2010
Increased Dendrite Branching in AβPP/PS1 Mice and Elongation of Dendrite Arbors by Fasudil Administration
Couch BA, DeMarco GJ, Gourley SL, Koleske AJ. Increased Dendrite Branching in AβPP/PS1 Mice and Elongation of Dendrite Arbors by Fasudil Administration. Journal Of Alzheimer’s Disease 2010, 20: 1003-1008. PMID: 20413901, PMCID: PMC3077946, DOI: 10.3233/jad-2010-091114.Peer-Reviewed Original ResearchConceptsDendrite arborsPS1 miceAβPP/PS1 miceAmyloid-beta overproductionPS1 transgenic miceCA1 pyramidal neuronsROCK inhibitor fasudilROCK signalingPyramidal neuronsDendritic regressionFasudil administrationPharmacological reductionInhibitor fasudilTransgenic miceAlzheimer's diseaseMiceDendrite branchingRho-kinaseArborsDiseaseNeuronsSignalingAtrophyFasudilAbeta
2009
Cellular Prion Protein Mediates the Toxicity of β-Amyloid Oligomers: Implications for Alzheimer Disease
Nygaard HB, Strittmatter SM. Cellular Prion Protein Mediates the Toxicity of β-Amyloid Oligomers: Implications for Alzheimer Disease. JAMA Neurology 2009, 66: 1325-1328. PMID: 19901162, PMCID: PMC2849161, DOI: 10.1001/archneurol.2009.223.Peer-Reviewed Original ResearchConceptsAlzheimer's diseaseCellular prion proteinPathogenesis of ADBeta-amyloid plaquesAge-related dementiaSoluble oligomeric assembliesPrion proteinPotential clinical implicationsBeta-amyloid oligomersΒ-amyloid oligomersHigh-affinity receptorCommon causeSynaptic plasticityTherapeutic interventionsClinical implicationsAbeta oligomersNovel targetRecent evidenceToxic effectsDiseasePathogenesisDementiaAbetaPlaquesBrain
2006
Subcutaneous Nogo Receptor Removes Brain Amyloid-β and Improves Spatial Memory in Alzheimer's Transgenic Mice
Park JH, Widi GA, Gimbel DA, Harel NY, Lee DH, Strittmatter SM. Subcutaneous Nogo Receptor Removes Brain Amyloid-β and Improves Spatial Memory in Alzheimer's Transgenic Mice. Journal Of Neuroscience 2006, 26: 13279-13286. PMID: 17182778, PMCID: PMC2856604, DOI: 10.1523/jneurosci.4504-06.2006.Peer-Reviewed Original ResearchConceptsAmyloid precursor proteinTransgenic miceAlzheimer's diseaseAbeta clearanceAbeta plaque loadAlzheimer's transgenic miceImproved spatial memoryRadial arm water mazeNogo-66 receptorEffective therapeutic approachPotential therapeutic benefitSpatial memoryAmyloid-beta peptidePlaque loadAbeta levelsBrain amyloidDisease onsetAbeta productionTherapeutic approachesNogo receptorTherapeutic benefitWater mazeInverse correlationAbetaMice
2000
Amyloid Beta-Induced Neuronal Death is Bax-Dependent but Caspase-Independent
Selznick L, Zheng T, Flavell R, Rakic P, Roth K. Amyloid Beta-Induced Neuronal Death is Bax-Dependent but Caspase-Independent. Journal Of Neuropathology & Experimental Neurology 2000, 59: 271-279. PMID: 10759182, DOI: 10.1093/jnen/59.4.271.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid Chloromethyl KetonesAmyloid beta-PeptidesAnimalsApoptosisbcl-2-Associated X ProteinCaspase 3Caspase InhibitorsCaspasesCell DeathCells, CulturedCysteine Proteinase InhibitorsDose-Response Relationship, DrugFemaleGlycoproteinsIn Situ Nick-End LabelingMaleMiceMice, KnockoutMicrotubule-Associated ProteinsMicrotubulesNeuronsPaclitaxelProto-Oncogene ProteinsProto-Oncogene Proteins c-bcl-2TelencephalonConceptsNeuronal deathNeuronal apoptosisCaspase-3 activationTelencephalic neuronsFibrillar amyloid-beta (Abeta) peptidesAbeta-induced neuronal apoptosisAD treatment strategiesAbeta-induced neuronal deathPathogenesis of ADAlzheimer's disease brainEffects of AbetaAmyloid-beta peptideApoptotic nuclear featuresUnderlying pathophysiologyTreatment strategiesDisease brainSenile plaquesNeurotoxic effectsAmyloid betaCalpain inhibitionPharmacological inhibitionBeta peptideNuclear featuresAbetaCaspase-3
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