2021
Spreading of Alzheimer tau seeds is enhanced by aging and template matching with limited impact of amyloid-β
Nies SH, Takahashi H, Herber CS, Huttner A, Chase A, Strittmatter SM. Spreading of Alzheimer tau seeds is enhanced by aging and template matching with limited impact of amyloid-β. Journal Of Biological Chemistry 2021, 297: 101159. PMID: 34480901, PMCID: PMC8477193, DOI: 10.1016/j.jbc.2021.101159.Peer-Reviewed Original ResearchConceptsTau seedsAlzheimer's diseaseAD model miceWT mouse brainPathological tauSynaptic lossTau accumulationWT miceMouse tauTau pathologyTau burdenModel miceTau inclusionsPharmacological interventionsAD riskCognitive declineMouse brainTau aggregatesPyk2 kinaseKnowledge of factorsKinase inhibitorsMiceFyn kinase inhibitorAβMouse aging
2017
Identification of Intrinsic Axon Growth Modulators for Intact CNS Neurons after Injury
Fink KL, López-Giráldez F, Kim IJ, Strittmatter SM, Cafferty WB. Identification of Intrinsic Axon Growth Modulators for Intact CNS Neurons after Injury. Cell Reports 2017, 18: 2687-2701. PMID: 28297672, PMCID: PMC5389739, DOI: 10.1016/j.celrep.2017.02.058.Peer-Reviewed Original ResearchConceptsSpinal cord injuryCentral nervous systemFunctional recoveryIntact neuronsAdult mammalian central nervous systemPartial spinal cord injuryInjury-induced sproutingUnilateral brainstem lesionsGreater functional recoverySpontaneous functional recoveryCorticospinal motor neuronsCorticospinal tract axonsMammalian central nervous systemWild-type miceNew synapse formationGrowth modulatorsAdjacent injuryBrainstem lesionsCord injuryFunctional deficitsIntact circuitryCNS neuronsMotor neuronsCircuit plasticityNervous system
2008
Release of MICAL Autoinhibition by Semaphorin-Plexin Signaling Promotes Interaction with Collapsin Response Mediator Protein
Schmidt EF, Shim SO, Strittmatter SM. Release of MICAL Autoinhibition by Semaphorin-Plexin Signaling Promotes Interaction with Collapsin Response Mediator Protein. Journal Of Neuroscience 2008, 28: 2287-2297. PMID: 18305261, PMCID: PMC2846290, DOI: 10.1523/jneurosci.5646-07.2008.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsCell Adhesion MoleculesCell Line, TransformedChick EmbryoCytoskeletal ProteinsFlavin-Adenine DinucleotideGanglia, SpinalGenetic VectorsHIVHumansImmunoprecipitationIntracellular Signaling Peptides and ProteinsLIM Domain ProteinsMembrane GlycoproteinsMicrofilament ProteinsMixed Function OxygenasesMutationNerve Tissue ProteinsNeuritesNeuronsPeptide FragmentsProtein BindingSemaphorin-3ASemaphorinsSignal TransductionTransfectionConceptsCollapsin response mediator proteinsMediator proteinsCytoplasmic proteinsEnzymatic domainsCatalytic domainPlexin functionPlexin receptorsTerminal domainMICALPromotes interactionAxon guidanceNeuronal developmentAxonal guidanceEnzymatic activityProteinAutoinhibitionDomainPlexinsSignalingSemaphorinsActivatorAssociatesInteractionActivityActivation
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 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
A Neutralizing Anti-Nogo66 Receptor Monoclonal Antibody Reverses Inhibition of Neurite Outgrowth by Central Nervous System Myelin*
Li W, Walus L, Rabacchi SA, Jirik A, Chang E, Schauer J, Zheng BH, Benedetti NJ, Liu BP, Choi E, Worley D, Silvian L, Mo W, Mullen C, Yang W, Strittmatter SM, Sah DW, Pepinsky B, Lee DH. A Neutralizing Anti-Nogo66 Receptor Monoclonal Antibody Reverses Inhibition of Neurite Outgrowth by Central Nervous System Myelin*. Journal Of Biological Chemistry 2004, 279: 43780-43788. PMID: 15297463, DOI: 10.1074/jbc.m401803200.Peer-Reviewed Original ResearchConceptsOligodendrocyte myelin glycoproteinRat dorsal root ganglion neuronsDorsal root ganglion neuronsMonoclonal antibodiesMyelin glycoproteinNeurite outgrowthMyelin proteinsUseful therapeutic approachCNS myelin substrateNogo66 receptorCentral nervous system myelinGanglion neuronsTherapeutic approachesCNS repairMyelin substrateCentral nervous system myelin proteinsInhibitory effectNgR1AntibodiesNeurite growthMyelinSystem myelinReverses inhibitionMolecular epitopes
2003
