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 contractionCellsNP1
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 phosphataseReceptorsNGR
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