nucleotide polymorphismsC. elegansGenome-wide association study approachLongevity/agingFunctional genomics approachConvergent functional genomics approachOrthologs of genesOxidative stress resistanceCorresponding human orthologsHutchinson-Gilford progeria syndromeSeries of genesTop candidate genesGene expression studiesOlder wormsUnbiased drug screenANK3 expressionGenomic approachesAntagonistic pleiotropyGene expression biomarkersHuman orthologLow expression levelsStress resistanceSingle nucleotide polymorphismsBioinformatics analysisTop genes
2015
Calcineurin Aγ is a Functional Phosphatase That Modulates Synaptic Vesicle Endocytosis*
Cottrell JR, Li B, Kyung JW, Ashford CJ, Mann JJ, Horvath TL, Ryan TA, Kim SH, Gerber DJ. Calcineurin Aγ is a Functional Phosphatase That Modulates Synaptic Vesicle Endocytosis*. Journal Of Biological Chemistry 2015, 291: 1948-1956. PMID: 26627835, PMCID: PMC4722470, DOI: 10.1074/jbc.m115.705319.Peer-Reviewed Original ResearchConceptsSynaptic vesicle cyclingVesicle cyclingHippocampal neuronsPsychiatric diseasesSynaptic vesicle endocytosisCultured rat hippocampal neuronsRNAi-mediated knockdownCalcineurin catalytic subunitRat hippocampal neuronsFunctional phosphataseCombination of immunocytochemistryVesicle endocytosisLow expression levelsCatalytic subunitPresynaptic substratePresynaptic terminalsPresynaptic functionΓ isoformsCalcineurin AαCatalytic isoformsImmuno-EMSpecific functionsExpression levelsMost tissuesPPP3CC
2011
Characterization of HCV Interactions with Toll-Like Receptors and RIG-I in Liver Cells
Eksioglu E, Zhu H, Bayouth L, Bess J, Liu H, Nelson D, Liu C. Characterization of HCV Interactions with Toll-Like Receptors and RIG-I in Liver Cells. PLOS ONE 2011, 6: e21186. PMID: 21695051, PMCID: PMC3117876, DOI: 10.1371/journal.pone.0021186.Peer-Reviewed Original ResearchMeSH KeywordsCell DeathCell Line, TumorDEAD Box Protein 58DEAD-box RNA HelicasesDown-RegulationHepacivirusHost-Pathogen InteractionsHumansInterferon-betaLiverProtein BindingReceptors, ImmunologicSignal TransductionTNF-Related Apoptosis-Inducing LigandToll-Like ReceptorsViral Envelope ProteinsVirus ReplicationConceptsHuh7.5 cellsViral replicationHCV chronic patientsExpression of TLR3Toll-like receptorsHCV envelope proteinsExpression levelsRIG-I expressionHCV interactionChronic patientsHCVTRAIL pathwayViral escapeViral infectionInnate immunityViral pathogenesisTLR3Induction of apoptosisAntiviral stateIFN inductionLow expression levelsLiver cellsLH86Envelope proteinIFN
2007
Inferring activity changes of transcription factors by binding association with sorted expression profiles
Cheng C, Yan X, Sun F, Li LM. Inferring activity changes of transcription factors by binding association with sorted expression profiles. BMC Bioinformatics 2007, 8: 452. PMID: 18021409, PMCID: PMC2194743, DOI: 10.1186/1471-2105-8-452.Peer-Reviewed Original ResearchConceptsTranscription factorsExpression profilesMicroarray dataTarget gene selectionPost-transcriptional modificationsChIP-chip dataMicroarray expression profilesExpression differentiationLow expression levelsProfile of expressionTarget genesRegulatory mechanismsGene expressionBiological processesMicroarray studiesAffinity dataGene selectionSame machineryExpression levelsGenesActivity changesSignificance cutoffDifferentiationMeaningful hypothesesAffinity scores
2001
β1 adducin gene expression in DRG is developmentally regulated and is upregulated by glial-derived neurotrophic factor and nerve growth factor