Fibroblast Growth Factor-Inducible-14 Is Induced in Axotomized Neurons and Promotes Neurite Outgrowth
Tanabe K, Bonilla I, Winkles JA, Strittmatter SM. Fibroblast Growth Factor-Inducible-14 Is Induced in Axotomized Neurons and Promotes Neurite Outgrowth. Journal Of Neuroscience 2003, 23: 9675-9686. PMID: 14573547, PMCID: PMC6740475, DOI: 10.1523/jneurosci.23-29-09675.2003.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxotomyGanglia, SpinalGene Expression ProfilingGene Expression RegulationHumansMaleMembrane ProteinsMiceMice, Inbred C57BLNerve RegenerationNeuritesNeuronsOligonucleotide Array Sequence AnalysisPC12 CellsPseudopodiaRac1 GTP-Binding ProteinRatsReceptors, Tumor Necrosis FactorRNA, MessengerSciatic NeuropathyTWEAK ReceptorConceptsFibroblast Growth Factor-Inducible 14Dorsal root gangliaDozens of genesDRG neuronsRho family GTPasesPC12 cellsGene expression patternsNeurite outgrowthAxotomized neuronsMRNA expression profilesPromotes Neurite OutgrowthNerve growth factor treatmentRac1 inactivationRac1 GTPaseExpression patternsExpression profilesMicroarray analysisAxotomized DRG neuronsOverexpression of Fn14Rac1 activationNorthern analysisSciatic nerve injurySciatic nerve transectionCoordinated shiftImmunoprecipitation studiesRho Kinase Inhibition Enhances Axonal Regeneration in the Injured CNS
Fournier AE, Takizawa BT, Strittmatter SM. Rho Kinase Inhibition Enhances Axonal Regeneration in the Injured CNS. Journal Of Neuroscience 2003, 23: 1416-1423. PMID: 12598630, PMCID: PMC6742251, DOI: 10.1523/jneurosci.23-04-01416.2003.Peer-Reviewed Original ResearchMeSH KeywordsADP Ribose TransferasesAmidesAnimalsAxonsBotulinum ToxinsCells, CulturedChick EmbryoEnzyme InhibitorsFemaleGanglia, SpinalIntracellular Signaling Peptides and ProteinsMotor ActivityMyelin ProteinsNerve RegenerationNeuritesNogo ProteinsPC12 CellsProtein Serine-Threonine KinasesPyridinesRatsRats, Sprague-DawleyRho GTP-Binding ProteinsRho-Associated KinasesSpinal Cord InjuriesConceptsAxonal regenerationAdult ratsNeurite outgrowthCorticospinal tract lesionsNeurite outgrowth inhibitorChick DRG neuronsRho-kinase inhibitionCST fibersDRG neuronsCST lesionLocomotor recoveryTract lesionsSpinal cordOutgrowth inhibitorInhibits neurite outgrowthNogo-66Activity levelsMyelinKinase inhibitionLesionsActivation of RhoRatsC3 transferaseInhibition of p160ROCKInhibitors
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 phosphataseReceptorsNGRMyelin-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 PhospholipasesNogo-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 mammalsNogo
2000
Dendrites go up, axons go down
Strittmatter S. Dendrites go up, axons go down. Nature 2000, 404: 557-559. PMID: 10766224, DOI: 10.1038/35007181.Peer-Reviewed Original Research
1997
A novel action of collapsin: Collapsin‐1 increases antero‐ and retrograde axoplasmic transport independently of growth cone collapse
Goshima Y, Kawakami T, Hori H, Sugiyama Y, Takasawa S, Hashimoto Y, Kagoshima‐Maezono M, Takenaka T, Misu Y, Strittmatter S. A novel action of collapsin: Collapsin‐1 increases antero‐ and retrograde axoplasmic transport independently of growth cone collapse. Developmental Neurobiology 1997, 33: 316-328. PMID: 9298768, DOI: 10.1002/(sici)1097-4695(199709)33:3<316::aid-neu9>3.0.co;2-4.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonal TransportCells, CulturedDose-Response Relationship, DrugGanglia, SpinalGlycoproteinsGTP-Binding ProteinsIntercellular Signaling Peptides and ProteinsMiceMice, Inbred C57BLMyelin ProteinsNerve Growth FactorsNeuritesOrganellesPeptidesPertussis ToxinSemaphorin-3AVirulence Factors, BordetellaWasp VenomsRac1 Mediates Collapsin-1-Induced Growth Cone Collapse
Jin Z, Strittmatter SM. Rac1 Mediates Collapsin-1-Induced Growth Cone Collapse. Journal Of Neuroscience 1997, 17: 6256-6263. PMID: 9236236, PMCID: PMC6568359, DOI: 10.1523/jneurosci.17-16-06256.1997.Peer-Reviewed Original ResearchADP Ribose TransferasesAnimalsBotulinum ToxinsCdc42 GTP-Binding ProteinCell Cycle ProteinsCells, CulturedChick EmbryoGanglia, SpinalGlycoproteinsGTP-Binding ProteinsLysophospholipidsMyelin ProteinsNerve Growth FactorsNeuritesRac GTP-Binding ProteinsRecombinant ProteinsRho GTP-Binding ProteinsSemaphorin-3ASensitivity and SpecificityThrombin
