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 vesselsNeuronsFamilySitesMesenchymeSemaphorins
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
1989
A membrane-targeting signal in the amino terminus of the neuronal protein GAP-43
Zuber M, Strittmatter S, Fishman M. A membrane-targeting signal in the amino terminus of the neuronal protein GAP-43. Nature 1989, 341: 345-348. PMID: 2797153, DOI: 10.1038/341345a0.Peer-Reviewed Original ResearchConceptsGrowth cone membraneN-terminusNeuronal protein GAP-43Membrane-targeting signalMembrane-binding abilityTargeting signalsGAP-43Plasma membraneTransduction systemAmino terminusMutational analysisProminent proteinsParticular proteinFusion proteinShort stretchesMembrane distributionLaser scanning confocal microscopyRegulated growthProteinConfocal microscopyEpithelial cellsProtein GAP-43MembraneModification correlatesDiscrete domains