2019
Hypersensitive IFN Responses in Lupus Keratinocytes Reveal Key Mechanistic Determinants in Cutaneous Lupus
Tsoi L, Hile G, Berthier C, Sarkar M, Reed T, Liu J, Uppala R, Patrick M, Raja K, Xing X, Xing E, He K, Gudjonsson J, Kahlenberg J. Hypersensitive IFN Responses in Lupus Keratinocytes Reveal Key Mechanistic Determinants in Cutaneous Lupus. The Journal Of Immunology 2019, 202: 2121-2130. PMID: 30745462, PMCID: PMC6424612, DOI: 10.4049/jimmunol.1800650.Peer-Reviewed Original ResearchConceptsSystemic lupus erythematosusIFN responseFood and Drug Administration-approved therapiesSLE skinSystemic lupus erythematosus patientsSystemic lupus erythematosus susceptibility lociIncreased IFN signaturesSmall interfering RNA knockdownComplex autoimmune diseaseRNA sequencing samplesResponse to IFNTranscription factor PITX1Cutaneous lupusGenes in vitroLupus erythematosusType II IFNTreatment optionsHyperinflammatory responseIFN signatureAutoimmune diseasesSkin inflammationSusceptibility lociIFNRNA knockdownControl keratinocytes
2016
TLR8 Couples SOCS-1 and Restrains TLR7-Mediated Antiviral Immunity, Exacerbating West Nile Virus Infection in Mice
Paul AM, Acharya D, Le L, Wang P, Stokic DS, Leis AA, Alexopoulou L, Town T, Flavell RA, Fikrig E, Bai F. TLR8 Couples SOCS-1 and Restrains TLR7-Mediated Antiviral Immunity, Exacerbating West Nile Virus Infection in Mice. The Journal Of Immunology 2016, 197: 4425-4435. PMID: 27798161, PMCID: PMC5123688, DOI: 10.4049/jimmunol.1600902.Peer-Reviewed Original ResearchConceptsWest Nile virusAntiviral immunityWNV infectionWest Nile virus infectionOverexpression of TLR7Induced IFNsWild-type controlsSuppressor of cytokineTLR7 expressionNeuronal deathVirus infectionHuman TLR7TLR7TLR8InfectionMiceX proteinReduced expressionImmunityNile virusSOCS-1RNA knockdownIFNNovel roleProapoptotic genes
2014
An airway epithelial iNOS–DUOX2–thyroid peroxidase metabolome drives Th1/Th2 nitrative stress in human severe asthma
Voraphani N, Gladwin MT, Contreras AU, Kaminski N, Tedrow JR, Milosevic J, Bleecker ER, Meyers DA, Ray A, Ray P, Erzurum SC, Busse WW, Zhao J, Trudeau JB, Wenzel SE. An airway epithelial iNOS–DUOX2–thyroid peroxidase metabolome drives Th1/Th2 nitrative stress in human severe asthma. Mucosal Immunology 2014, 7: 1175-1185. PMID: 24518246, PMCID: PMC4130801, DOI: 10.1038/mi.2014.6.Peer-Reviewed Original ResearchConceptsInducible nitric oxide synthaseHuman airway epithelial cellsDual oxidase 2Severe asthmaNitrative stressThyroid peroxidaseIL-13Ex vivoSevere refractory asthmaNitric oxide synthaseTh2 cytokine expressionAirway epithelial cellsRefractory asthmaLower interleukinHigher interferonCytokine expressionOxide synthaseOxidase 2AsthmaIFNEpithelial cellsEpithelial cell systemSuperoxide dismutaseRNA knockdownEndogenous peroxidaseAIP1 Mediates Vascular Endothelial Cell Growth Factor Receptor-3–Dependent Angiogenic and Lymphangiogenic Responses