Ghassemi F, Dib-Hajj S, Waxman S. β1 adducin gene expression in DRG is developmentally regulated and is upregulated by glial-derived neurotrophic factor and nerve growth factor. Brain Research 2001, 90: 118-124. PMID: 11406290, DOI: 10.1016/s0169-328x(01)00091-2.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalmodulin-Binding ProteinsCells, CulturedCytoskeletonGanglia, SpinalGene Expression ProfilingGene Expression Regulation, DevelopmentalGlial Cell Line-Derived Neurotrophic FactorNerve Growth FactorNerve Growth FactorsNerve Tissue ProteinsNeurons, AfferentNeuroprotective AgentsRatsRats, Sprague-DawleyReverse Transcriptase Polymerase Chain ReactionConceptsGlial-derived neurotrophic factorReal-time reverse transcription-polymerase chain reactionNeurotrophic factorTrigeminal ganglionDRG culturesRat DRGGrowth factorDorsal root ganglion culturesAdult rat DRGRat dorsal root ganglion culturesSuperior cervical ganglionReverse transcription-polymerase chain reactionExpression levelsNerve growth factorNon-neural tissuesDRG tissueCervical ganglionSciatic nervePolymerase chain reactionGanglion culturesAdducin geneLevel of expressionGangliaLow expression levelsGene expression
2000
Differential localization of human nongastric H+-K+-ATPase ATP1AL1 in polarized renal epithelial cells
Reinhardt J, Grishin A, Oberleithner H, Caplan M. Differential localization of human nongastric H+-K+-ATPase ATP1AL1 in polarized renal epithelial cells. American Journal Of Physiology. Renal Physiology 2000, 279: f417-f425. PMID: 10966921, DOI: 10.1152/ajprenal.2000.279.3.f417.Peer-Reviewed Original ResearchConceptsApical plasma membranePlasma membraneRenal epithelial cellsIon pumpsPlasma membrane localizationConfocal immunofluorescence microscopyEpithelial cellsATPase beta subunitRenal epithelial cell lineMembrane localizationLow expression levelsEpithelial cell lineSurface biotinylationPump subunitsBeta subunitFunctional expressionStable transfectionLateral membranesMDCK cellsATP1AL1Immunofluorescence microscopyDifferential localizationSorting mechanismStable interactionExpression levels
1999
Mutational Analysis of Cell Cycle Inhibition by Integrin β1C *
Meredith J, Kiosses W, Takada Y, Schwartz M. Mutational Analysis of Cell Cycle Inhibition by Integrin β1C *. Journal Of Biological Chemistry 1999, 274: 8111-8116. PMID: 10075712, DOI: 10.1074/jbc.274.12.8111.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceAnimalsCells, CulturedDNA Mutational AnalysisDNA ReplicationDose-Response Relationship, DrugHumansIntegrin beta1MiceMice, Inbred C3HMolecular Sequence DataMutagenesis, Site-DirectedReceptors, Interleukin-2Recombinant Fusion ProteinsStructure-Activity RelationshipConceptsCytoplasmic domainGreen fluorescent protein fusion proteinFluorescent protein fusion proteinProtein fusion proteinMembrane-proximal regionCell cycle progressionAnalysis of deletionsHuman interleukin-2 receptorBeta5 cytoplasmic domainsMembrane targetingMouse 10T1/2 cellsGrowth inhibitionCell cycle inhibitionTransmembrane domainLow expression levelsProstate epithelial cellsAcid domainCytoplasmic variantsTac subunitMutational analysisCycle progressionFusion proteinIntact receptorCell line DU145Human endothelial cell line
1993
MEK2 is a kinase related to MEK1 and is differentially expressed in murine tissues.
Brott BK, Alessandrini A, Largaespada DA, Copeland NG, Jenkins NA, Crews CM, Erikson RL. MEK2 is a kinase related to MEK1 and is differentially expressed in murine tissues. Molecular Cancer Research 1993, 4: 921-9. PMID: 8297798.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino AcidsAnimalsAnimals, NewbornBase SequenceBrainChromosome MappingCloning, MolecularFemaleGene Expression RegulationMaleMAP Kinase Kinase 1MAP Kinase Kinase 2MiceMitogen-Activated Protein Kinase KinasesMolecular Sequence DataNucleic Acid HybridizationProtein Serine-Threonine KinasesProtein-Tyrosine KinasesRecombinant ProteinsRNA, MessengerSequence AnalysisConceptsERK-1Dual-specificity kinaseMurine chromosome 9Substantial sequence homologyErk/MAPMultigene familyLow expression levelsMEK2 proteinsAdult mouse brainSequence homologyAmino terminusDifferent genesERK-2MEK2MEK1Northern analysisChromosome 9Complementary DNAMurine tissuesExpression levelsKinase
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