2022
Metformin, phenformin, and galegine inhibit complex IV activity and reduce glycerol-derived gluconeogenesis
LaMoia TE, Butrico GM, Kalpage HA, Goedeke L, Hubbard BT, Vatner DF, Gaspar RC, Zhang XM, Cline GW, Nakahara K, Woo S, Shimada A, Hüttemann M, Shulman GI. Metformin, phenformin, and galegine inhibit complex IV activity and reduce glycerol-derived gluconeogenesis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2122287119. PMID: 35238637, PMCID: PMC8916010, DOI: 10.1073/pnas.2122287119.Peer-Reviewed Original ResearchConceptsGlucose-lowering effectPlasma glucose concentrationComplex I activityHepatic gluconeogenesisType 2 diabetes mellitusGlucose concentrationGlycerol-3-phosphate dehydrogenase activityI activityDiabetes mellitusSelective inhibitionMetforminInhibitionRelevant concentrationsGluconeogenesisPhenforminVivoMost studiesDehydrogenase activityGalegineMellitus
2021
Low-dose Aspirin prevents hypertension and cardiac fibrosis when thromboxane A2 is unrestrained
D'Agostino I, Tacconelli S, Bruno A, Contursi A, Mucci L, Hu X, Xie Y, Chakraborty R, Jain K, Sacco A, Zucchelli M, Landolfi R, Dovizio M, Falcone L, Ballerini P, Hwa J, Patrignani P. Low-dose Aspirin prevents hypertension and cardiac fibrosis when thromboxane A2 is unrestrained. Pharmacological Research 2021, 170: 105744. PMID: 34182131, DOI: 10.1016/j.phrs.2021.105744.Peer-Reviewed Original ResearchMeSH KeywordsAdultAnimalsAntifibrotic AgentsAntihypertensive AgentsAspirinBiomarkersBlood PlateletsBlood PressureCardiomyopathiesCase-Control StudiesCells, CulturedDisease Models, AnimalEssential HypertensionFemaleFibrosisHumansMaleMice, Inbred C57BLMice, KnockoutMiddle AgedMyocytes, CardiacMyofibroblastsPlatelet Aggregation InhibitorsReceptors, EpoprostenolReceptors, ThromboxaneThromboxane A2ConceptsProfibrotic gene expressionEnhanced blood pressureBlood pressureCardiac fibrosisPlatelet TXAHypertensive patientsOverload-induced cardiac fibrosisLow-dose aspirin administrationEarly cardiac fibrosisPlatelet-derived thromboxaneLow-dose aspirinEssential hypertensive patientsEssential hypertension patientsHigh-salt dietSalt-sensitive hypertensionCardiac collagen depositionNumber of myofibroblastsSelective inhibitionGene expressionPrevents hypertensionTP overexpressionUrinary TXMAspirin administrationHypertensive miceAspirin treatment
2013
The Angelman Syndrome Protein Ube3a Is Required for Polarized Dendrite Morphogenesis in Pyramidal Neurons
Miao S, Chen R, Ye J, Tan G, Li S, Zhang J, Jiang Y, Xiong Z. The Angelman Syndrome Protein Ube3a Is Required for Polarized Dendrite Morphogenesis in Pyramidal Neurons. Journal Of Neuroscience 2013, 33: 327-333. PMID: 23283345, PMCID: PMC6618628, DOI: 10.1523/jneurosci.2509-12.2013.Peer-Reviewed Original ResearchConceptsPyramidal neuronsApical dendritesLong apical dendritesNeuron dendritic arborsDendrite outgrowthUbiquitin protein ligase E3ANovel pathological mechanismBasal dendritesCorticospinal tractDendritic arborsMouse modelPathological mechanismsMammalian prefrontal cortexExcitatory cellsPrefrontal cortexNeuronsDendrite morphogenesisCellular mechanismsDendritic morphologySelective inhibitionUBE3AMiceDendritesMolecular mechanismsDownregulation
2012
Prefrontal D1 dopamine signaling is required for temporal control
