2016
Mx1 reveals innate pathways to antiviral resistance and lethal influenza disease
Pillai PS, Molony RD, Martinod K, Dong H, Pang IK, Tal MC, Solis AG, Bielecki P, Mohanty S, Trentalange M, Homer RJ, Flavell RA, Wagner DD, Montgomery RR, Shaw AC, Staeheli P, Iwasaki A. Mx1 reveals innate pathways to antiviral resistance and lethal influenza disease. Science 2016, 352: 463-466. PMID: 27102485, PMCID: PMC5465864, DOI: 10.1126/science.aaf3926.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAdultAgedAged, 80 and overAnimalsBacterial InfectionsCaspase 1CaspasesCaspases, InitiatorFemaleHumansImmunity, InnateInfluenza A virusInfluenza, HumanInterferon-betaMaleMembrane GlycoproteinsMiceMonocytesMyxovirus Resistance ProteinsNeutrophilsOrthomyxoviridae InfectionsRespiratory Tract InfectionsToll-Like Receptor 7Viral LoadYoung AdultConceptsBacterial burdenAntiviral resistanceNeutrophil-dependent tissue damageMyD88-dependent signalingAntiviral interferon productionCaspase-1/11IAV diseaseViral loadInfluenza diseaseOlder humansTissue damageInterferon productionInflammasome responseOlder adultsTLR7Vivo consequencesDiseaseMiceIAVBurdenMx geneHumansMonocytesMortalityInfluenzaInterferon-induced guanylate-binding proteins in inflammasome activation and host defense
Kim BH, Chee JD, Bradfield CJ, Park ES, Kumar P, MacMicking JD. Interferon-induced guanylate-binding proteins in inflammasome activation and host defense. Nature Immunology 2016, 17: 481-489. PMID: 27092805, PMCID: PMC4961213, DOI: 10.1038/ni.3440.Peer-Reviewed Original ResearchConceptsGuanylate-binding proteinsMicrobial pathogensInflammasome responseHost defenseProteinInflammasome activationWide varietyPathogensDefense
2015
Suppression of NLRX1 in chronic obstructive pulmonary disease
Kang MJ, Yoon CM, Kim BH, Lee CM, Zhou Y, Sauler M, Homer R, Dhamija A, Boffa D, West AP, Shadel GS, Ting JP, Tedrow JR, Kaminski N, Kim WJ, Lee CG, Oh YM, Elias JA. Suppression of NLRX1 in chronic obstructive pulmonary disease. Journal Of Clinical Investigation 2015, 125: 2458-2462. PMID: 25938787, PMCID: PMC4497738, DOI: 10.1172/jci71747.Peer-Reviewed Original ResearchConceptsChronic obstructive pulmonary diseaseObstructive pulmonary diseaseCigarette smokeAlveolar destructionPulmonary diseaseHuman chronic obstructive pulmonary diseaseExpression of NLRX1Innate immune pathwaysInnate immune responseQuality of lifeCOPD patientsPulmonary functionSubsequent inflammationImmune responseInflammasome activationMurine modelIndependent cohortImmune pathwaysInflammationDisease severityInflammasome responseImportant mediatorCell apoptosisNLRX1Tissue effects
2014
Neue Einblicke in die Pathogenese der Nierensteine
Knauf F. Neue Einblicke in die Pathogenese der Nierensteine. Die Nephrologie 2014, 9: 196-203. DOI: 10.1007/s11560-013-0850-0.Peer-Reviewed Original ResearchRenal stone diseaseStone diseaseMajority of patientsMethodsThis review articleNovel therapeutic agentsPathogenesis of nephrolithiasisSelective literature researchUrine volumeRisk factorsUrine collectionUrine pHCalcium stonesTherapeutic approachesMouse modelStone formationInflammasome responseTherapeutic agentsKidney stonesStone analysisUric acidConcentration of calciumPathogenesisDiseaseReview articleChronic problems
2013
Flagellar Motility Is a Key Determinant of the Magnitude of the Inflammasome Response to Pseudomonas aeruginosa
Patankar YR, Lovewell RR, Poynter ME, Jyot J, Kazmierczak BI, Berwin B. Flagellar Motility Is a Key Determinant of the Magnitude of the Inflammasome Response to Pseudomonas aeruginosa. Infection And Immunity 2013, 81: 2043-2052. PMID: 23529619, PMCID: PMC3676033, DOI: 10.1128/iai.00054-13.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosis Regulatory ProteinsCARD Signaling Adaptor ProteinsCaspase 1Cell DeathCytoskeletal ProteinsDendritic CellsFlagellaGene Expression RegulationInflammasomesInterleukin-1betaMacrophages, PeritonealMiceMice, Inbred C57BLMice, KnockoutMovementPhagocytosisPseudomonas aeruginosaPseudomonas InfectionsConceptsBacterial motilityFlagellar motilityBacterial flagellar motilityInnate immune systemWild-type P. aeruginosaInflammasome activationP. aeruginosaFlagellar expressionIngest bacteriaBone marrow-derived dendritic cellsImmune systemNLRC4 inflammasome activationBacterial associationsCaspase-1 activationBacterial interactionsMarrow-derived dendritic cellsChronic Pseudomonas aeruginosa infectionIL-1β levelsCell surfacePseudomonas aeruginosa infectionIL-1β productionInflammasome responseMotilityDendritic cellsAeruginosa infection
2012
GBP5 Promotes NLRP3 Inflammasome Assembly and Immunity in Mammals
Shenoy AR, Wellington DA, Kumar P, Kassa H, Booth CJ, Cresswell P, MacMicking JD. GBP5 Promotes NLRP3 Inflammasome Assembly and Immunity in Mammals. Science 2012, 336: 481-485. PMID: 22461501, DOI: 10.1126/science.1217141.Peer-Reviewed Original ResearchMeSH KeywordsAlum CompoundsAnimalsApoptosis Regulatory ProteinsCARD Signaling Adaptor ProteinsCarrier ProteinsCaspase 1Cell LineCytoskeletal ProteinsGTP-Binding ProteinsHumansInflammasomesInterferon-gammaInterleukin-1betaLipopolysaccharidesListeria monocytogenesListeriosisMacrophagesMiceNLR Family, Pyrin Domain-Containing 3 ProteinProtein MultimerizationRNA InterferenceSalmonella typhimuriumUric AcidConceptsGuanylate binding protein 5IL-1β/ILImpaired host defensePresence of infectionNLRP3 inflammasome activationCaspase-1 cleavageNLRP3 inflammasome responseNLRP3 inflammasome assemblyInflammasome assemblyBinding protein 5Inflammatory responseInflammasome activationImmune systemTissue damageInflammasome responseHost defenseInflammasome complexCaspase-1Sensory complexProtein 5InflammasomePathogenic bacteriaILInterleukinNLR
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