2020
Nogo receptor decoy promotes recovery and corticospinal growth in non-human primate spinal cord injury
Wang X, Zhou T, Maynard GD, Terse PS, Cafferty WB, Kocsis JD, Strittmatter SM. Nogo receptor decoy promotes recovery and corticospinal growth in non-human primate spinal cord injury. Brain 2020, 143: 1697-1713. PMID: 32375169, PMCID: PMC7850069, DOI: 10.1093/brain/awaa116.Peer-Reviewed Original ResearchConceptsPrimate spinal cord injurySpinal cord injuryCord injuryFemale African green monkeysTreatment-related adverse eventsChronic neurological deficitsNogo receptor 1Left motor cortexRecovery of functionPreclinical rodent modelsSpinal cord injury animalsAfrican green monkeysRaphespinal fibersAdverse eventsCervical cordNeurological deficitsSurgical complicationsCNS traumaTreatment cessationCorticospinal axonsLumbar catheterInjury animalsNeural recoverySpontaneous feedingLateral hemisection
2011
Recovery from chronic spinal cord contusion after nogo receptor intervention
Wang X, Duffy P, McGee AW, Hasan O, Gould G, Tu N, Harel NY, Huang Y, Carson RE, Weinzimmer D, Ropchan J, Benowitz LI, Cafferty WB, Strittmatter SM. Recovery from chronic spinal cord contusion after nogo receptor intervention. Annals Of Neurology 2011, 70: 805-821. PMID: 22162062, PMCID: PMC3238798, DOI: 10.1002/ana.22527.Peer-Reviewed Original ResearchConceptsChronic spinal cord injurySpinal cord injuryContusion injuryCord injurySpinal cord contusion injuryCentral nervous system injuryBresnahan locomotor scoresOpen-field BassoSpinal hemisection injuryWeight-bearing statusSpinal cord contusionMonths of treatmentNervous system injuryMyelin-derived inhibitorCaudal spinal cordPositron emission tomographyNgR1 pathwayRaphespinal axonsSpinal contusionCord contusionHemisection injuryFunctional recoveryLocomotor scoresSystem injuryControl rats
2009
LGI1-associated epilepsy through altered ADAM23-dependent neuronal morphology
Owuor K, Harel NY, Englot DJ, Hisama F, Blumenfeld H, Strittmatter SM. LGI1-associated epilepsy through altered ADAM23-dependent neuronal morphology. Molecular And Cellular Neuroscience 2009, 42: 448-457. PMID: 19796686, PMCID: PMC2783222, DOI: 10.1016/j.mcn.2009.09.008.Peer-Reviewed Original ResearchConceptsNeuronal morphologyAutosomal dominant partial epilepsyCA1 pyramidal neuronsSeizure thresholdSpontaneous seizuresPartial epilepsyPyramidal neuronsDendritic arborizationLGI1PSD-95LGI1 geneEpilepsy genesADAM23ADPEAFADAM22EpilepsyNeurite outgrowthIon channelsBrain genesUnbiased screenAuditory featuresOutgrowthSeizuresArborizationRelated proteins
2006
Delayed Nogo receptor therapy improves recovery from spinal cord contusion
Wang X, Baughman KW, Basso DM, Strittmatter SM. Delayed Nogo receptor therapy improves recovery from spinal cord contusion. Annals Of Neurology 2006, 60: 540-549. PMID: 16958113, PMCID: PMC2855693, DOI: 10.1002/ana.20953.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonsDisease Models, AnimalDrug Administration ScheduleDrug Therapy, CombinationFemaleInjections, IntraventricularLocomotionMyelin SheathPhosphodiesterase InhibitorsPyramidal TractsRatsRats, Sprague-DawleyRecombinant Fusion ProteinsRecovery of FunctionRolipramSpinal Cord InjuriesTime FactorsTreatment OutcomeConceptsSpinal cord contusionCord contusionSpinal cordAxonal growthHuman spinal cord injuryAdult central nervous systemBresnahan locomotor scoresFc treatment groupVehicle-treated groupTime of injuryCyclic adenosine monophosphate phosphodiesterase inhibitorSpinal cord injuryRecovery of locomotionAddition of rolipramRostral spinal cordCentral nervous systemCaudal spinal cordBeneficial behavioral effectsDelayed therapyNeurological recoveryRaphespinal axonsAcute therapyCorticospinal axonsLocomotor scoresIntracerebroventricular route