Narayanan NS, Land BB, Solder JE, Deisseroth K, DiLeone RJ. Prefrontal D1 dopamine signaling is required for temporal control. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: 20726-20731. PMID: 23185016, PMCID: PMC3528521, DOI: 10.1073/pnas.1211258109.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceBehavior, AnimalBiological ClocksMaleMiceMice, TransgenicModels, NeurologicalNeural PathwaysOptogeneticsPrefrontal CortexRatsReceptors, Dopamine D1RewardRNA InterferenceRNA, Small InterferingSignal TransductionSynaptic TransmissionTime FactorsTyrosine 3-MonooxygenaseVentral Tegmental AreaConceptsVentral tegmental areaD1 dopamine receptorsDopamine receptorsTegmental areaDopaminergic projectionsPrefrontal neuronsMidbrain ventral tegmental areaD2 dopamine receptorsDopaminergic inputD1 receptorsDopaminergic neurotransmissionD1 dopamineDopaminergic diseasesTyrosine hydroxylaseDopamine signalingReceptorsPharmacological disruptionSelective inhibitionGoal-directed behaviorNeuronsRNA interferenceTiming taskBehavioral goalsControlNeurotransmission
2011
Erythrocyte peripheral type benzodiazepine receptor/voltage-dependent anion channels are upregulated by Plasmodium falciparum
Bouyer G, Cueff A, Egée S, Kmiecik J, Maksimova Y, Glogowska E, Gallagher PG, Thomas SL. Erythrocyte peripheral type benzodiazepine receptor/voltage-dependent anion channels are upregulated by Plasmodium falciparum. Blood 2011, 118: 2305-2312. PMID: 21795748, DOI: 10.1182/blood-2011-01-329300.Peer-Reviewed Original ResearchConceptsPeripheral-type benzodiazepine receptorBenzodiazepine receptorsNew permeability pathwaysP falciparumPlasmodium falciparumFalciparum-infected erythrocytesAnti-malarial therapyP falciparum-infected erythrocytesErythrocyte membranesInfected erythrocytesAnion channelIntraerythrocytic growthFalciparumReceptorsSelective inhibitionEndogenous channelsVoltage-dependent anion channelPharmacologic applicationsPermeability pathwaysErythrocytesMolecular identityObvious targetTherapy
2009
Taste Coding after Selective Inhibition by Chlorhexidine
Wang M, Marks L, Frank M. Taste Coding after Selective Inhibition by Chlorhexidine. Chemical Senses 2009, 34: 653-666. PMID: 19703921, PMCID: PMC2745350, DOI: 10.1093/chemse/bjp047.Peer-Reviewed Original ResearchConceptsTaste of NaClMM chlorhexidineChlorhexidine gluconatePrototypic stimulusMultiple receptorsChlorhexidineBitter stimuliQuinine tastesGustatory systemSalt tasteQuinine hydrochlorideSelective inhibitionTaste codingQuininePartial inhibitionTreatmentSalty tasteStimuliInhibitionMultiple stimuliAcid taste
2007
Single-Nucleotide-Specific siRNA Targeting in a Dominant-Negative Skin Model
Hickerson RP, Smith FJ, Reeves RE, Contag CH, Leake D, Leachman SA, Milstone LM, McLean WH, Kaspar RL. Single-Nucleotide-Specific siRNA Targeting in a Dominant-Negative Skin Model. Journal Of Investigative Dermatology 2007, 128: 594-605. PMID: 17914454, DOI: 10.1038/sj.jid.5701060.Peer-Reviewed Original ResearchConceptsWild-type gene expressionBicistronic reporter constructFilament formationDominant-negative genetic disordersNumerous genetic disordersGenetic disordersKeratin filament formationRNA interferenceMutant formsReporter constructsGene expressionMutant mRNAFluorescent reportersMutant allelesCell culture modelSiRNAsSimultaneous expressionK6aK mutationPachyonychia congenitaExpressionCulture modelHuman keratinocytesSiRNASelective inhibition
2003
Selective inhibition of tumor microvascular permeability by cavtratin blocks tumor progression in mice
