2012
Nucleus Accumbens 1, a Pox virus and Zinc finger/Bric-a-brac Tramtrack Broad protein binds to TAR DNA-binding protein 43 and has a potential role in Amyotrophic Lateral Sclerosis
Scofield M, Korutla L, Jackson T, Kalivas P, Mackler S. Nucleus Accumbens 1, a Pox virus and Zinc finger/Bric-a-brac Tramtrack Broad protein binds to TAR DNA-binding protein 43 and has a potential role in Amyotrophic Lateral Sclerosis. Neuroscience 2012, 227: 44-54. PMID: 23022214, PMCID: PMC3505276, DOI: 10.1016/j.neuroscience.2012.09.043.Peer-Reviewed Original ResearchMeSH KeywordsAnalysis of VarianceAnimalsAspartic AcidCell DeathCholine O-AcetyltransferaseCytoplasmDNA-Binding ProteinsEmbryo, MammalianGene Expression RegulationGlial Fibrillary Acidic ProteinGlutamic AcidImmunoprecipitationNeoplasm ProteinsNeuronsPhosphopyruvate HydrataseProtein BindingRatsRepressor ProteinsSpinal CordTransfectionUbiquitinationConceptsNucleus accumbens-1Amyotrophic lateral sclerosisPOZ/BTB domainUbiquitin-proteasome systemTDP-43Protein 43Lateral sclerosisBTB domainPrimary spinal cord culturesDevelopment of ALSTAR DNA-binding protein 43POZ/BTB proteinDNA-binding protein 43Extracellular glutamate levelsTDP-43 expressionFull-length TDP-43Spinal cord culturesGST pulldown assaysPost-translational modificationsUbiquitinated protein aggregatesCholinergic neuronsGlutamate toxicityCord culturesGlutamate levelsSpinal cord
2007
NAC1, a cocaine‐regulated POZ/BTB protein interacts with CoREST
Korutla L, Degnan R, Wang P, Mackler S. NAC1, a cocaine‐regulated POZ/BTB protein interacts with CoREST. Journal Of Neurochemistry 2007, 101: 611-618. PMID: 17254023, DOI: 10.1111/j.1471-4159.2006.04387.x.Peer-Reviewed Original ResearchConceptsPOZ/BTB proteinPOZ/BTB domainBTB proteinsBTB domainProtein-protein interactionsHEK293T cellsNeuro-2a cellsT cellsTranscriptional regulatorsRepressor proteinRat brain samplesBrain samplesCoRESTCoimmunoprecipitation studiesHomodimer formationHomodimer assemblyRepressor mechanismProtein expressionProteinDirect interactionEndogenous interactionPresent studyPox virus
2005
The POZ/BTB protein NAC1 interacts with two different histone deacetylases in neuronal‐like cultures
Korutla L, Wang P, Mackler S. The POZ/BTB protein NAC1 interacts with two different histone deacetylases in neuronal‐like cultures. Journal Of Neurochemistry 2005, 94: 786-793. PMID: 16033423, DOI: 10.1111/j.1471-4159.2005.03206.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnimals, NewbornBlotting, WesternButyratesCells, CulturedEnzyme InhibitorsGene Expression RegulationHippocampusHistone DeacetylasesHumansHydroxamic AcidsImmunoprecipitationMiceNerve Tissue ProteinsNeuroblastomaNeuronsPlasmidsProtein BindingProtein IsoformsRatsRepressor ProteinsTranscription, GeneticTransfectionTwo-Hybrid System TechniquesConceptsPOZ/BTB proteinProtein-protein interactionsBTB proteinsHistone deacetylasesPOZ domainTwo-hybridGlutathione S-transferase pulldownRecruit histone deacetylasesDifferent histone deacetylasesTranscriptional repressionGST pulldownSNAC1Histone deacetylase inhibitionCorepressorDeacetylasesRepressionDeacetylase inhibitionProteinPulldownHDAC-3NaC1MSin3ANucleus accumbensCNS regionsCoimmunoprecipitation
2002
Differences in expression, actions and cocaine regulation of two isoforms for the brain transcriptional regulator NAC1
