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
2014
The Nogo Receptor NgR1 Mediates Infection by Mammalian Reovirus
Konopka-Anstadt JL, Mainou BA, Sutherland DM, Sekine Y, Strittmatter SM, Dermody TS. The Nogo Receptor NgR1 Mediates Infection by Mammalian Reovirus. Cell Host & Microbe 2014, 15: 681-691. PMID: 24922571, PMCID: PMC4100558, DOI: 10.1016/j.chom.2014.05.010.Peer-Reviewed Original ResearchConceptsCentral nervous systemReceptor NgR1Reovirus infectionExpression of NgR1Primary cortical neuronsDistinct cell surface moleculesJunctional adhesion molecule ASoluble NgR1Cell surface moleculesNeurotropic virusesCortical neuronsMammalian reovirusesNonsusceptible cellsNervous systemNgR1Null miceSystemic spreadInfectionIndependent receptorsMultiple receptorsReovirus replicationInitial siteReovirus virionsNeuronsReceptors
2012
Vps10 Family Proteins and the Retromer Complex in Aging-Related Neurodegeneration and Diabetes
Lane RF, St George-Hyslop P, Hempstead BL, Small SA, Strittmatter SM, Gandy S. Vps10 Family Proteins and the Retromer Complex in Aging-Related Neurodegeneration and Diabetes. Journal Of Neuroscience 2012, 32: 14080-14086. PMID: 23055476, PMCID: PMC3576841, DOI: 10.1523/jneurosci.3359-12.2012.Peer-Reviewed Original ResearchConceptsBrain-derived neurotrophic factorType 2 diabetes mellitusNeurotrophic signaling pathwaysFrontotemporal lobar degenerationNon-neuronal cellsPathogenesis of neurodegenerationGenetic risk factorsBDNF levelsDiabetes mellitusFamily of receptorsNeurotrophic factorRisk factorsParkinson's diseaseTrk receptorsAcute responseAutosomal dominant formAlzheimer's diseaseNeurodegenerative diseasesDiseaseCell surface receptorsReceptorsSignaling pathwaysSurface receptorsPleiotropic functionsIntracellular responses
2011
Membrane-type Matrix Metalloproteinase-3 Regulates Neuronal Responsiveness to Myelin through Nogo-66 Receptor 1 Cleavage*
Ferraro GB, Morrison CJ, Overall CM, Strittmatter SM, Fournier AE. Membrane-type Matrix Metalloproteinase-3 Regulates Neuronal Responsiveness to Myelin through Nogo-66 Receptor 1 Cleavage*. Journal Of Biological Chemistry 2011, 286: 31418-31424. PMID: 21768085, PMCID: PMC3173120, DOI: 10.1074/jbc.m111.249169.Peer-Reviewed Original ResearchConceptsMatrix metalloproteinase-3Primary neuronsMetalloproteinase-3Neuronal responsesSH-SY5Y neuroblastoma cellsMetalloproteinase-dependent mannerNeuronal responsivenessAxonal regrowthCortical neuronsNeuronal knockdownNgR1Receptor 1Neuroblastoma cellsNeuronsCell surfaceMT3-MMPMyelinSpecific metalloproteinasesGlycosylphosphatidylinositol-anchored receptorInhibitorsPhysiological consequencesCleavage fragmentsCleavage-resistant formMetalloproteinasesReceptorsMyelin associated inhibitors: A link between injury-induced and experience-dependent plasticity
Akbik F, Cafferty WB, Strittmatter SM. Myelin associated inhibitors: A link between injury-induced and experience-dependent plasticity. Experimental Neurology 2011, 235: 43-52. PMID: 21699896, PMCID: PMC3189418, DOI: 10.1016/j.expneurol.2011.06.006.Peer-Reviewed Original ResearchConceptsExperience-dependent plasticityAnatomical rearrangementsNogo-66 receptor 1Spinal cord injuryNeurologic recoveryFunctional recoveryInciting stimulusCNS injuryCord injuryAxonal regenerationAdult CNSInjury studiesAnimal modelsReceptor 1Common receptorPaired-ImmunoglobulinMyelinInhibitorsInjuryAnatomical growthCNSReceptorsWide spectrumExtracellular matrixGrowth inhibitor
