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
2002
Regenerating nerves follow the road more traveled
Fournier AE, Strittmatter SM. Regenerating nerves follow the road more traveled. Nature Neuroscience 2002, 5: 821-822. PMID: 12196804, DOI: 10.1038/nn0902-821.Peer-Reviewed Original Research
2001
Repulsive factors and axon regeneration in the CNS
Fournier A, Strittmatter S. Repulsive factors and axon regeneration in the CNS. Current Opinion In Neurobiology 2001, 11: 89-94. PMID: 11179877, DOI: 10.1016/s0959-4388(00)00178-1.Peer-Reviewed Original ResearchMeSH KeywordsAxonsCentral Nervous SystemHumansMyelin ProteinsMyelin SheathNerve Growth FactorsNerve RegenerationNogo Proteins
2000
Semaphorin3a Enhances Endocytosis at Sites of Receptor–F-Actin Colocalization during Growth Cone Collapse
Fournier A, Nakamura F, Kawamoto S, Goshima Y, Kalb R, Strittmatter S. Semaphorin3a Enhances Endocytosis at Sites of Receptor–F-Actin Colocalization during Growth Cone Collapse. Journal Of Cell Biology 2000, 149: 411-422. PMID: 10769032, PMCID: PMC2175148, DOI: 10.1083/jcb.149.2.411.Peer-Reviewed Original ResearchDendrites 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
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
1998
Semaphorins A and E act as antagonists of neuropilin-1 and agonists of neuropilin-2 receptors
Takahashi T, Nakamura F, Jin Z, Kalb R, Strittmatter S. Semaphorins A and E act as antagonists of neuropilin-1 and agonists of neuropilin-2 receptors. Nature Neuroscience 1998, 1: 487-493. PMID: 10196546, DOI: 10.1038/2203.Peer-Reviewed Original Research
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 vesselsNeuronsFamilySitesMesenchymeSemaphorinsA 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 componentsNeurons