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 functionRanBPM 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
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