Korutla L, Wang P, Lewis D, Neustadter J, Stromberg M, Mackler S. Differences in expression, actions and cocaine regulation of two isoforms for the brain transcriptional regulator NAC1. Neuroscience 2002, 110: 421-429. PMID: 11906783, DOI: 10.1016/s0306-4522(01)00518-8.Peer-Reviewed Original ResearchConceptsBTB/POZ proteinPOZ proteinShort isoformDNA binding domainsPost-transcriptional processingSemi-quantitative reverse transcription-polymerase chain reaction analysisPeripheral tissuesRat brainTranscriptional repressionSubnuclear localizationTranscription-polymerase chain reaction analysisBinding domainsReverse transcription-polymerase chain reaction analysisReporter systemCell cycleCocaine-induced locomotionRat nucleus accumbensWestern blot analysisTranscriptionAmino acidsIsoformsProteinChain reaction analysisBlot analysisNeuronal function
1999
SP‐A as a cytokine: Surfactant protein‐A–regulated transcription of surfactant proteins and other genes
Korutla L, Strayer D. SP‐A as a cytokine: Surfactant protein‐A–regulated transcription of surfactant proteins and other genes. Journal Of Cellular Physiology 1999, 178: 379-386. PMID: 9989784, DOI: 10.1002/(sici)1097-4652(199903)178:3<379::aid-jcp12>3.0.co;2-c.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsCarrier ProteinsCells, CulturedFemaleGene Expression RegulationGenes, fosGenes, junMacrophages, PeritonealProteolipidsPulmonary AlveoliPulmonary Surfactant-Associated Protein APulmonary Surfactant-Associated ProteinsPulmonary SurfactantsRatsRats, Sprague-DawleyRNA, MessengerTranscription, GeneticConceptsType II cellsSurfactant secretionProtein gene transcriptionSurfactant proteinsSurfactant gene expressionOverall transcript levelsC-fos transcriptionSP-A receptorII cellsSP-C mRNA levelsHost antimicrobial defenseSurfactant proteins SPMRNA levelsTranscript stabilityGene transcriptionSP-A effectsTranscript levelsGene expressionTranscriptionC-JunAlveolar type II cellsNew transcriptionSurfactant-associated proteinsSpProtein
1995
Induction of Expression of Interferon-Stimulated Gene Factor-3 (ISGF-3) Proteins by Interferons
Kumar R, Korutla L. Induction of Expression of Interferon-Stimulated Gene Factor-3 (ISGF-3) Proteins by Interferons. Experimental Cell Research 1995, 216: 143-148. PMID: 7529187, DOI: 10.1006/excr.1995.1018.Peer-Reviewed Original ResearchCell NucleusCytosolDNA-Binding ProteinsGene Expression RegulationHumansInterferon Type IInterferon-gammaInterferon-Stimulated Gene Factor 3Interferon-Stimulated Gene Factor 3, gamma SubunitKineticsPhosphorylationPhosphotyrosineRecombinant ProteinsRNA, MessengerTranscription FactorsTumor Cells, CulturedTyrosine
1994
Cell cycle-dependent modulation of alpha-interferon-inducible gene expression and activation of signaling components in Daudi cells.
Kumar R, Korutla L, Zhang K. Cell cycle-dependent modulation of alpha-interferon-inducible gene expression and activation of signaling components in Daudi cells. Journal Of Biological Chemistry 1994, 269: 25437-25441. PMID: 7929242, DOI: 10.1016/s0021-9258(18)47269-9.Peer-Reviewed Original ResearchMeSH Keywords2',5'-Oligoadenylate SynthetaseBase SequenceBurkitt LymphomaCell CycleDNA-Binding ProteinsEnzyme ActivationG1 PhaseGene Expression RegulationHumansInterferon-alphaJanus Kinase 1Molecular Sequence DataProteinsProtein-Tyrosine KinasesS PhaseSignal TransductionSTAT1 Transcription FactorTrans-ActivatorsTumor Cells, CulturedTYK2 KinaseConceptsTyk-2 kinaseJAK-1Synthetase proteinTyrosine phosphorylationGene expressionCell cycle-dependent modulationCell cycleCell cycle-dependent expressionCell cycle-dependent changesInducible gene expressionGene factor 3Unique expression patternCycle-dependent expressionG1/S phaseCell cycle progressionG1/SIFN-inducible gene expressionG2/M.Human Burkitt lymphoma Daudi cellsInduction of expressionG1/S blockG2/MDaudi cellsIFN-alpha-inducible genesCycle-dependent changes