2008
The N-Terminal Domain of Nogo-A Inhibits Cell Adhesion and Axonal Outgrowth by an Integrin-Specific Mechanism
Hu F, Strittmatter SM. The N-Terminal Domain of Nogo-A Inhibits Cell Adhesion and Axonal Outgrowth by an Integrin-Specific Mechanism. Journal Of Neuroscience 2008, 28: 1262-1269. PMID: 18234903, PMCID: PMC2856844, DOI: 10.1523/jneurosci.1068-07.2008.Peer-Reviewed Original ResearchConceptsCell adhesionFocal adhesion kinase activationN-terminal domainAxonal outgrowthInhibits cell adhesionAxonal growth conesCNS axon regenerationKinase activationCertain integrinsIntegrin activatorIntegrin beta1Widespread expressionExtracellular matrixSecond domainAlpha5 integrinUnknown mechanismIntegrinsGrowth conesNogo-A proteinCell linesAlpha6 integrinNogo-66 receptorAxonal growthAdult brainOutgrowth
2006
RanBPM 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 developmentSelective temporal and regional alterations of Nogo-A and small proline-rich repeat protein 1A (SPRR1A) but not Nogo-66 receptor (NgR) occur following traumatic brain injury in the rat
Marklund N, Fulp CT, Shimizu S, Puri R, McMillan A, Strittmatter SM, McIntosh TK. Selective temporal and regional alterations of Nogo-A and small proline-rich repeat protein 1A (SPRR1A) but not Nogo-66 receptor (NgR) occur following traumatic brain injury in the rat. Experimental Neurology 2006, 197: 70-83. PMID: 16321384, PMCID: PMC2849132, DOI: 10.1016/j.expneurol.2005.08.029.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, WesternBrainBrain InjuriesCell CountCornified Envelope Proline-Rich ProteinsDensitometryFunctional LateralityGPI-Linked ProteinsHippocampusImmunohistochemistryMaleMembrane ProteinsMicrotubule-Associated ProteinsMyelin ProteinsNogo ProteinsNogo Receptor 1OligodendrogliaRatsRats, Sprague-DawleyReceptors, Cell SurfaceThalamusConceptsTraumatic brain injurySmall proline-rich repeat protein 1ANogo-66 receptorBrain injuryIpsilateral cortexReticular thalamusNeuN cellsLateral fluid percussion brain injuryTraumatic central nervous system injuryFluid percussion brain injuryAxonal outgrowthCentral nervous system injuryIpsilateral external capsuleOligodendrocyte marker RIPNeuN-positive cellsNeuronal marker NeuNExpression of NogoNervous system injuryWhite matter tractsImportant brain regionsNgR expressionPoor regenerative capacitySPRR1A expressionWestern blot analysisSystem injury
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
Nogo-66 Receptor Prevents Raphespinal and Rubrospinal Axon Regeneration and Limits Functional Recovery from Spinal Cord Injury
Kim JE, Liu BP, Park JH, Strittmatter SM. Nogo-66 Receptor Prevents Raphespinal and Rubrospinal Axon Regeneration and Limits Functional Recovery from Spinal Cord Injury. Neuron 2004, 44: 439-451. PMID: 15504325, DOI: 10.1016/j.neuron.2004.10.015.Peer-Reviewed Original ResearchMeSH Keywords5,7-DihydroxytryptamineAnimalsAxonsBehavior, AnimalBlotting, NorthernBlotting, SouthernBrainCell CountCells, CulturedCloning, MolecularCornified Envelope Proline-Rich ProteinsDesipramineDisease Models, AnimalEvoked Potentials, MotorFemaleGanglia, SpinalGlial Fibrillary Acidic ProteinGlucoseGPI-Linked ProteinsGrowth ConesImmunohistochemistryMiceMice, Inbred C57BLMice, KnockoutMotor ActivityMyelin ProteinsMyelin SheathMyelin-Associated GlycoproteinNerve RegenerationNeuronsNogo ProteinsNogo Receptor 1Phospholipid EthersProteinsPyramidal TractsReceptors, Cell SurfaceRecovery of FunctionSerotoninSerotonin AgentsSpinal CordSpinal Cord InjuriesTime FactorsConceptsAdult CNSNogo-66Spinal cord injuryAdult mammalian CNSNogo-66 receptorDorsal hemisectionDRG neuronsFunctional recoveryRubrospinal fibersCord injuryMyelin inhibitorsComplete transectionCorticospinal fibersMotor functionSpinal cordMotor impairmentAxon regenerationMammalian CNSAxonal growthAxonal outgrowthCNS myelinMiceInhibitory proteinInjuryGrowth cones