2010
Lynx for Braking Plasticity
Higley MJ, Strittmatter SM. Lynx for Braking Plasticity. Science 2010, 330: 1189-1190. PMID: 21109660, PMCID: PMC3244692, DOI: 10.1126/science.1198983.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAgingAmblyopiaAnimalsChondroitin Sulfate ProteoglycansDominance, OcularMembrane GlycoproteinsMiceMice, KnockoutNeuronal PlasticityNeuropeptidesNicotinic AntagonistsReceptors, ImmunologicReceptors, NicotinicSensory DeprivationSignal TransductionVision, OcularVisual CortexVisual PathwaysConceptsVisual cortex plasticityVisual cortex neuronsNicotinic acetylcholine receptorsJuvenile plasticityNeurological performanceCortex neuronsJuvenile brainOcular dominanceAdult miceAcetylcholine receptorsVisual cortexAdult animalsSensory inputAdultsYoung mammalsMiceMedical implicationsEyesSuch plasticityPlasticityCortexNeuronsBrainReceptors
2009
β-amyloid oligomers and cellular prion protein in Alzheimer’s disease
Gunther EC, Strittmatter SM. β-amyloid oligomers and cellular prion protein in Alzheimer’s disease. Journal Of Molecular Medicine 2009, 88: 331-338. PMID: 19960174, PMCID: PMC2846635, DOI: 10.1007/s00109-009-0568-7.Peer-Reviewed Original ResearchConceptsCreutzfeldt-Jakob diseaseAβ oligomersDisease pathophysiologyCellular prion proteinProgression of ADAlzheimer's disease pathophysiologyΒ-amyloid oligomersΒ-amyloid peptidePrion proteinBrain slicesAlzheimer's diseaseSynaptic functionFunctional receptorsNeurodegenerative diseasesDiseasePotential mediatorsAβ assembliesReceptorsAβ monomersPrPCPathophysiologyNeurotoxicityPlaquesProgression
2007
Nogo receptor interacts with brain APP and Abeta to reduce pathologic changes in Alzheimer's transgenic mice.
Park JH, Strittmatter SM. Nogo receptor interacts with brain APP and Abeta to reduce pathologic changes in Alzheimer's transgenic mice. Current Alzheimer Research 2007, 4: 568-70. PMID: 18220524, PMCID: PMC2846284, DOI: 10.2174/156720507783018235.Peer-Reviewed Original ResearchConceptsTransgenic miceAlzheimer's diseasePlaque depositionAdult central nervous systemAlzheimer's transgenic miceNogo-66 receptorAmyloid β plaquesCentral nervous systemAxonal sproutingAβ accumulationΒ plaquesDystrophic neuritesPathologic changesNogo receptorNervous systemBrain APPDiseasePotential mechanistic basisMiceExpression increasesNGR modificationReceptorsNeurite responseNGRMechanistic basis
2006
Identification of a receptor necessary for Nogo-B stimulated chemotaxis and morphogenesis of endothelial cells
Miao RQ, Gao Y, Harrison KD, Prendergast J, Acevedo LM, Yu J, Hu F, Strittmatter SM, Sessa WC. Identification of a receptor necessary for Nogo-B stimulated chemotaxis and morphogenesis of endothelial cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 2006, 103: 10997-11002. PMID: 16835300, PMCID: PMC1544163, DOI: 10.1073/pnas.0602427103.Peer-Reviewed Original ResearchConceptsAmino terminusNogo isoformsHeterologous expression systemDiscovery of agonistsLoop domainNative endothelial cellsEndothelial cellsExpression systemCell spreadingTube formationTerminusNogo-66 receptorIsoformsChemotaxisReceptorsAngiogenesisCellsMorphogenesisVascular remodelingIdentificationPathwayRemodelingNogoVascular functionCardiovascular functionRanBPM Contributes to Semaphorin3A Signaling through Plexin-A Receptors
