2019
Thin Skinned: Aged Adipocyte Atrophy Impacts Innate Immunity
Wasko RR, Horsley V. Thin Skinned: Aged Adipocyte Atrophy Impacts Innate Immunity. Trends In Immunology 2019, 40: 175-177. PMID: 30713009, DOI: 10.1016/j.it.2019.01.009.Peer-Reviewed Original Research
2017
Activation of master virulence regulator PhoP in acidic pH requires the Salmonella-specific protein UgtL
Choi J, Groisman EA. Activation of master virulence regulator PhoP in acidic pH requires the Salmonella-specific protein UgtL. Science Signaling 2017, 10 PMID: 28851823, PMCID: PMC5966036, DOI: 10.1126/scisignal.aan6284.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntimicrobial Cationic PeptidesBacterial ProteinsDisease Models, AnimalFemaleGene Expression Regulation, BacterialHydrogen-Ion ConcentrationMagnesiumMembrane ProteinsMiceMice, Inbred BALB CPeptidesPhosphorylationSalmonella InfectionsSalmonella typhimuriumSignal TransductionVirulenceConceptsPhoP activation
2016
Cathelicidin Insufficiency in Patients with Fatal Leptospirosis
Lindow JC, Wunder EA, Popper SJ, Min JN, Mannam P, Srivastava A, Yao Y, Hacker KP, Raddassi K, Lee PJ, Montgomery RR, Shaw AC, Hagan JE, Araújo GC, Nery N, Relman DA, Kim CC, Reis MG, Ko AI. Cathelicidin Insufficiency in Patients with Fatal Leptospirosis. PLOS Pathogens 2016, 12: e1005943. PMID: 27812211, PMCID: PMC5094754, DOI: 10.1371/journal.ppat.1005943.Peer-Reviewed Original ResearchConceptsHost immune responseHigh bacterial loadBacterial loadAcute leptospirosisCase fatalityFatal casesDisease progressionImmune responseHigher systemic bacterial loadsValuable new therapeutic approachPro-inflammatory cytokine receptorsAdaptive immune signaturesSystemic bacterial loadsIndependent risk factorTime of hospitalizationDuration of illnessHigh case fatalityPoor clinical outcomeNew therapeutic approachesBlood transcriptional profilingLimited study sizeFatal leptospirosisLethal leptospirosisRANTES levelsSerum cathelicidinThe role for neutrophil extracellular traps in cystic fibrosis autoimmunity
Skopelja S, Hamilton BJ, Jones JD, Yang ML, Mamula M, Ashare A, Gifford AH, Rigby WF. The role for neutrophil extracellular traps in cystic fibrosis autoimmunity. JCI Insight 2016, 1: e88912. PMID: 27777975, PMCID: PMC5070963, DOI: 10.1172/jci.insight.88912.Peer-Reviewed Original ResearchConceptsAnti-citrullinated protein autoantibodiesNeutrophil extracellular trapsAnti-BPI autoantibodiesDevelopment of autoimmunityCystic fibrosisBactericidal permeability-increasing proteinProtein autoantibodiesExtracellular trapsACPA-positive RA patientsDiminished lung functionRheumatoid arthritis patientsAirway inflammationAutoantibody levelsCF disease severityRA patientsRespiratory failureArthritis patientsLung functionSputum cultureAutoantibody profileLung damagePermeability-increasing proteinAutoantibody specificitiesChronic infectionCF patientsAcidic pH sensing in the bacterial cytoplasm is required for Salmonella virulence
Choi J, Groisman EA. Acidic pH sensing in the bacterial cytoplasm is required for Salmonella virulence. Molecular Microbiology 2016, 101: 1024-1038. PMID: 27282333, PMCID: PMC5015592, DOI: 10.1111/mmi.13439.Peer-Reviewed Original ResearchStructures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition
Gagnon MG, Roy RN, Lomakin IB, Florin T, Mankin AS, Steitz TA. Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition. Nucleic Acids Research 2016, 44: 2439-2450. PMID: 26809677, PMCID: PMC4797290, DOI: 10.1093/nar/gkw018.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesBinding SitesCattleCrystallography, X-RayEscherichia coliInsect ProteinsModels, MolecularMolecular Sequence DataPeptides, CyclicProtein BindingProtein BiosynthesisRibosomesRNA, MessengerRNA, TransferSpecies SpecificityThermus thermophilus
2015
Antimicrobial peptides targeting bacterial ribosome