2005
Nogo-A Interacts with the Nogo-66 Receptor through Multiple Sites to Create an Isoform-Selective Subnanomolar Agonist
Hu F, Liu BP, Budel S, Liao J, Chin J, Fournier A, Strittmatter SM. Nogo-A Interacts with the Nogo-66 Receptor through Multiple Sites to Create an Isoform-Selective Subnanomolar Agonist. Journal Of Neuroscience 2005, 25: 5298-5304. PMID: 15930377, PMCID: PMC2855126, DOI: 10.1523/jneurosci.5235-04.2005.Peer-Reviewed Original ResearchMeSH KeywordsAlkaline PhosphataseAnimalsAxonsBinding SitesCell LineChick EmbryoChlorocebus aethiopsGlutathione TransferaseGPI-Linked ProteinsHumansIn Vitro TechniquesLigandsMiceMyelin ProteinsNogo ProteinsNogo Receptor 1PeptidesProtein IsoformsProtein Structure, TertiaryReceptors, Cell SurfaceRecombinant Fusion Proteins
2004
Blockade of Nogo-66, Myelin-Associated Glycoprotein, and Oligodendrocyte Myelin Glycoprotein by Soluble Nogo-66 Receptor Promotes Axonal Sprouting and Recovery after Spinal Injury
Li S, Liu BP, Budel S, Li M, Ji B, Walus L, Li W, Jirik A, Rabacchi S, Choi E, Worley D, Sah DW, Pepinsky B, Lee D, Relton J, Strittmatter SM. Blockade of Nogo-66, Myelin-Associated Glycoprotein, and Oligodendrocyte Myelin Glycoprotein by Soluble Nogo-66 Receptor Promotes Axonal Sprouting and Recovery after Spinal Injury. Journal Of Neuroscience 2004, 24: 10511-10520. PMID: 15548666, PMCID: PMC6730300, DOI: 10.1523/jneurosci.2828-04.2004.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonsEvoked Potentials, MotorFemaleGPI-Linked ProteinsInjections, SpinalMotor ActivityMyelin ProteinsMyelin-Associated GlycoproteinMyelin-Oligodendrocyte GlycoproteinNogo ProteinsNogo Receptor 1OligodendrogliaPeptide FragmentsRatsRats, Sprague-DawleyReceptors, Cell SurfaceReceptors, PeptideRecombinant Fusion ProteinsSerotoninSolubilitySpinal CordSpinal Cord InjuriesConceptsAxonal sproutingTraumatic spinal cord injurySpinal-injured ratsSpinal cord injuryAdult mammalian CNSNogo-66 receptorOligodendrocyte myelin glycoproteinMyelin associated glycoproteinRaphespinal fibersLocomotor recoveryCord injurySpinal injuryMammalian CNSNgR functionTherapeutic potentialAxonal growthNogo-66Myelin glycoproteinInjuryMyelin proteinsImproved locomotionViral blockadeBlockadeFc proteinSproutingNeogenin mediates the action of repulsive guidance molecule
Rajagopalan S, Deitinghoff L, Davis D, Conrad S, Skutella T, Chedotal A, Mueller BK, Strittmatter SM. Neogenin mediates the action of repulsive guidance molecule. Nature Cell Biology 2004, 6: 756-762. PMID: 15258590, DOI: 10.1038/ncb1156.Peer-Reviewed Original ResearchConceptsRepulsive guidance moleculeRetinal ganglion cell axonsGuidance moleculesGanglion cell axonsDorsal root ganglion axonsTemporal retinal axonsVisual map formationReceptor mechanismsCell axonsNeogenin expressionRetinal axonsGanglion axonsAxonal responsivenessOptic tectumChick retinaNeogeninSub-nanomolar affinityAxonsAxonal guidanceNeogenin functionsResponsive stateNeural tubeMap formationExpressionRetinaNogo Receptor Antagonism Promotes Stroke Recovery by Enhancing Axonal Plasticity