Togashi H, Schmidt EF, Strittmatter SM. RanBPM Contributes to Semaphorin3A Signaling through Plexin-A Receptors. Journal Of Neuroscience 2006, 26: 4961-4969. PMID: 16672672, PMCID: PMC2846289, DOI: 10.1523/jneurosci.0704-06.2006.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsCell Adhesion MoleculesCell DeathCell SizeCells, CulturedChick EmbryoCloning, MolecularCricetinaeCricetulusCytoskeletal ProteinsDose-Response Relationship, DrugDrug InteractionsEnzyme InhibitorsGanglia, SpinalGene ExpressionGreen Fluorescent ProteinsHumansImmunoprecipitationIn Situ Nick-End LabelingNerve Tissue ProteinsNeuritesNeuronsNeuropilin-1Nuclear ProteinsRan GTP-Binding ProteinSemaphorin-3ASignal TransductionTranscription Factor AP-1TransfectionTwo-Hybrid System TechniquesConceptsPlexin-A1Collapsin response mediator proteinsNervous system developmentReceptor complex consistingSignal transductionRanBPMMediator proteinsMicrotubule functionCell spreadingComplex consistingAxonal guidanceNeuronal cellsAxonal guidance cuesProteinGuidance cuesPlexinsAxonal outgrowthExpressionSema3ATransductionReceptorsDomainOverexpressionNeuropilinsSystem development
2005
Experience-Driven Plasticity of Visual Cortex Limited by Myelin and Nogo Receptor
McGee AW, Yang Y, Fischer QS, Daw NW, Strittmatter SM. Experience-Driven Plasticity of Visual Cortex Limited by Myelin and Nogo Receptor. Science 2005, 309: 2222-2226. PMID: 16195464, PMCID: PMC2856689, DOI: 10.1126/science.1114362.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsChondroitin Sulfate ProteoglycansDarknessDominance, OcularElectrophysiologyGamma-Aminobutyric AcidGene TargetingGPI-Linked ProteinsMiceMice, Inbred C57BLMutationMyelin Basic ProteinMyelin ProteinsMyelin SheathMyelin-Associated GlycoproteinNeuritesNeuronal PlasticityNeuronsNogo ProteinsNogo Receptor 1Photic StimulationReceptors, Cell SurfaceSignal TransductionVisual CortexConceptsOcular dominanceOcular dominance plasticityNogo-66 receptorExperience-dependent plasticityPostnatal critical periodCritical periodFunctional recoveryAxonal regenerationMonocular deprivationNogo receptorDays postnatalVisual cortexNeural circuitryPathological traumaJuvenile ageMyelinReceptorsNGRPlasticityPostnatalCortexOMgpTraumaNogoCessation
2004
RGM and its receptor neogenin regulate neuronal survival
Matsunaga E, Tauszig-Delamasure S, Monnier PP, Mueller BK, Strittmatter SM, Mehlen P, Chédotal A. RGM and its receptor neogenin regulate neuronal survival. Nature Cell Biology 2004, 6: 749-755. PMID: 15258591, DOI: 10.1038/ncb1157.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisAvian ProteinsCaspasesCell SurvivalCells, CulturedChick EmbryoChickensDown-RegulationEnzyme ActivationGene Expression Regulation, DevelopmentalGreen Fluorescent ProteinsImmunohistochemistryIn Situ HybridizationLuminescent ProteinsMembrane ProteinsMutagenesis, Site-DirectedNeuronsRatsRNA, Small InterferingConceptsRepulsive guidance moleculeNeural tubePro-apoptotic activityAxon guidance proteinCytoplasmic domainImmortalized neuronal cellsGene transfer technologyDependence receptorsCell deathGuidance proteinsNeuronal cellsNeogenin receptorGuidance moleculesNeuronal survivalRetinal axonsChick embryosNeogeninReceptor neogeninExpressionCaspasesReceptorsTransfer technologyEmbryosProteinApoptosis
