2017
Chapter Thirteen Synaptotoxic Signaling by Amyloid Beta Oligomers in Alzheimer's Disease Through Prion Protein and mGluR5
Brody AH, Strittmatter SM. Chapter Thirteen Synaptotoxic Signaling by Amyloid Beta Oligomers in Alzheimer's Disease Through Prion Protein and mGluR5. Advances In Pharmacology 2017, 82: 293-323. PMID: 29413525, PMCID: PMC5835229, DOI: 10.1016/bs.apha.2017.09.007.Peer-Reviewed Original ResearchConceptsAlzheimer's diseaseNovel potential therapeutic targetDisease-modifying AD therapiesPotential therapeutic targetAmyloid-beta oligomersPrion proteinSynapse lossTau pathologySynaptic dysfunctionAD symptomsSynaptic damageAD pathophysiologyNeuronal dysfunctionSynaptic toxicityDisease progressionAD progressionAD therapyMemory dysfunctionTherapeutic targetCellular prion proteinBeta oligomersDysfunctionDiseaseGlobal health crisisMGluR5
2016
Chapter 8 Targeting Aβ Receptors to Modify Alzheimer’s Disease Progression
Haas L, Strittmatter S. Chapter 8 Targeting Aβ Receptors to Modify Alzheimer’s Disease Progression. 2016, 227-250. DOI: 10.1016/b978-0-12-802173-6.00008-3.Peer-Reviewed Original ResearchAlzheimer's diseaseDisease progressionIntervention sitesCourse of ADMetabotropic glutamate receptor 5Glutamate receptor 5Receptor-mediated mechanismAlzheimer's disease progressionHigh-affinity natureAD pathophysiologyReceptor mechanismsReceptor 5Preclinical successMGluR5 pathwayAβ receptorsCellular prion proteinSuch receptorsPathological processesDiseasePathophysiological signalsReceptorsPrion proteinSpecific pathwaysPathwayHigh affinity
2010
Laurén et al. reply
Laurén J, Gimbel D, Nygaard H, Gilbert J, Strittmatter S. Laurén et al. reply. Nature 2010, 466: e4-e5. DOI: 10.1038/nature09218.Peer-Reviewed Original ResearchDisease model miceTransgenic Alzheimer's disease model miceAlzheimer's disease model miceDisease miceModel miceDisease progressionTransgenic Alzheimer's disease miceSpatial learningAlzheimer's disease miceAlzheimer's disease progressionSynapse lossAxonal degenerationEarly deathTransgenic miceCellular prion proteinMicePrion proteinPrPCDeficitsExpression cloningDirect assessmentDegeneration
2009
Reticulon-4A (Nogo-A) Redistributes Protein Disulfide Isomerase to Protect Mice from SOD1-Dependent Amyotrophic Lateral Sclerosis
Yang YS, Harel NY, Strittmatter SM. Reticulon-4A (Nogo-A) Redistributes Protein Disulfide Isomerase to Protect Mice from SOD1-Dependent Amyotrophic Lateral Sclerosis. Journal Of Neuroscience 2009, 29: 13850-13859. PMID: 19889996, PMCID: PMC2797811, DOI: 10.1523/jneurosci.2312-09.2009.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmyotrophic Lateral SclerosisAnimalsChlorocebus aethiopsCOS CellsGlycineMaleMiceMice, CongenicMice, Inbred C57BLMice, KnockoutMice, TransgenicMolecular ChaperonesMyelin ProteinsNeuroprotective AgentsNogo ProteinsProtein Disulfide-IsomerasesSuperoxide DismutaseSuperoxide Dismutase-1Tissue DistributionConceptsAmyotrophic lateral sclerosisLateral sclerosisFatal motor neuron diseaseSubset of patientsALS disease progressionMotor neuron diseaseTransgenic mouse modelPotential therapeutic approachEndoplasmic reticulum stressHomogeneous expression patternNeuron diseaseALS pathophysiologyDisease onsetDisease progressionTherapeutic approachesMouse modelChaperone protein disulfide isomeraseReticulum stressNovel intracellular roleReticulon proteinsMiceSclerosisPatientsUnfolded protein responseNogoA