Lee JK, Kim JE, Sivula M, Strittmatter SM. Nogo Receptor Antagonism Promotes Stroke Recovery by Enhancing Axonal Plasticity. Journal Of Neuroscience 2004, 24: 6209-6217. PMID: 15240813, PMCID: PMC6729662, DOI: 10.1523/jneurosci.1643-04.2004.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonsBehavior, AnimalDisease Models, AnimalGPI-Linked ProteinsInfarction, Middle Cerebral ArteryMaleMiceMice, KnockoutMyelin ProteinsNeuronal PlasticityNogo ProteinsNogo Receptor 1RatsRats, Sprague-DawleyReceptors, Cell SurfaceReceptors, PeptideRecombinant Fusion ProteinsRecovery of FunctionStrokeTreatment OutcomeConceptsAxonal plasticityStroke recoveryIpsilateral cervical spinal cordMiddle cerebral artery occlusionFocal brain infarctionCerebral artery occlusionCervical spinal cordComplex motor functionContralateral red nucleusUndamaged cortexBrain infarctionArtery occlusionIschemic strokeAxonal sproutingIntracerebroventricular administrationArterial occlusionPharmacological blockadeMotor functionSpinal cordControl animalsRed nucleusAxonal connectionsBehavioral improvementMutant miceStroke
2003
Structural bases for CRMP function in plexin‐dependent semaphorin3A signaling
Deo RC, Schmidt EF, Elhabazi A, Togashi H, Burley SK, Strittmatter SM. Structural bases for CRMP function in plexin‐dependent semaphorin3A signaling. The EMBO Journal 2003, 23: 9-22. PMID: 14685275, PMCID: PMC1271659, DOI: 10.1038/sj.emboj.7600021.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmino Acid SequenceAmino Acid SubstitutionAnimalsCell Adhesion MoleculesCell LineChick EmbryoChlorocebus aethiopsCOS CellsCrystallography, X-RayGanglia, SpinalHumansHydrogen BondingImmunophilinsMiceModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedNerve Tissue ProteinsPhosphoproteinsProtein Structure, SecondaryProtein Structure, TertiaryReceptors, Cell SurfaceRecombinant Fusion ProteinsSemaphorin-3ASequence Homology, Amino AcidSignal TransductionStructure-Activity RelationshipConceptsCollapsin response mediator proteinsStructure-based mutagenesisCOS-7 cellsSurface-exposed residuesTetrameric assemblyPhysical complexAxonal specificationMediator proteinsStructural basisFunctional domainsAlanine substitutionsActive proteinCytosolic phosphoproteinNeuronal differentiationAxonal repulsionAxonal guidanceReceptor componentsProteinStructural viewX-ray crystal structureCRMP1Sema3ACell contractionCellsNP1
2002
Myelin-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 Phospholipases
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
1997
Neuronal and Non-Neuronal Collapsin-1 Binding Sites in Developing Chick Are Distinct from Other Semaphorin Binding Sites