2003
The Nogo-66 receptor: focusing myelin inhibition of axon regeneration
McGee AW, Strittmatter SM. The Nogo-66 receptor: focusing myelin inhibition of axon regeneration. Trends In Neurosciences 2003, 26: 193-198. PMID: 12689770, DOI: 10.1016/s0166-2236(03)00062-6.Peer-Reviewed Original ResearchMeSH KeywordsAcute-Phase ProteinsAnimalsAxonsCells, CulturedGPI-Linked ProteinsHumansIn Vitro TechniquesMiceMyelin ProteinsMyelin SheathMyelin-Associated GlycoproteinMyelin-Oligodendrocyte GlycoproteinNerve RegenerationNeural InhibitionNeuronal PlasticityNogo ProteinsNogo Receptor 1RatsReceptor, Nerve Growth FactorReceptors, Cell SurfaceReceptors, Nerve Growth FactorSignal TransductionConceptsNogo-66 receptorMembrane protein NogoSpinal cord injuryFunctional recoveryCord injuryAxonal regrowthSecond messenger pathwaysProtein NogoAdult CNSAxon regenerationMyelin inhibitionAxonal outgrowthAdditional studiesCNS myelinMyelinNeurite elongationPhysiological roleReceptorsMolecular determinantsInhibitorsInhibitionNGRCurrent understanding
2002
Truncated Soluble Nogo Receptor Binds Nogo-66 and Blocks Inhibition of Axon Growth by Myelin
Fournier AE, Gould GC, Liu BP, Strittmatter SM. Truncated Soluble Nogo Receptor Binds Nogo-66 and Blocks Inhibition of Axon Growth by Myelin. Journal Of Neuroscience 2002, 22: 8876-8883. PMID: 12388594, PMCID: PMC6757674, DOI: 10.1523/jneurosci.22-20-08876.2002.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAxonsCell LineChick EmbryoGPI-Linked ProteinsGrowth ConesHumansKidneyMiceMolecular Sequence DataMutagenesis, Site-DirectedMyelin ProteinsMyelin SheathNeuritesNogo ProteinsNogo Receptor 1Peptide FragmentsProtein BindingProtein Structure, TertiaryReceptors, Cell SurfaceRepetitive Sequences, Amino AcidRetinaSequence DeletionSignal TransductionSolubilityConceptsChick retinal ganglion cellsRetinal ganglion cellsOutgrowth inhibitionMechanism of NogoGanglion cellsNogo receptorOutgrowth inhibitorViral infectionMyelin inhibitionInhibitory signalingNogo-66Axon growthCNS myelinAxon outgrowthMyelinRegenerative growthNogoCOS-7 cellsInhibitionAlkaline phosphataseReceptorsNGRModulation of axonal regeneration in neurodegenerative disease
Strittmatter SM. Modulation of axonal regeneration in neurodegenerative disease. Journal Of Molecular Neuroscience 2002, 19: 117-121. PMID: 12212768, DOI: 10.1007/s12031-002-0021-7.Peer-Reviewed Original ResearchLocalization of Nogo-A and Nogo-66 Receptor Proteins at Sites of Axon–Myelin and Synaptic Contact
