2018
Liquid and Hydrogel Phases of PrPC Linked to Conformation Shifts and Triggered by Alzheimer’s Amyloid-β Oligomers
Kostylev MA, Tuttle MD, Lee S, Klein LE, Takahashi H, Cox TO, Gunther EC, Zilm KW, Strittmatter SM. Liquid and Hydrogel Phases of PrPC Linked to Conformation Shifts and Triggered by Alzheimer’s Amyloid-β Oligomers. Molecular Cell 2018, 72: 426-443.e12. PMID: 30401430, PMCID: PMC6226277, DOI: 10.1016/j.molcel.2018.10.009.Peer-Reviewed Original ResearchConceptsAmino-terminal GlyCellular prion proteinProtein phase separationAmyloid-β OligomersPlasma membraneMembraneless organellesAla residuesRecombinant PrPPrion proteinCell surfaceConformation shiftConformational transitionHelical conformationAβ speciesPrPSupSpongiform degenerationEndogenous AβOsOrganellesPrPCSuch domainsSpeciesDomainProteinAβOs
2014
Therapeutic Molecules and Endogenous Ligands Regulate the Interaction between Brain Cellular Prion Protein (PrPC) and Metabotropic Glutamate Receptor 5 (mGluR5)*
Haas LT, Kostylev MA, Strittmatter SM. Therapeutic Molecules and Endogenous Ligands Regulate the Interaction between Brain Cellular Prion Protein (PrPC) and Metabotropic Glutamate Receptor 5 (mGluR5)*. Journal Of Biological Chemistry 2014, 289: 28460-28477. PMID: 25148681, PMCID: PMC4192497, DOI: 10.1074/jbc.m114.584342.Peer-Reviewed Original ResearchMeSH KeywordsAlzheimer DiseaseAmyloid beta-PeptidesAnimalsAntibodiesBinding SitesBiological AssayBrain ChemistryCell MembraneDisease Models, AnimalGene Expression RegulationHEK293 CellsHumansLigandsMiceMice, TransgenicPeptide MappingProtein BindingProtein Structure, TertiaryPrPC ProteinsReceptor, Metabotropic Glutamate 5Recombinant ProteinsSignal TransductionSmall Molecule LibrariesConceptsMetabotropic glutamate receptor 5Glutamate receptor 5Receptor 5Endogenous ligandMouse brainAD transgenic model miceCellular prion proteinAmino acids 91Transgenic model miceSoluble amyloid β (Aβ) oligomersAlzheimer's disease pathophysiologySilent allosteric modulatorsAgonists/antagonistsExtracellular AβOsMGluR5 activitySynthetic AβOsPrion proteinAmyloid-β OligomersModel miceCell membrane preparationsMGluR5Neurotoxic signalsBrain homogenatesAlzheimer's diseaseDisease pathophysiologyThe Nogo Receptor NgR1 Mediates Infection by Mammalian Reovirus
Konopka-Anstadt JL, Mainou BA, Sutherland DM, Sekine Y, Strittmatter SM, Dermody TS. The Nogo Receptor NgR1 Mediates Infection by Mammalian Reovirus. Cell Host & Microbe 2014, 15: 681-691. PMID: 24922571, PMCID: PMC4100558, DOI: 10.1016/j.chom.2014.05.010.Peer-Reviewed Original ResearchConceptsCentral nervous systemReceptor NgR1Reovirus infectionExpression of NgR1Primary cortical neuronsDistinct cell surface moleculesJunctional adhesion molecule ASoluble NgR1Cell surface moleculesNeurotropic virusesCortical neuronsMammalian reovirusesNonsusceptible cellsNervous systemNgR1Null miceSystemic spreadInfectionIndependent receptorsMultiple receptorsReovirus replicationInitial siteReovirus virionsNeuronsReceptors
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 Research
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
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
1993
Mediation by G Proteins of Signals That Cause Collapse of Growth Cones
Igarashi M, Strittmatter S, Vartanian T, Fishman M. Mediation by G Proteins of Signals That Cause Collapse of Growth Cones. Science 1993, 259: 77-79. PMID: 8418498, DOI: 10.1126/science.8418498.Peer-Reviewed Original Research
1990
G0 is a major growth cone protein subject to regulation by GAP-43
Strittmatter S, Valenzuela D, Kennedy T, Neer E, Fishman M. G0 is a major growth cone protein subject to regulation by GAP-43. Nature 1990, 344: 836-841. PMID: 2158629, DOI: 10.1038/344836a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrain ChemistryCell MembraneGAP-43 ProteinGrowth SubstancesGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Guanosine TriphosphateMembrane GlycoproteinsMolecular Sequence DataMolecular WeightNerve Tissue ProteinsPeptide FragmentsProtein BindingRatsReceptors, Cell SurfaceReceptors, NeurotransmitterSequence Homology, Nucleic AcidSignal TransductionThionucleotidesConceptsTransmembrane receptorsNeuronal growth cone membraneAmino-terminal domainGTP-binding proteinsGrowth cone membraneExtracellular signalsGrowth cone proteinGAP-43Cone membraneGrowth conesCone proteinNeuronal growthProteinS bindingMajor componentG0ReceptorsGTPRegulationIntracellularBindingMembraneDomain
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
1983
[3H]Captopril binding to membrane associated angiotensin converting enzyme
Strittmatter S, Kapiloff M, Snyder S. [3H]Captopril binding to membrane associated angiotensin converting enzyme. Biochemical And Biophysical Research Communications 1983, 112: 1027-1033. PMID: 6303332, DOI: 10.1016/0006-291x(83)91721-7.Peer-Reviewed Original Research