Takahashi T, Nakamura F, Strittmatter S. Neuronal and Non-Neuronal Collapsin-1 Binding Sites in Developing Chick Are Distinct from Other Semaphorin Binding Sites. Journal Of Neuroscience 1997, 17: 9183-9193. PMID: 9364065, PMCID: PMC6573609, DOI: 10.1523/jneurosci.17-23-09183.1997.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAvian ProteinsAxonsBinding SitesCells, CulturedCentral Nervous SystemChick EmbryoDNA, ComplementaryFetal ProteinsGanglia, SpinalGlycoproteinsLungMembrane ProteinsMesodermMiceMotor NeuronsMultigene FamilyNerve Growth FactorsNerve Tissue ProteinsNeuronsNeurotrophin 3Organ SpecificityRatsRats, Sprague-DawleyReceptors, Cell SurfaceRecombinant Fusion ProteinsSemaphorin-3AConceptsFusion proteinBinding sitesGrowth conesDRG neuronsNon-neuronal tissuesExtracellular proteinsF fusion proteinSemaphorin familyDRG growth conesProteinLow nanomolar affinityMajor blood vesselsLigand familyBrainstem neuronsSympathetic neuronsNanomolar affinityNervous systemAxonal pathsBiological activityBlood vesselsNeuronsFamilySitesMesenchymeSemaphorins
1995
Collapsin-induced growth cone collapse mediated by an intracellular protein related to UNC-33
Goshima Y, Nakamura F, Strittmatter P, Strittmatter S. Collapsin-induced growth cone collapse mediated by an intracellular protein related to UNC-33. Nature 1995, 376: 509-514. PMID: 7637782, DOI: 10.1038/376509a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrainCaenorhabditis elegans ProteinsCell LineCell MembraneChick EmbryoGanglia, SpinalGlycoproteinsGTP-Binding ProteinsHelminth ProteinsIntercellular Signaling Peptides and ProteinsMolecular Sequence DataNerve Growth FactorsNerve Tissue ProteinsNeuritesNeuronsOocytesRecombinant Fusion ProteinsSemaphorin-3ASignal TransductionVirulence Factors, BordetellaXenopus laevisConceptsGrowth cone collapseDorsal root ganglion neuronsCollapsin response mediator proteinsCone collapseXenopus laevis oocyte expression systemChick nervous systemGanglion neuronsNervous systemOocyte expression systemUNC-33Inward currentsNeuronal proteinsAxonal pathfindingNeural developmentX. laevis oocytesGrowth conesLaevis oocytesIntracellular proteinsHeterotrimeric GTPMediator proteinsProteinIntracellular componentsNeurons
1992
GAP-43 as a modulator of G protein transduction in the growth cone.
Strittmatter SM. GAP-43 as a modulator of G protein transduction in the growth cone. Perspectives On Developmental Neurobiology 1992, 1: 13-9. PMID: 1364285.Peer-Reviewed Original ResearchConceptsGrowth cone membraneGrowth cone motilityMolecular mechanismsSame cellular functionCone motilityG protein-coupled transmembrane receptorsAmino acid stretchComplex cellular propertiesCone membraneGrowth conesNeurotransmitter releaseGrowth cone functionPossible molecular mechanismsCellular functionsGAP-43 functionHydrophilic proteinProtein transductionGAP-43Transmembrane receptorsGAP-43 regulationCysteine residuesTransduction systemSynaptic plasticityAmino terminusCell shape
1989
A membrane-targeting signal in the amino terminus of the neuronal protein GAP-43
Zuber M, Strittmatter S, Fishman M. A membrane-targeting signal in the amino terminus of the neuronal protein GAP-43. Nature 1989, 341: 345-348. PMID: 2797153, DOI: 10.1038/341345a0.Peer-Reviewed Original ResearchConceptsGrowth cone membraneN-terminusNeuronal protein GAP-43Membrane-targeting signalMembrane-binding abilityTargeting signalsGAP-43Plasma membraneTransduction systemAmino terminusMutational analysisProminent proteinsParticular proteinFusion proteinShort stretchesMembrane distributionLaser scanning confocal microscopyRegulated growthProteinConfocal microscopyEpithelial cellsProtein GAP-43MembraneModification correlatesDiscrete domains