Gratton J, Lin MI, Yu J, Weiss ED, Jiang ZL, Fairchild TA, Iwakiri Y, Groszmann R, Claffey KP, Cheng Y, Sessa WC. Selective inhibition of tumor microvascular permeability by cavtratin blocks tumor progression in mice. Cancer Cell 2003, 4: 31-39. PMID: 12892711, DOI: 10.1016/s1535-6108(03)00168-5.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCapillary PermeabilityCarcinoma, HepatocellularCarcinoma, Lewis LungCaveolin 1CaveolinsDisease ProgressionEndothelium, VascularEnzyme InhibitorsLiver Neoplasms, ExperimentalLung NeoplasmsMaleMiceMice, Inbred C57BLMice, KnockoutMice, NudeNeovascularization, PhysiologicNitric Oxide SynthaseNitric Oxide Synthase Type IINitric Oxide Synthase Type IIIPeptide FragmentsVascular Endothelial Growth Factor AConceptsEndothelial nitric oxide synthaseTumor progressionAntitumor actionDelays tumor progressionENOS knockout miceNitric oxide synthaseTumor blood vesselsTumor microvascular permeabilityOxide synthaseMicrovascular permeabilityKnockout miceAntiangiogenic effectsTumor vasculatureCell-permeable peptideMicrovascular hyperpermeabilityNovel targetNormal vasculatureHyperpermeabilityBlood vesselsCavtratinAntitumor therapyProgressionMiceSelective inhibitionVasculature
2001
The C-terminal domain of thrombospondin-1 induces vascular smooth muscle cell chemotaxis
Nesselroth S, Willis A, Fuse S, Olson E, Lawler J, Sumpio B, Gahtan V. The C-terminal domain of thrombospondin-1 induces vascular smooth muscle cell chemotaxis. Journal Of Vascular Surgery 2001, 33: 595-600. PMID: 11241132, DOI: 10.1067/mva.2001.112318.Peer-Reviewed Original ResearchConceptsVascular smooth muscle cellsVSMC chemotaxisThrombospondin-1VSMC migrationAortic vascular smooth muscle cellsTop wellsAcute phase reactantsBoyden chamber chemotaxisSmooth muscle cellsSmooth muscle cell chemotaxisVascular diseaseVascular lesionsVascular smooth muscle cell chemotaxisSerum-free mediumMuscle cellsTSP-1 moleculeCell chemotaxisChemotaxis assaysBottom wellsAntibodiesSelective inhibitionT-test
2000
Interferon γ Induction of Pulmonary Emphysema in the Adult Murine Lung
Wang Z, Zheng T, Zhu Z, Homer R, Riese R, Chapman H, Shapiro S, Elias J. Interferon γ Induction of Pulmonary Emphysema in the Adult Murine Lung. Journal Of Experimental Medicine 2000, 192: 1587-1600. PMID: 11104801, PMCID: PMC2193095, DOI: 10.1084/jem.192.11.1587.Peer-Reviewed Original ResearchConceptsAdult murine lungMurine lungProtease/antiprotease balanceChronic obstructive pulmonary diseaseSecretory leukocyte proteinase inhibitorNeutrophil-rich inflammationObstructive pulmonary diseaseInterferon γ inductionPulmonary diseasePulmonary complianceChronic inflammationInflammatory responseLung volumePulmonary emphysemaPulmonary tissueΓ inductionAlveolar enlargementMMP-9Matrix metalloproteinaseEmphysemaLungInflammationSelective inhibitionProminent proteaseMacrophagesIn vivo delivery of the caveolin-1 scaffolding domain inhibits nitric oxide synthesis and reduces inflammation
Bucci M, Gratton J, Rudic R, Acevedo L, Roviezzo F, Cirino G, Sessa W. In vivo delivery of the caveolin-1 scaffolding domain inhibits nitric oxide synthesis and reduces inflammation. Nature Medicine 2000, 6: 1362-1367. PMID: 11100121, DOI: 10.1038/82176.Peer-Reviewed Original ResearchConceptsCaveolin-1Signal transductionSmall-molecule mimicryCaveolae assemblyInternalization sequenceCoat proteinEndothelial cellsPhysiological importanceEndothelial nitric oxide synthase (eNOS) inhibitorTransductionCholesterol transportNitric oxide synthase inhibitorChimeric peptideInhibits nitric oxide synthesisOxide synthase inhibitorNitric oxide synthesisNew therapeutic approachesNitric oxide productionSelective inhibitionDomainPeptidesCaveolinAcute inflammationCellsSystemic administrationSelective Inhibition of NF-κB Activation by a Peptide That Blocks the Interaction of NEMO with the IκB Kinase Complex
