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 function
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
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 contractionCellsNP1Structure and axon outgrowth inhibitor binding of the Nogo‐66 receptor and related proteins
Barton WA, Liu BP, Tzvetkova D, Jeffrey PD, Fournier AE, Sah D, Cate R, Strittmatter SM, Nikolov DB. Structure and axon outgrowth inhibitor binding of the Nogo‐66 receptor and related proteins. The EMBO Journal 2003, 22: 3291-3302. PMID: 12839991, PMCID: PMC165649, DOI: 10.1093/emboj/cdg325.Peer-Reviewed Original ResearchDelayed Systemic Nogo-66 Receptor Antagonist Promotes Recovery from Spinal Cord Injury
Li S, Strittmatter SM. Delayed Systemic Nogo-66 Receptor Antagonist Promotes Recovery from Spinal Cord Injury. Journal Of Neuroscience 2003, 23: 4219-4227. PMID: 12764110, PMCID: PMC6741116, DOI: 10.1523/jneurosci.23-10-04219.2003.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAxonsAxotomyBehavior, AnimalCornified Envelope Proline-Rich ProteinsFemaleGanglia, SpinalGPI-Linked ProteinsInjections, SubcutaneousIntralaminar Thalamic NucleiMembrane ProteinsMiceMice, Inbred C57BLMolecular Sequence DataMolecular WeightMotor ActivityMyelin ProteinsNerve FibersNerve RegenerationNogo Receptor 1Peptide FragmentsProtein BiosynthesisProteinsPyramidal TractsReceptors, Cell SurfaceSerotoninSpinal CordSpinal Cord InjuriesConceptsSpinal cord injuryCord injuryCorticospinal axonsThoracic spinal cord injuryTherapeutic time windowSpinal cord hemisectionSpinal cord traumaCorticospinal tract axonsAdult mammalian CNSNogo-66 receptorOligodendrocyte myelin glycoproteinCNS axonal injuryCord lesionsSubcutaneous treatmentSystemic therapyCord hemisectionCord traumaIntrathecal applicationLocal therapyLocomotor recoveryFunctional recoverySerotonergic fibersAxonal injuryReceptor antagonistAxon sprouting
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 phosphataseReceptorsNGRNogo-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
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
2000
Identification of the Nogo inhibitor of axon regeneration as a Reticulon protein
GrandPré T, Nakamura F, Vartanian T, Strittmatter S. Identification of the Nogo inhibitor of axon regeneration as a Reticulon protein. Nature 2000, 403: 439-444. PMID: 10667797, DOI: 10.1038/35000226.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAxonsCattleCell DivisionCell LineCentral Nervous SystemChick EmbryoCloning, MolecularConsensus SequenceEscherichia coliGrowth InhibitorsHumansMembrane ProteinsMolecular Sequence DataMyelin ProteinsNerve RegenerationNogo ProteinsOligodendrogliaPC12 CellsRatsRecombinant ProteinsSequence Homology, Amino AcidConceptsCentral nervous systemPeripheral nervous systemCNS white matterAxonal regenerationAxon regenerationNervous systemWhite matterAdult central nervous systemMammalian axon regenerationIN-1 antibodiesReticulon 1Dorsal root ganglion growth conesFunctional recoverySpinal cordSchwann cellsCNS axonsExtracellular domainAxonal extensionNogoAxon extensionGrowth conesOligodendrocytesInhibitory activityReticulon 4Moderate degree
1999
A PDZ Protein Regulates the Distribution of the Transmembrane Semaphorin, M-SemF*
Wang L, Kalb R, Strittmatter S. A PDZ Protein Regulates the Distribution of the Transmembrane Semaphorin, M-SemF*. Journal Of Biological Chemistry 1999, 274: 14137-14146. PMID: 10318831, DOI: 10.1074/jbc.274.20.14137.Peer-Reviewed Original ResearchConceptsPDZ proteinsG-protein signal transduction pathwaySingle PDZ domainDetergent-resistant aggregatesSignal transduction pathwaysAxon guidance signalsPDZ domainCytoplasmic domainProtein interactionsTransduction pathwaysTransmembrane semaphorinsExpression studiesFour residuesGAIPSubcellular distributionHEK293 cellsSemaphorin familyCell surfaceProteinNeural proteinsGuidance signalsInteractsGIPCPDZSemaphorins
1996
A Family of Rat CRMP Genes Is Differentially Expressed in the Nervous System
Wang LH, Strittmatter SM. A Family of Rat CRMP Genes Is Differentially Expressed in the Nervous System. Journal Of Neuroscience 1996, 16: 6197-6207. PMID: 8815901, PMCID: PMC6579169, DOI: 10.1523/jneurosci.16-19-06197.1996.Peer-Reviewed Original ResearchMeSH KeywordsAgingAmino Acid SequenceAnimalsAnimals, NewbornEmbryonic and Fetal DevelopmentGanglia, SensoryGanglia, SympatheticGene ExpressionHumansIntercellular Signaling Peptides and ProteinsIsomerismMolecular Sequence DataMultigene FamilyNerve Tissue ProteinsNervous System Physiological PhenomenaProsencephalonRatsSemaphorin-3ASpinal CordP2Y1 purinergic receptors in sensory neurons: contribution to touch-induced impulse generation.