Lomakin IB, Gagnon MG, Steitz TA. Antimicrobial peptides targeting bacterial ribosome. Oncotarget 2015, 6: 18744-18745. PMID: 26300053, PMCID: PMC4662452, DOI: 10.18632/oncotarget.5114.Peer-Reviewed Original ResearchThe mechanism of inhibition of protein synthesis by the proline-rich peptide oncocin
Roy RN, Lomakin IB, Gagnon MG, Steitz TA. The mechanism of inhibition of protein synthesis by the proline-rich peptide oncocin. Nature Structural & Molecular Biology 2015, 22: 466-469. PMID: 25984972, PMCID: PMC4456192, DOI: 10.1038/nsmb.3031.Peer-Reviewed Original ResearchAntimicrobial Cationic PeptidesCrystallography, X-RayModels, MolecularProtein ConformationProtein Synthesis InhibitorsRibosomesThermus thermophilusAntimicrobial peptide resistance mediates resilience of prominent gut commensals during inflammation
Cullen TW, Schofield WB, Barry NA, Putnam EE, Rundell EA, Trent MS, Degnan PH, Booth CJ, Yu H, Goodman AL. Antimicrobial peptide resistance mediates resilience of prominent gut commensals during inflammation. Science 2015, 347: 170-175. PMID: 25574022, PMCID: PMC4388331, DOI: 10.1126/science.1260580.Peer-Reviewed Original Research
2013
Signal‐specific temporal response by the Salmonella PhoP/PhoQ regulatory system
Park S, Groisman EA. Signal‐specific temporal response by the Salmonella PhoP/PhoQ regulatory system. Molecular Microbiology 2013, 91: 135-144. PMID: 24256574, PMCID: PMC3890429, DOI: 10.1111/mmi.12449.Peer-Reviewed Original ResearchConceptsTransporter MgtATwo-component systems PhoP/PhoQPhoP-dependent genesAntimicrobial peptide C18G.PhoP/PhoQSalmonella enterica serovar TyphimuriumSensor PhoQEnterica serovar TyphimuriumVirulence functionsRepressing signalsGene setsPhoQMgtAGenesSerovar TyphimuriumElicit expressionPeriplasmPhoPActive formFull transcriptionExpressionPhoQ.TranscriptionCytoplasmicProteinRegulation of systemic iron homeostasis
Finberg KE. Regulation of systemic iron homeostasis. Current Opinion In Hematology 2013, 20: 208-214. PMID: 23426198, DOI: 10.1097/moh.0b013e32835f5a47.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsMeSH KeywordsAntimicrobial Cationic PeptidesBone Morphogenetic ProteinsErythropoiesisHepcidinsHomeostasisHumansIronIron Metabolism DisordersIron, DietarySignal TransductionConceptsSystemic iron balanceMolecular mechanismsBone morphogenetic protein (BMP) type IHypoxia-inducible factor (HIF) pathwayInducible factor pathwayProtein type IHepcidin synthesisIron balanceBMP pathwayTransferrin receptor 2Systemic iron homeostasisCapacity of erythropoietinIron homeostasisComplex biologyNonredundant roleTissue culture systemHepcidin levelsInfectious stimuliIron storesFactor pathwayDietary ironErythropoietic activityReceptor 2PathwayAnimal models
2012
Local Delivery of Gene-Modifying Triplex-Forming Molecules to the Epidermis
Rogers FA, Hu RH, Milstone LM. Local Delivery of Gene-Modifying Triplex-Forming Molecules to the Epidermis. Journal Of Investigative Dermatology 2012, 133: 685-691. PMID: 23014335, PMCID: PMC3532560, DOI: 10.1038/jid.2012.351.Peer-Reviewed Original ResearchConceptsIntradermal deliveryHairless miceTransgenic miceBasal keratinocytesMethod of deliveryNuclei of keratinocytesIntraperitoneal administrationSitu gene correctionBack skinLocal deliveryMiceDisease-causing genesEpidermal keratinocytesKeratinocytesLocal administrationAdministrationDeliverySkinEpidermisDaysIxodes scapularis JAK-STAT Pathway Regulates Tick Antimicrobial Peptides, Thereby Controlling the Agent of Human Granulocytic Anaplasmosis
Liu L, Dai J, Zhao YO, Narasimhan S, Yang Y, Zhang L, Fikrig E. Ixodes scapularis JAK-STAT Pathway Regulates Tick Antimicrobial Peptides, Thereby Controlling the Agent of Human Granulocytic Anaplasmosis. The Journal Of Infectious Diseases 2012, 206: 1233-1241. PMID: 22859824, PMCID: PMC3448968, DOI: 10.1093/infdis/jis484.Peer-Reviewed Original ResearchConceptsJAK-STAT pathwayTick salivary glandsA. phagocytophilum infectionAntimicrobial peptidesElectrophoretic mobility shift assaysPeptide-encoding genesMobility shift assaysPhagocytophilum infectionHuman granulocytic anaplasmosisGene familyTransducer activatorMammalian hostsRNA interferenceShift assaysTranscription pathwayGene expressionJAK-STATJanus kinaseGranulocytic anaplasmosisSalivary glandsPathwayGenesCritical roleAnaplasma phagocytophilumKey roleImpact of epidermal desquamation on tissue stores of iron