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 componentsNeuronsAn activated mutant of the a subunit of Go increases neurite outgrowth via protein kinase C
Xie R, Li L, Goshima Y, Strittmatter S. An activated mutant of the a subunit of Go increases neurite outgrowth via protein kinase C. Brain Research 1995, 87: 77-86. PMID: 7554235, DOI: 10.1016/0165-3806(95)00061-h.Peer-Reviewed Original ResearchMeSH KeywordsAlkaloidsAnimalsCalciumCalcium Channel BlockersCalcium-Transporting ATPasesDose-Response Relationship, DrugEnzyme InhibitorsEthers, CyclicGallic AcidGTP-Binding ProteinsMutationNeuritesOkadaic AcidPC12 CellsProtein Kinase CRatsSecond Messenger SystemsStaurosporineTerpenesThapsigarginTransfectionConceptsProtein kinase CAlpha oKinase CNeurite outgrowthNeuronal growth cone membraneProtein phosphatase inhibitorSignal transduction cascadeDifferent signal transduction cascadesNeurite extensionGrowth cone membranePhorbol ester treatmentPhosphatase inhibitorTransduction cascadeOkadaic acidEster treatmentPhorbol esterCone membraneNeurite elongationMutantsIntracellular mechanismsKinase inhibitorsOutgrowthSubunitsIntracellular calcium levelsPresence of agents
1994
GAP-43 amino terminal peptides modulate growth cone morphology and neurite outgrowth
Strittmatter S, Igarashi M, Fishman M. GAP-43 amino terminal peptides modulate growth cone morphology and neurite outgrowth. Journal Of Neuroscience 1994, 14: 5503-5513. PMID: 8083750, PMCID: PMC6577098, DOI: 10.1523/jneurosci.14-09-05503.1994.Peer-Reviewed Original ResearchConceptsGAP-43G-protein activityPertussis toxinNeuronal growth-associated protein GAP-43Neurite outgrowthGrowth-associated protein GAP-43Dorsal root ganglion cellsG protein-mediated eventsGrowth cone membraneDorsal root gangliaProtein GAP-43N1E-115 neuroblastoma cellsChick dorsal root ganglion cellsChick dorsal root gangliaNeurite extensionCone membraneEmbryonic chick dorsal root gangliaRoot gangliaGanglion cellsRetinal neuronsPeptide stimulationGrowth cone collapseGrowth cone morphologyNeuroblastoma cellsPotential modulatorsActivated mutants of the alpha subunit of G(o) promote an increased number of neurites per cell
Strittmatter S, Fishman M, Zhu X. Activated mutants of the alpha subunit of G(o) promote an increased number of neurites per cell. Journal Of Neuroscience 1994, 14: 2327-2338. PMID: 8158271, PMCID: PMC6577129, DOI: 10.1523/jneurosci.14-04-02327.1994.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCell LineChlorocebus aethiopsDNA PrimersDose-Response Relationship, DrugGTP-Binding ProteinsIntercellular Signaling Peptides and ProteinsKineticsMacromolecular SubstancesMolecular Sequence DataMutagenesis, Site-DirectedNeuritesNeuroblastomaPC12 CellsPeptidesPertussis ToxinPoint MutationTransfectionTumor Cells, CulturedVirulence Factors, BordetellaWasp VenomsConceptsAlpha oNumber of neuritesPertussis toxin-sensitive G proteinToxin-sensitive G proteinGrowth conesAlpha subunitG proteinsNeurite outgrowthTotal neurite lengthN1E-115 cellsAlpha i2Activated alpha subunitNeuroblastoma cellsNeurite numberNeurite lengthNeuronal growth conesAlpha sOncogenic mutationsActivation stateO mutantsActivationNeuritesCellsPoint mutationsSubunits
1992
GAP‐43 as a plasticity protein in neuronal form and repair
Strittmatter S, Vartanian T, Fishman M. GAP‐43 as a plasticity protein in neuronal form and repair. Developmental Neurobiology 1992, 23: 507-520. PMID: 1431834, DOI: 10.1002/neu.480230506.Peer-Reviewed Original ResearchConceptsGrowth cone membraneShort amino-terminal sequenceG proteinsCone membranePlasticity proteinsSpecific cellular domainsAmino-terminal sequenceMembrane localizationG-protein activityGAP-43Cellular domainsProtein activityCell shapeIntracellular proteinsActin filamentsBeta subunitRemarkable plasticityNeural developmentSuch plasticityTerminal sequenceProteinNeurite extensionGuanine nucleotidesNeurite growthAxonal extensionGAP-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