Nakamura F, Strittmatter SM. P2Y1 purinergic receptors in sensory neurons: contribution to touch-induced impulse generation. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 10465-10470. PMID: 8816824, PMCID: PMC38408, DOI: 10.1073/pnas.93.19.10465.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsApyraseChickensFemaleGanglia, SpinalMembrane PotentialsMolecular Sequence DataNerve FibersNeurons, AfferentOocytesPhysical StimulationPurinergic P2 Receptor AgonistsPyridoxal PhosphateRatsReceptors, Purinergic P2Receptors, Purinergic P2X3Receptors, Purinergic P2Y1RNA, MessengerSciatic NerveSkinSuraminTime FactorsTranscription, GeneticXenopus laevisConceptsNerve endingsPurinergic receptorsSensory neuronsAction potentialsSmall fiber sensory neuronsDorsal root ganglion neuronsDistal nerve endingsSensory action potentialsPeripheral nerve endingsSensory nerve fibersP2 receptor agonistsP2Y1 purinergic receptorRelease of ATPP2 antagonistsGanglion neuronsReceptor agonistNerve fibersLight touchNeuronsXenopus laevis oocytesSomatic sensationsReceptorsImpulse generationExtracellular spaceLaevis oocytes
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
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 modulatorsAn intrinsic guanine nucleotide exchange inhibitor in Gi2 alpha. Significance of G-protein self-suppression which antagonizes receptor signal.
Okamoto T, Murayama Y, Strittmatter SM, Katada T, Asano S, Ogata E, Nishimoto I. An intrinsic guanine nucleotide exchange inhibitor in Gi2 alpha. Significance of G-protein self-suppression which antagonizes receptor signal. Journal Of Biological Chemistry 1994, 269: 13756-13759. PMID: 8188651, DOI: 10.1016/s0021-9258(17)36711-x.Peer-Reviewed Original ResearchConceptsIntrinsic guanineHeterotrimeric G-protein familyG proteinsReceptor signalsGi2 alphaG protein familyProto-oncogene productProtein familyC-terminusResidues 338Alpha subunitReceptor polypeptideBasal activityAlpha activationPolypeptideGuanineReceptor stimulationAlphaExchange inhibitorInhibitorsReceptorsTerminusSubunitsProteinGi2Activated 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 mutationsSubunitsAn amino-terminal domain of the growth-associated protein gap-43 mediates its effects on filopodial formation and cell spreading
Strittmatter S, Valenzuela D, Fishman M. An amino-terminal domain of the growth-associated protein gap-43 mediates its effects on filopodial formation and cell spreading. Journal Of Cell Science 1994, 107: 195-204. PMID: 8175908, DOI: 10.1242/jcs.107.1.195.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCarcinoma, Squamous CellCell LineCell MembraneCell MovementChlorocebus aethiopsColforsinCyclic AMPGAP-43 ProteinGene ExpressionGenetic VectorsGrowth SubstancesHumansMembrane GlycoproteinsMolecular Sequence DataNerve Tissue ProteinsNeuronsPlasmidsSequence DeletionStructure-Activity RelationshipTransfectionTumor Cells, CulturedConceptsAmino-terminal domainCell shapeAmino terminusFusion proteinA431 cellsCell shape changesCOS-7 cellsProtein kinase CGrowth cone membraneCell surface activityLevel of forskolinMutant proteinsHeterotrimeric GTPNon-neuronal cellsG protein stimulationProtein mutantsChimeric geneGAP-43Filopodial formationFunctional domainsCell spreadingBind calmodulinKinase CMajor substratePeptide stretch
1993
Functional expression of sodium channel mutations identified in families with periodic paralysis
Cannon S, Strittmatter S. Functional expression of sodium channel mutations identified in families with periodic paralysis. Neuron 1993, 10: 317-326. PMID: 8382500, DOI: 10.1016/0896-6273(93)90321-h.Peer-Reviewed Original ResearchConceptsSodium channel alpha subunitChannel alpha subunitAlpha subunitFunctional expressionMammalian cell linesSame functional defectSodium channel mutationsBenign polymorphismsSingle-channel conductanceMutationsChannel mutationsCell linesSubunitsMyotubesFunctional defectsPeriodic paralysisProcess of inactivationPotassium dependenceNoninactivating componentNew regionsInactivationExpressionPolymorphismSodium currentFamily
1990
G0 is a major growth cone protein subject to regulation by GAP-43
Strittmatter S, Valenzuela D, Kennedy T, Neer E, Fishman M. G0 is a major growth cone protein subject to regulation by GAP-43. Nature 1990, 344: 836-841. PMID: 2158629, DOI: 10.1038/344836a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrain ChemistryCell MembraneGAP-43 ProteinGrowth SubstancesGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Guanosine TriphosphateMembrane GlycoproteinsMolecular Sequence DataMolecular WeightNerve Tissue ProteinsPeptide FragmentsProtein BindingRatsReceptors, Cell SurfaceReceptors, NeurotransmitterSequence Homology, Nucleic AcidSignal TransductionThionucleotidesConceptsTransmembrane receptorsNeuronal growth cone membraneAmino-terminal domainGTP-binding proteinsGrowth cone membraneExtracellular signalsGrowth cone proteinGAP-43Cone membraneGrowth conesCone proteinNeuronal growthProteinS bindingMajor componentG0ReceptorsGTPRegulationIntracellularBindingMembraneDomain