2019
Plexina2 and CRMP2 Signaling Complex Is Activated by Nogo-A-Liganded Ngr1 to Restrict Corticospinal Axon Sprouting after Trauma
Sekine Y, Algarate PT, Cafferty WBJ, Strittmatter SM. Plexina2 and CRMP2 Signaling Complex Is Activated by Nogo-A-Liganded Ngr1 to Restrict Corticospinal Axon Sprouting after Trauma. Journal Of Neuroscience 2019, 39: 3204-3216. PMID: 30804090, PMCID: PMC6788813, DOI: 10.1523/jneurosci.2996-18.2019.Peer-Reviewed Original ResearchConceptsCNS traumaNeural repairMouse cervical spinal cordSpinal cord traumaCervical spinal cordNon-neuronal cellsInteraction of NogoAxon growth inhibitionAxonal guidance mechanismsNeurological recoveryAxonal sproutingCNS pathwaysCord traumaFunctional recoveryAxon sproutingSpinal cordNgR1 functionUnilateral pyramidotomyAxon regenerationAdult traumaNgR1TraumaAxon growthNogoCytoplasmic mediators
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
2010
Chapter 240 Semaphorins and their Receptors in Vertebrates and Invertebrates
Schmidt E, Togashi H, Strittmatter S. Chapter 240 Semaphorins and their Receptors in Vertebrates and Invertebrates. 2010, 1961-1966. DOI: 10.1016/b978-0-12-374145-5.00240-0.Peer-Reviewed Original ResearchExpression of Sema4DDorsal root gangliaTypes of neuronsNon-neuronal cellsT lymphocyte activationCentral nervous system developmentMalignant lung cellsNeuronal cell migrationAxon guidance factorsRoot gangliaNervous system developmentCardiovascular abnormalitiesImmune responseNerve bundlesAxoplasmic transportNervous systemImmune systemCardiovascular systemLung cellsAdult animalsAxonsReduced levelsSemaphorinsGuidance factorsCell migration
2003
Chapter 267 Semaphorins and their Receptors in Vertebrates and Invertebrates
Schmidt E, Togashi H, Strittmatter S. Chapter 267 Semaphorins and their Receptors in Vertebrates and Invertebrates. 2003, 877-881. DOI: 10.1016/b978-012124546-7/50628-8.Peer-Reviewed Original ResearchFunctions of semaphorinsNervous system developmentMalignant lung cellsCentral nervous system developmentVertebrate semaphorinsNon-neuronal cellsCytoplasmic localizationAdult tissuesSemaphorin familyExpression of Sema4DWidespread expressionSemaphorinsOlfactory neuronsGuidance cuesCertain receptorsGrowth conesT lymphocyte activationRetraction of axonsAntagonistic activityReduced levelsCardiovascular abnormalitiesCertain neuronsAttractantsImmune systemLung cells
1994
An 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
1991
Growth cone transduction: Go and GAP-43
STRITTMATTER S, VALENZUELA D, VARTANIAN T, SUDO Y, ZUBER M, FISHMAN M. Growth cone transduction: Go and GAP-43. Journal Of Cell Science. Supplement 1991, 1991: 27-33. PMID: 1840457, DOI: 10.1242/jcs.1991.supplement_15.5.Peer-Reviewed Original ResearchConceptsGrowth cone membraneExtracellular signalsIntracellular proteinsGrowth cone targetingNon-cytoskeletal proteinsG protein familyG-protein-linked receptorsAppropriate synaptic targetsComplex brain architectureCone membraneGrowth conesProtein-linked receptorsGrowth cone functionNeuronal growth conesMembrane associationProtein familyNon-neuronal cellsGAP-43Filopodial formationAmino terminusCell shapeExtrinsic cluesSecond messengerGrowth proteinsProtein