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
Nogo-66 receptor antagonist peptide promotes axonal regeneration
GrandPré T, Li S, Strittmatter SM. Nogo-66 receptor antagonist peptide promotes axonal regeneration. Nature 2002, 417: 547-551. PMID: 12037567, DOI: 10.1038/417547a.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAxonsBinding, CompetitiveCentral Nervous SystemCulture Media, ConditionedFemaleGPI-Linked ProteinsGrowth ConesMolecular Sequence DataMotor ActivityMyelin ProteinsMyelin SheathNerve RegenerationNeuritesNogo Receptor 1Peptide FragmentsProtein Structure, TertiaryRatsRats, Sprague-DawleyReceptors, Cell SurfaceSpinal Cord InjuriesConceptsCentral nervous systemAxonal regenerationNogo-66NEP1-40Antagonist peptideAxonal outgrowthNogo-66 receptorPotential therapeutic agentCorticospinal tract regenerationAxonal outgrowth inhibitionCNS myelin inhibitionSignificant axon growthIntrathecal administrationFunctional recoveryCNS injuryCorticospinal tractOutgrowth inhibitorCompetitive antagonistNervous systemMyelin inhibitionTherapeutic agentsAxon growthMonoclonal antibodiesAdult mammalsNogoSmall Proline-Rich Repeat Protein 1A Is Expressed by Axotomized Neurons and Promotes Axonal Outgrowth
Bonilla IE, Tanabe K, Strittmatter SM. Small Proline-Rich Repeat Protein 1A Is Expressed by Axotomized Neurons and Promotes Axonal Outgrowth. Journal Of Neuroscience 2002, 22: 1303-1315. PMID: 11850458, PMCID: PMC6757578, DOI: 10.1523/jneurosci.22-04-01303.2002.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsAxonsAxotomyCell DifferentiationCell Surface ExtensionsCornified Envelope Proline-Rich ProteinsCOS CellsGanglia, SpinalMaleMembrane ProteinsMiceMice, Inbred C57BLNerve CrushNerve RegenerationNeuronsOligonucleotide Array Sequence AnalysisProtein BiosynthesisProteinsRNA, MessengerS100 ProteinsSciatic NerveSciatic NeuropathySpinal Cord InjuriesTransfectionConceptsSmall proline-rich repeat protein 1AProtein 1AAxonal outgrowthMembrane rufflesP21/WAFDifferentiation genesCDNA microarrayNerve regenerationF-actinEpithelial differentiation genesPeripheral axonal damageSciatic nerve regenerationSuccessful nerve regenerationAbility of neuronsSPRR1AGenesUninjured neuronsAxotomized neuronsRange of substratesAxonal damageSensory neuronsOutgrowthNeuronsRufflesAxons
2000
Transduction of Inhibitory Signals by the Axonal Growth Cone
Wang L, Fournier A, Nakamura F, Takahashi T, Kalb R, Strittmatter S. Transduction of Inhibitory Signals by the Axonal Growth Cone. Contemporary Neuroscience 2000, 131-153. DOI: 10.1007/978-1-59259-200-5_6.Peer-Reviewed Original Research
1995
Neuronal Guidance Molecules: Inhibitory and Soluble Factors
Strittmatter S. Neuronal Guidance Molecules: Inhibitory and Soluble Factors. The Neuroscientist 1995, 1: 255-258. DOI: 10.1177/107385849500100502.Peer-Reviewed Original ResearchCell-surface adhesive proteinsMatrix-bound factorsGuidance moleculesImportance of moleculesAxonal guidance factorsAxonal growth conesExtracellular matrix componentsNeural developmentSoluble factorsPhysiological roleSemaphorin familyMolecular levelNeuronal guidance moleculesAdhesive proteinsGrowth conesGuidance factorsMatrix componentsGrowth inhibitorCentral roleAxonal outgrowthCNS myelinAxonal growth inhibitorsAxonal guidance moleculesRegenerationMoleculesNeuronal pathfinding is abnormal in mice lacking the neuronal growth cone protein GAP-43
Strittmatter S, Fankhauser C, Huang P, Mashimo H, Fishman M. Neuronal pathfinding is abnormal in mice lacking the neuronal growth cone protein GAP-43. Cell 1995, 80: 445-452. PMID: 7859286, DOI: 10.1016/0092-8674(95)90495-6.Peer-Reviewed Original Research