Zhou HJ, Chen X, Huang Q, Liu R, Zhang H, Wang Y, Jin Y, Liang X, Lu L, Xu Z, Min W. AIP1 Mediates Vascular Endothelial Cell Growth Factor Receptor-3–Dependent Angiogenic and Lymphangiogenic Responses. Arteriosclerosis Thrombosis And Vascular Biology 2014, 34: 603-615. PMID: 24407031, PMCID: PMC3952062, DOI: 10.1161/atvbaha.113.303053.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsCarrier ProteinsCells, CulturedCorneaEndocytosisEndothelial CellsEndothelium, VascularEye ProteinsGuanylate KinasesHumansLymphangiogenesisMiceMice, KnockoutMicroRNAsNeuronsras GTPase-Activating ProteinsReceptors, NotchRecombinant ProteinsRetinal NeovascularizationRNA InterferenceRNA, Small InterferingVascular Endothelial Growth Factor CVascular Endothelial Growth Factor Receptor-2Vascular Endothelial Growth Factor Receptor-3ConceptsLymphatic endothelial cellsASK1-interacting protein-1VEGFR-3 signalingHuman lymphatic endothelial cellsVEGFR-3Vascular endothelial cell growth factor receptorEndothelial cellsReduced expressionDevelopmental lymphangiogenesisScaffold proteinAIP1 functionsGrowth factor receptorLymphangiogenic signalingNovel functionVEGFR-2 activityRNA knockdownCell growth factor receptorLymphangiogenic responseSimilar defectsFirst insightProtein 1Vascular endothelial cellsPathological angiogenesisSpecific deletionFactor receptor
2013
Mosquito Saliva Serine Protease Enhances Dissemination of Dengue Virus into the Mammalian Host
Conway MJ, Watson AM, Colpitts TM, Dragovic SM, Li Z, Wang P, Feitosa F, Shepherd DT, Ryman KD, Klimstra WB, Anderson JF, Fikrig E. Mosquito Saliva Serine Protease Enhances Dissemination of Dengue Virus into the Mammalian Host. Journal Of Virology 2013, 88: 164-175. PMID: 24131723, PMCID: PMC3911723, DOI: 10.1128/jvi.02235-13.Peer-Reviewed Original ResearchConceptsDengue virusDENV infectivityAedes aegypti salivaMurine lymph nodesSalivary gland extractsAegypti salivaPrevention of diseaseLymph nodesMosquito salivaDENV loadVivo modelSerine protease activityNovel targetViral attachmentViral infectivityVirus infectivitySerine protease inhibitorHeparan sulfate proteoglycanExtracellular matrix proteinsRNA knockdownProtease inhibitorsInfectivitySulfate proteoglycanCell migrationMammalian hosts
2011
Phosphoproteomic Screen Identifies Potential Therapeutic Targets in Melanoma
Tworkoski K, Singhal G, Szpakowski S, Zito CI, Bacchiocchi A, Muthusamy V, Bosenberg M, Krauthammer M, Halaban R, Stern DF. Phosphoproteomic Screen Identifies Potential Therapeutic Targets in Melanoma. Molecular Cancer Research 2011, 9: 801-812. PMID: 21521745, PMCID: PMC3117976, DOI: 10.1158/1541-7786.mcr-10-0512.Peer-Reviewed Original ResearchMeSH KeywordsApoptosisCell Line, TumorCell MovementCell ProliferationErbB ReceptorsGene Expression Regulation, NeoplasticGene Knockdown TechniquesHEK293 CellsHumansInfant, NewbornMelanocytesMelanomaPhosphoproteinsPhosphorylationProteomicsReceptor Protein-Tyrosine KinasesReceptor, IGF Type 2RNA, Small InterferingSignal TransductionSkin NeoplasmsSTAT3 Transcription FactorConceptsTherapeutic targetReceptor tyrosine kinasesMelanoma cellsPotential therapeutic targetIdentifies potential therapeutic targetsActive receptor tyrosine kinasesTyrosine kinaseMelanoma cell migrationReceptor expressionBreast cancerAxl knockdownAutocrine circuitTherapeutic interventionsCancer subtypesReceptor tyrosine kinase activationTyrosine kinase activationNovel targetActivated receptorsAxlRNA knockdownMelanomaCell migrationHER3KnockdownIGF1R