Wang X, Chun SJ, Treloar H, Vartanian T, Greer CA, Strittmatter SM. Localization of Nogo-A and Nogo-66 Receptor Proteins at Sites of Axon–Myelin and Synaptic Contact. Journal Of Neuroscience 2002, 22: 5505-5515. PMID: 12097502, PMCID: PMC6758202, DOI: 10.1523/jneurosci.22-13-05505.2002.Peer-Reviewed Original ResearchConceptsAdult CNSLimited axonal regenerationSpinal cord injuryNogo-66 receptorInteraction of NogoAxonal plasticityCord injurySynaptic contactsAxonal regenerationNgR proteinMyelinated fibersPostnatal neuronsLocalization of NogoMyelinated axonsAxonal growthOligodendrocyte surfacePhysiologic roleAxonsNogoProtein expressionNeuronsReceptorsInhibitory proteinInjuryCNSMyelin-Associated Glycoprotein as a Functional Ligand for the Nogo-66 Receptor
Liu BP, Fournier A, GrandPré T, Strittmatter SM. Myelin-Associated Glycoprotein as a Functional Ligand for the Nogo-66 Receptor. Science 2002, 297: 1190-1193. PMID: 12089450, DOI: 10.1126/science.1073031.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonsBinding SitesChick EmbryoCloning, MolecularCOS CellsGanglia, SpinalGene LibraryGPI-Linked ProteinsLigandsMiceMyelin ProteinsMyelin-Associated GlycoproteinNerve RegenerationNeuritesNeuronsNogo ProteinsNogo Receptor 1Peptide FragmentsPhosphatidylinositol Diacylglycerol-LyaseProtein Structure, TertiaryReceptors, Cell SurfaceRecombinant Fusion ProteinsSialic AcidsTransfectionType C PhospholipasesChapter 25 Nogo and the Nogo-66 receptor
Fournier AE, GrandPré T, Gould G, Wang X, Strittmatter SM. Chapter 25 Nogo and the Nogo-66 receptor. Progress In Brain Research 2002, 137: 361-369. PMID: 12440378, DOI: 10.1016/s0079-6123(02)37027-4.Peer-Reviewed Original ResearchConceptsNogo-66 receptorAxonal regenerationNogo-66Oligodendrocyte myelin glycoproteinAxonal inhibitionAdult vertebrate CNSUnresponsive neuronsChondroitin sulfate proteoglycanCentral nervous system myelinCNS injuryReceptor expressionAxon regenerationMyelin inhibitionMyelin glycoproteinReceptor componentsNogoReceptorsSystem myelinAxonal surfaceSulfate proteoglycanNeuronsInhibitionMyelinVertebrate CNSHigh affinity
2001
Identification of a receptor mediating Nogo-66 inhibition of axonal regeneration
Fournier A, GrandPre T, Strittmatter S. Identification of a receptor mediating Nogo-66 inhibition of axonal regeneration. Nature 2001, 409: 341-346. PMID: 11201742, DOI: 10.1038/35053072.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAmino Acid SequenceAnimalsAxonsBinding SitesCell DivisionCell LineChickensCloning, MolecularCOS CellsDNA, ComplementaryGene ExpressionGPI-Linked ProteinsGrowth ConesHumansMiceMolecular Sequence DataMyelin ProteinsNerve RegenerationNogo ProteinsNogo Receptor 1Protein Structure, TertiaryReceptors, Cell SurfaceRecombinant Fusion ProteinsConceptsNogo-66Axonal regenerationHuman CNS injuryNogo-66 receptorAxonal inhibitionAdult vertebrate CNSUnresponsive neuronsCentral nervous system myelinCNS injuryReceptor expressionAxon regenerationEnhanced recoveryGlycophosphatidylinositol-linked proteinAxonal extensionNogoNeuronsReceptorsSystem myelinAxonal surfaceInhibitionCell typesVertebrate CNSExtracellular domainHigh affinityCell morphology
1998
Semaphorins A and E act as antagonists of neuropilin-1 and agonists of neuropilin-2 receptors
Takahashi T, Nakamura F, Jin Z, Kalb R, Strittmatter S. Semaphorins A and E act as antagonists of neuropilin-1 and agonists of neuropilin-2 receptors. Nature Neuroscience 1998, 1: 487-493. PMID: 10196546, DOI: 10.1038/2203.Peer-Reviewed Original Research