May M, D'Acquisto F, Madge L, Glöckner J, Pober J, Ghosh S. Selective Inhibition of NF-κB Activation by a Peptide That Blocks the Interaction of NEMO with the IκB Kinase Complex. Science 2000, 289: 1550-1554. PMID: 10968790, DOI: 10.1126/science.289.5484.1550.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAnti-Inflammatory Agents, Non-SteroidalCells, CulturedCOS CellsE-SelectinEndothelium, VascularGene Expression RegulationHeLa CellsHumansI-kappa B KinaseInflammationMiceMice, Inbred C57BLMolecular Sequence DataMutationNF-kappa BPeptidesPoint MutationProtein Serine-Threonine KinasesProtein Structure, TertiaryRecombinant Fusion ProteinsConceptsNF-kappaBBasal NF-kappaB activityExperimental mouse modelTranscription factor nuclear factorCytokine-induced NF-kappaB activationCell-permeable NBD peptideInhibitor of kappaBNF-κB activationNF-kappaB activityNF-kappaB activationAssociation of NEMOIKK complexAcute inflammationDevelopment of drugsProinflammatory activationInflammatory responseNBD peptideMouse modelProinflammatory stimuliIκB kinase (IKK) complexNuclear factorRegulatory protein NEMOInflammationSelective inhibitionExpression of genesThe Selective Proteasome Inhibitors Lactacystin and Epoxomicin Can Be Used to Either Up- or Down-Regulate Antigen Presentation at Nontoxic Doses
Schwarz K, de Giuli R, Schmidtke G, Kostka S, van den Broek M, Kim K, Crews C, Kraft R, Groettrup M. The Selective Proteasome Inhibitors Lactacystin and Epoxomicin Can Be Used to Either Up- or Down-Regulate Antigen Presentation at Nontoxic Doses. The Journal Of Immunology 2000, 164: 6147-6157. PMID: 10843664, PMCID: PMC2507740, DOI: 10.4049/jimmunol.164.12.6147.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcysteineAmino Acid SequenceAnimalsAntigen PresentationAntigens, ViralApoptosisCell DivisionCell LineCysteine EndopeptidasesCysteine Proteinase InhibitorsDose-Response Relationship, ImmunologicDown-RegulationGlycoproteinsHumansHybridomasHydrolysisLymphocyte ActivationLymphocytic choriomeningitis virusMiceMice, Inbred BALB CMice, Inbred C57BLMolecular Sequence DataMultienzyme ComplexesNucleoproteinsOligopeptidesPeptide FragmentsProteasome Endopeptidase ComplexT-Lymphocytes, CytotoxicTumor Cells, CulturedUbiquitinsUp-RegulationViral ProteinsConceptsAg presentationProteasome inhibitor lactacystinCellular proliferationProteasome activitySelective inhibitionMHC class IDose-dependent mannerTransplant rejectionAutoimmune diseasesMouse CMVAntigen presentationMost MHC class INontoxic dosesChymotrypsin-like activityClass ISelective proteasome inhibitor lactacystinApoptosis inductionMicroM lactacystinViral proteinsPresentationInhibitionComplete inhibitionLactacystinVivoProliferationPR39, a peptide regulator of angiogenesis