Milstone LM, Hu RH, Dziura JD, Zhou J. Impact of epidermal desquamation on tissue stores of iron. Journal Of Dermatological Science 2012, 67: 9-14. PMID: 22575277, PMCID: PMC3374011, DOI: 10.1016/j.jdermsci.2012.04.003.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntimicrobial Cationic PeptidesCell ProliferationDisease Models, AnimalEpidermisFemaleGene Expression RegulationHemochromatosisHemochromatosis ProteinHepcidinsHistocompatibility Antigens Class IHomeostasisHuman papillomavirus 16HumansIronKidneyLiverMaleMembrane ProteinsMiceMice, 129 StrainMice, Inbred C57BLMice, KnockoutMice, TransgenicPapillomavirus InfectionsReceptors, TransferrinConceptsIron metabolismDifferent mouse modelsSignificant reductionHPV16 E7 geneSystemic iron metabolismSystemic proteinsIron statusMouse modelTissue storesE7 genesSystemic levelsEpidermal turnoverInternal organsEpidermal desquamationTransferrin receptorMetabolic studiesKnockout modelsCorneocyte desquamationDesquamationKidneyHuman skinEpidermal homeostasisMetabolismEpidermisSkin
2011
Unraveling Mechanisms Regulating Systemic Iron Homeostasis
Finberg KE. Unraveling Mechanisms Regulating Systemic Iron Homeostasis. Hematology 2011, 2011: 532-537. PMID: 22160085, PMCID: PMC3648641, DOI: 10.1182/asheducation-2011.1.532.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsMeSH KeywordsAntimicrobial Cationic PeptidesErythropoiesisHepcidinsHomeostasisHumansInflammationIronModels, BiologicalConceptsSystemic iron homeostasisIron homeostasisProduction of hepcidinSystemic iron balanceHepcidin levelsRed blood cellsIron overloadDietary ironErythropoietic activityHepcidin responseAnimal modelsIron balanceIron disordersIron deficiencyBlood cellsHepcidinPhysiological stimuliDeleterious effectsLiverIron loadingHomeostasisTissue culture systemMolecular mechanismsKey regulatorAvailability of ironTmprss6 is a genetic modifier of the Hfe-hemochromatosis phenotype in mice
Finberg KE, Whittlesey RL, Andrews NC. Tmprss6 is a genetic modifier of the Hfe-hemochromatosis phenotype in mice. Blood 2011, 117: 4590-4599. PMID: 21355094, PMCID: PMC3099575, DOI: 10.1182/blood-2010-10-315507.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntimicrobial Cationic PeptidesFemaleGenotypeHemochromatosisHemochromatosis ProteinHepcidinsHeterozygoteHistocompatibility Antigens Class IHomozygoteHumansIronLiverMaleMembrane ProteinsMiceMice, Inbred C57BLMice, TransgenicPhenotypeSerine EndopeptidasesSignal TransductionUp-RegulationConceptsBMP/SmadBone morphogenetic proteinSystemic iron deficiencyGenetic lossHereditary hemochromatosis protein HFENatural genetic variationHemochromatosis protein HFEIron deficiencySmad target genesIron deficiency anemiaSystemic iron overloadElevated hepatic expressionExpression of hepcidinIron-refractory iron deficiency anemiaTransmembrane serine proteaseDietary iron absorptionSystemic iron homeostasisGenetic variationGenetic approachesTarget genesMacrophage iron releaseHepcidin elevationMorphogenetic proteinsDeficiency anemiaHepcidin production
2010
Down-regulation of Bmp/Smad signaling by Tmprss6 is required for maintenance of systemic iron homeostasis
