2016
Mood stabilizers inhibit cytomegalovirus infection
Ornaghi S, Davis JN, Gorres KL, Miller G, Paidas MJ, van den Pol AN. Mood stabilizers inhibit cytomegalovirus infection. Virology 2016, 499: 121-135. PMID: 27657833, PMCID: PMC5102808, DOI: 10.1016/j.virol.2016.09.012.Peer-Reviewed Original ResearchConceptsCytomegalovirus infectionAvailable anti-CMV drugsAnti-CMV drugsCommon infectious causeCongenital birth defectsInfected newbornsFetal exposureInfectious causesInfected fetusesMood stabilizersMouse CMVMood disordersImmunocompromised individualsPsychiatric disordersBody weightViral resistanceHuman CMVDevelopmental maturationBirth defectsSpecific inhibitionCMVInfectionValnoctamideDisordersDrugs
2010
Biology and Therapeutic Targeting of Sp1 Transactivation In Myeloma
Fulciniti M, Amin S, Nanjappa P, Rodig S, Hideshima T, Pal J, Mohan V, Lee K, Shammas M, Minvielle S, Prabhala R, Avet-Loiseau H, Cheng L, Anderson K, Munshi N. Biology and Therapeutic Targeting of Sp1 Transactivation In Myeloma. Blood 2010, 116: 134. DOI: 10.1182/blood.v116.21.134.134.Peer-Reviewed Original ResearchSp1 activityTranscription factorsCell growthApoptotic pathwayOverexpression of Sp1Role of Sp1GC-rich motifsGene expression profilesMitochondrial apoptotic pathwayPathway inhibitor U0126ERK pathway inhibitor U0126Important regulatory roleSpecific inhibitionSp1 transactivationMAPK genesSp1 siRNAMM cell growthSp1 activationMM cellsCellular processesNuclear localizationDNA bindingSp1Transcriptional activityPromoter activityFunctional Studies of Plasmodium falciparum Dipeptidyl Aminopeptidase I Using Small Molecule Inhibitors and Active Site Probes
Deu E, Leyva MJ, Albrow VE, Rice MJ, Ellman JA, Bogyo M. Functional Studies of Plasmodium falciparum Dipeptidyl Aminopeptidase I Using Small Molecule Inhibitors and Active Site Probes. Cell Chemical Biology 2010, 17: 808-819. PMID: 20797610, PMCID: PMC2929396, DOI: 10.1016/j.chembiol.2010.06.007.Peer-Reviewed Original ResearchConceptsDipeptidyl aminopeptidasesActivity-based probesSmall molecules resultsNew targetsSmall molecule inhibitorsDipeptidyl aminopeptidase IActive site probesValuable new targetsAminopeptidase IAntimalarial targetImmature trophozoitesMolecule inhibitorsFunctional studiesCovalent inhibitorsParasite growthMalaria parasitesHemoglobin degradationSite probesLow nanomolar concentrationsSpecific inhibitionPlasmodium falciparumNanomolar concentrationsWidespread resistanceInhibitionTarget
2008
Hypothalamic Fatty Acid Metabolism Mediates the Orexigenic Action of Ghrelin
López M, Lage R, Saha AK, Pérez-Tilve D, Vázquez MJ, Varela L, Sangiao-Alvarellos S, Tovar S, Raghay K, Rodríguez-Cuenca S, Deoliveira RM, Castañeda T, Datta R, Dong JZ, Culler M, Sleeman MW, Álvarez C, Gallego R, Lelliott CJ, Carling D, Tschöp MH, Diéguez C, Vidal-Puig A. Hypothalamic Fatty Acid Metabolism Mediates the Orexigenic Action of Ghrelin. Cell Metabolism 2008, 7: 389-399. PMID: 18460330, DOI: 10.1016/j.cmet.2008.03.006.Peer-Reviewed Original ResearchMeSH KeywordsAMP-Activated Protein Kinase KinasesAnimalsBlotting, WesternCarnitine O-Palmitoyltransferasefas ReceptorFastingFatty Acid SynthasesFatty AcidsFeeding BehaviorGhrelinHypothalamusIn Situ HybridizationLeptinMaleMalonyl Coenzyme AMiceMice, Inbred C57BLMice, KnockoutMice, ObesePhosphorylationProtein KinasesRatsRats, Sprague-DawleyConceptsHypothalamic fatty acid metabolismFatty acid metabolismFatty acid synthaseAcid metabolismCarnitine palmitoyltransferase 1 activityFatty acid biosynthesisRegion-specific mannerGhrelin's effectsOrexigenic responseHypothalamic levelOrexigenic actionVentromedial nucleusFood intakeCurrent evidenceFAS expressionGhrelinAcid biosynthesisRelevant regulatory systemGenetic approachesProtein kinaseAMPK activityAcid synthaseSpecific inhibitionRegulatory systemPhysiological mechanisms
2002
Cyclooxygenase 2 activity modulates the severity of murine Lyme arthritis
Anguita J, Samanta S, Ananthanarayanan SK, Revilla B, Geba GP, Barthold SW, Fikrig E. Cyclooxygenase 2 activity modulates the severity of murine Lyme arthritis. Pathogens And Disease 2002, 34: 187-191. PMID: 12423770, PMCID: PMC4307933, DOI: 10.1111/j.1574-695x.2002.tb00623.x.Peer-Reviewed Original ResearchConceptsJoint inflammationCOX-2B. burgdorferi-specific antibodyBurgdorferi-specific antibodiesOnset of arthritisDegree of inflammationNoninfectious inflammatory diseasesCyclooxygenase-2 activityCOX-2 activityB. burgdorferiCOX-2 gene expressionMurine Lyme arthritisSpecific inhibitionLyme arthritisCytokine responsesInfectious arthritisRheumatoid arthritisInfected miceInflammatory diseasesInducible isoformMurine jointsArthritisInflammationMRNA expressionLyme disease
1987
Serodiagnostic assay for visceral leishmaniasis employing monoclonal antibodies
Jaffe C, McMahon-Pratt D. Serodiagnostic assay for visceral leishmaniasis employing monoclonal antibodies. Transactions Of The Royal Society Of Tropical Medicine And Hygiene 1987, 81: 587-594. PMID: 3445339, DOI: 10.1016/0035-9203(87)90418-4.Peer-Reviewed Original ResearchConceptsVisceral leishmaniasisMonoclonal antibodiesSerodiagnostic assaysVL seraParasite antigensChagas diseaseSystemic lupus erythematosusNon-endemic areasDifferent parasite antigensLeishmania antigenLupus erythematosusMucocutaneous leishmaniasisLepromatous leprosyNegative control seraPositive casesSpecies-specific monoclonal antibodiesNormal serumControl seraRapid diagnosisAntigenSerum dilutionSerumAntibodiesLeishmaniasisSpecific inhibition
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