2008
AIP1 Recruits Phosphatase PP2A to ASK1 in Tumor Necrosis Factor–Induced ASK1-JNK Activation
Min W, Lin Y, Tang S, Yu L, Zhang H, Wan T, Luhn T, Fu H, Chen H. AIP1 Recruits Phosphatase PP2A to ASK1 in Tumor Necrosis Factor–Induced ASK1-JNK Activation. Circulation Research 2008, 102: 840-848. PMID: 18292600, DOI: 10.1161/circresaha.107.168153.Peer-Reviewed Original ResearchConceptsASK1-JNK signalingASK1 dephosphorylationAssociation of PP2APP2A catalytic subunitCatalytic inactive formPP2A inhibitor okadaicASK1-JNK activationC-Jun N-terminal kinaseActivation of JNKEndothelial cellsN-terminal kinasePhosphatase PP2ACritical rolePotential phosphataseProtein phosphataseGAP domainInhibitor okadaicProtein familyCatalytic subunitC2 domainPP2AAIP1Novel memberApoptotic signalingRNA knockdown
2007
RIP1-mediated AIP1 Phosphorylation at a 14-3-3-binding Site Is Critical for Tumor Necrosis Factor-induced ASK1-JNK/p38 Activation*
Zhang R, Zhang H, Lin Y, Li J, Pober JS, Min W. RIP1-mediated AIP1 Phosphorylation at a 14-3-3-binding Site Is Critical for Tumor Necrosis Factor-induced ASK1-JNK/p38 Activation*. Journal Of Biological Chemistry 2007, 282: 14788-14796. PMID: 17389591, DOI: 10.1074/jbc.m701148200.Peer-Reviewed Original ResearchMeSH Keywords14-3-3 ProteinsAdaptor Proteins, Signal TransducingAmino Acid SubstitutionAnimalsApoptosisCarrier ProteinsCattleCells, CulturedEndothelial CellsEnzyme ActivationGuanylate KinasesHumansMAP Kinase Kinase 4MAP Kinase Kinase Kinase 5MAP Kinase Signaling SystemMultiprotein ComplexesMutation, Missensep38 Mitogen-Activated Protein KinasesPhosphorylationProtein BindingProtein Processing, Post-TranslationalProteinsReceptor-Interacting Protein Serine-Threonine KinasesTNF Receptor-Associated Factor 2Tumor Necrosis Factor-alphaConceptsJNK/p38 activationP38 activationTRAF2-ASK1ASK1-JNK activationPhospho-specific antibodiesTNF treatmentEndothelial cellsComplex formationGAP domainProtein familyTerminal domainAIP1Novel memberApoptotic signalingTNF signalingRNA knockdownRIP1PhosphorylationProtein 1ASK1-interacting protein-1EC apoptosisTRAF2ASK1Similar kineticsTumor necrosis factor
2006
Increased ICAM-1 Expression Causes Endothelial Cell Leakiness, Cytoskeletal Reorganization and Junctional Alterations
Clark PR, Manes TD, Pober JS, Kluger MS. Increased ICAM-1 Expression Causes Endothelial Cell Leakiness, Cytoskeletal Reorganization and Junctional Alterations. Journal Of Investigative Dermatology 2006, 127: 762-774. PMID: 17195014, DOI: 10.1038/sj.jid.5700670.Peer-Reviewed Original ResearchConceptsEC barrier functionCell junctionsHuman dermal microvascular ECsSmall-interfering RNA knockdownEC shape changesEndothelial cellsG actin ratioActin cytoskeletonShape changesCytoskeleton organizationCell elongationICAM-1 inductionCytoskeletal reorganizationIntracellular regionCell shapeRNA knockdownHuman dermal microvascular endothelial cellsDermal microvascular endothelial cellsZona occludens-1NF-kappaB activationJunctional alterationsCytoskeletonBarrier functionCell leakinessMicrovascular endothelial cells
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