Finberg KE, Whittlesey RL, Fleming MD, Andrews NC. Down-regulation of Bmp/Smad signaling by Tmprss6 is required for maintenance of systemic iron homeostasis. Blood 2010, 115: 3817-3826. PMID: 20200349, PMCID: PMC2865872, DOI: 10.1182/blood-2009-05-224808.Peer-Reviewed Original ResearchMeSH KeywordsAnemia, Iron-DeficiencyAnimalsAntimicrobial Cationic PeptidesBlotting, WesternBone Morphogenetic ProteinsDown-RegulationFemaleGPI-Linked ProteinsHemochromatosis ProteinHepatocytesHepcidinsHomeostasisInhibitor of Differentiation Protein 1IronLiverMembrane ProteinsMiceMice, Inbred C57BLMice, KnockoutReverse Transcriptase Polymerase Chain ReactionRNA, MessengerSerine EndopeptidasesSignal TransductionSmad ProteinsConceptsIron deficiency anemiaSystemic iron homeostasisHepcidin expressionSmad signalingIntravenous iron therapyOral iron treatmentSystemic iron overloadIron regulatory hormone hepcidinBMP/Smad signalingBmp6 mRNA levelsSmad Signaling PathwayIron homeostasisIron therapyIron storesDeficiency anemiaIron overloadHepatic levelsType II transmembrane serine proteaseIRIDA patientsTransmembrane serine proteaseFamilial disorderHormone hepcidinIron treatmentHepcidin transcriptionMice
2009
Iron-Refractory Iron Deficiency Anemia
Finberg KE. Iron-Refractory Iron Deficiency Anemia. Seminars In Hematology 2009, 46: 378-386. PMID: 19786206, DOI: 10.1053/j.seminhematol.2009.06.006.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsMeSH KeywordsAdministration, OralAnemia, Iron-DeficiencyAnemia, RefractoryAntimicrobial Cationic PeptidesChildChild, PreschoolFemaleGPI-Linked ProteinsHematinicsHemochromatosis ProteinHepcidinsHumansInfantInfusions, ParenteralIronIron CompoundsLiverMaleMembrane ProteinsMutationSerine EndopeptidasesTreatment FailureUp-RegulationConceptsIron-refractory iron deficiency anemiaIron deficiency anemiaDeficiency anemiaOral iron treatmentParenteral iron therapyAutosomal recessive disorderIron therapyClinical presentationRecent studiesHepcidin expressionIron absorptionIRIDA patientsTransmembrane serine proteaseIron treatmentAnemiaElevated levelsRecessive disorderHepcidinLiverDisordersTMPRSS6Serine proteases
2008
Molecular Basis for Proline- and Arginine-Rich Peptide Inhibition of Proteasome
Anbanandam A, Albarado DC, Tirziu DC, Simons M, Veeraraghavan S. Molecular Basis for Proline- and Arginine-Rich Peptide Inhibition of Proteasome. Journal Of Molecular Biology 2008, 384: 219-227. PMID: 18823992, PMCID: PMC2632303, DOI: 10.1016/j.jmb.2008.09.021.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntimicrobial Cationic PeptidesCells, CulturedChymotrypsinEndothelial CellsGene Expression RegulationHumansHydrophobic and Hydrophilic InteractionsMagnetic Resonance SpectroscopyMolecular Sequence DataMutant ProteinsNF-kappa BProteasome InhibitorsTumor Necrosis Factor-alphaVascular Cell Adhesion Molecule-1
2007
Protection against myocardial ischemia-reperfusion injury by the angiogenic Masterswitch protein PR 39 gene therapy: the roles of HIF1alpha stabilization and FGFR1 signaling.
Muinck ED, Nagy N, Tirziu D, Murakami M, Gurusamy N, Goswami SK, Ghatpande S, Engelman RM, Simons M, Das DK. Protection against myocardial ischemia-reperfusion injury by the angiogenic Masterswitch protein PR 39 gene therapy: the roles of HIF1alpha stabilization and FGFR1 signaling. Antioxidants And Redox Signaling 2007, 9: 437-45. PMID: 17280485, DOI: 10.1089/ars.2006.1501.Peer-Reviewed Original ResearchMeSH KeywordsAdenoviridaeAnimalsAntimicrobial Cationic PeptidesApoptosisBlotting, WesternCell LineGenetic TherapyHumansHypoxia-Inducible Factor 1, alpha SubunitIn Situ Nick-End LabelingMaleMalondialdehydeMiceMice, Inbred C57BLMutationMyocardial Reperfusion InjuryReactive Oxygen SpeciesReceptor, Fibroblast Growth Factor, Type 1Signal TransductionTime FactorsConceptsCoronary flowMyocardial ischemic reperfusion injuryMyocardial ischemia-reperfusion injuryEmpty vectorIschemia-reperfusion injuryIschemic reperfusion injuryLVdP/dtVentricular developed pressureMin of ischemiaBaseline coronary flowMyocardial infarct sizeGene therapyReperfusion injuryCardioprotective abilityInfarct sizeDeveloped pressureHIF-1alpha proteinTTC stainingAortic flowHeart rateCardiomyocyte apoptosisEx vivoCardioprotectionHIF1alpha stabilizationHemodynamics
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