Li J, Post M, Volk R, Gao Y, Li M, Metais C, Sato K, Tsai J, Aird W, Rosenberg R, Hampton T, Li J, Sellke F, Carmeliet P, Simons M. PR39, a peptide regulator of angiogenesis. Nature Medicine 2000, 6: 49-55. PMID: 10613823, DOI: 10.1038/71527.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntimicrobial Cationic PeptidesAortaCapillariesCattleCell HypoxiaCells, CulturedCoronary VesselsCysteine EndopeptidasesDNA-Binding ProteinsEndothelium, VascularHeartHumansHypoxia-Inducible Factor 1Hypoxia-Inducible Factor 1, alpha SubunitIn Vitro TechniquesMacrophagesMiceMice, Inbred C57BLMice, TransgenicMultienzyme ComplexesMyocardial InfarctionMyocardial IschemiaNeovascularization, PhysiologicNuclear ProteinsPeptidesProteasome Endopeptidase ComplexRecombinant ProteinsSwineTranscription FactorsUbiquitinsUmbilical Veinsvon Willebrand FactorConceptsHypoxia-inducible factor-1α (HIF-1α) degradationMacrophage-derived peptideHypoxia-inducible factor-1α (HIF-1α) proteinCoronary flow studiesInflammation-induced angiogenesisInduction of angiogenesisMyocardial vasculatureTissue injuryPotent inductorFunctional blood vesselsBlood vesselsVascular structuresAngiogenesisSelective inhibitionPR39
1999
Selective inhibition of HEMA gene expression by photooxidation in Arabidopsis thaliana
Kumar M, Chaturvedi S, Söll D. Selective inhibition of HEMA gene expression by photooxidation in Arabidopsis thaliana. Phytochemistry 1999, 51: 847-851. PMID: 10423858, DOI: 10.1016/s0031-9422(99)00114-4.Peer-Reviewed Original ResearchConceptsArabidopsis thalianaChloroplasts of plantsGlutamyl-tRNA reductaseCarotenoid biosynthesisFirst enzymeALA formationPhotobleaching herbicidesPhotooxidative damageGene expressionSelective inhibitionCarotenoid pigmentsNorflurazonThalianaPlantsChloroplastsFirst precursorPathwayExpressionEnzymeInitial metaboliteAlaBiosynthesisInhibitionTetrapyrrolesGlutamate
1993
Competence induction by PDGF requires sustained calcium influx by a mechanism distinct from storage-dependent calcium influx
Estacion M, Mordan L. Competence induction by PDGF requires sustained calcium influx by a mechanism distinct from storage-dependent calcium influx. Cell Calcium 1993, 14: 439-454. PMID: 8395338, DOI: 10.1016/0143-4160(93)90003-o.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBucladesineCalciumCalcium ChannelsCell CompartmentationCell DivisionCell LineCell MembraneColforsinContact InhibitionDNA ReplicationDrug SynergismExtracellular SpaceFibroblastsGallic AcidInsulinIon Channel GatingLanthanumMiceMice, Inbred C3HNifedipinePlatelet-Derived Growth FactorS PhaseSignal TransductionTetradecanoylphorbol AcetateConceptsCalcium influxIntracellular storage sitesExtracellular calciumCalcium influx pathwaySustained calcium influxIntracellular calcium concentrationExtracellular calcium influxRelease of calciumPercentage of cellsC3H 10T1/2 mouse fibroblastsPDGF exposureSustained elevationTMB-8Influx pathwayBiphasic increaseSustained increaseDibutyryl cGMPCalcium concentrationS phasePDGFDibutyryl cAMPCell replicationSelective inhibitionReplicative competenceProgression
1978
Inhibition of translation by poliovirus: inactivation of a specific initiation factor.
Rose J, Trachsel H, Leong K, Baltimore D. Inhibition of translation by poliovirus: inactivation of a specific initiation factor. Proceedings Of The National Academy Of Sciences Of The United States Of America 1978, 75: 2732-2736. PMID: 208073, PMCID: PMC392637, DOI: 10.1073/pnas.75.6.2732.Peer-Reviewed Original ResearchConceptsUninfected cellsHost mRNA translationPoliovirus infectionVSV mRNAsUninfected HeLa cellsInfected cellsSelective inhibitionSlow inactivationMixed extractPoliovirus-induced inhibitionInhibitionMRNACellsPoliovirusLysatesProtein synthesisMRNA translationInitiation factorsInhibition of translationExtractTranslation initiation factor
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