2019
Anti‐PrPC antibody rescues cognition and synapses in transgenic alzheimer mice
Cox TO, Gunther EC, Brody AH, Chiasseu MT, Stoner A, Smith LM, Haas LT, Hammersley J, Rees G, Dosanjh B, Groves M, Gardener M, Dobson C, Vaughan T, Chessell I, Billinton A, Strittmatter SM. Anti‐PrPC antibody rescues cognition and synapses in transgenic alzheimer mice. Annals Of Clinical And Translational Neurology 2019, 6: 554-574. PMID: 30911579, PMCID: PMC6414488, DOI: 10.1002/acn3.730.Peer-Reviewed Original ResearchConceptsAPP/PS1 transgenic micePS1 transgenic miceBrain antibodiesTransgenic miceDisease pathophysiologyDisease pathologyTransgenic Alzheimer's miceAlzheimer's disease pathologyAlzheimer's disease pathophysiologyHuman monoclonal antibodyPreclinical therapeutic efficacyHigh-affinity receptorAmyloid-beta oligomersLast doseTransgenic brainsPlaque pathologyAlzheimer's micePreclinical dataSynaptic damageAnti-PrPc antibodiesSynaptic densityIntraperitoneal dosingBrain biochemistryCentral synapsesTherapeutic efficacy
2016
Binding Sites for Amyloid-β Oligomers and Synaptic Toxicity
Smith LM, Strittmatter SM. Binding Sites for Amyloid-β Oligomers and Synaptic Toxicity. Cold Spring Harbor Perspectives In Medicine 2016, 7: a024075. PMID: 27940601, PMCID: PMC5411685, DOI: 10.1101/cshperspect.a024075.Peer-Reviewed Original ResearchConceptsAlzheimer's diseaseAβ oligomersSoluble Aβ oligomersFibrillary amyloidNeuronal impairmentSynaptic dysfunctionAD pathogenesisSynaptic toxicityAmyloid-β OligomersCellular prion proteinNeuronal cascadesFurther studiesCell surface proteinsDiseaseAβPrion proteinOligomer toxicityToxicityDysfunctionMolecular basisPathogenesisDementiaProteinPlaquesImpairment
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 pathophysiology
2011
Cartilage Acidic Protein–1B (LOTUS), an Endogenous Nogo Receptor Antagonist for Axon Tract Formation
Sato Y, Iketani M, Kurihara Y, Yamaguchi M, Yamashita N, Nakamura F, Arie Y, Kawasaki T, Hirata T, Abe T, Kiyonari H, Strittmatter SM, Goshima Y, Takei K. Cartilage Acidic Protein–1B (LOTUS), an Endogenous Nogo Receptor Antagonist for Axon Tract Formation. Science 2011, 333: 769-773. PMID: 21817055, PMCID: PMC3244695, DOI: 10.1126/science.1204144.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonsBinding SitesCalcium-Binding ProteinsCell LineCells, CulturedGPI-Linked ProteinsGrowth ConesHumansImmunohistochemistryLigandsMiceMice, Inbred ICRMyelin ProteinsNogo ProteinsNogo Receptor 1Olfactory PathwaysProsencephalonProtein BindingReceptors, Cell SurfaceSignal TransductionConceptsTract formationNogo receptor 1Axon growth inhibitorsProtein 1BEndogenous antagonismAxon tract formationReceptor antagonistGrowth cone collapseAxonal projectionsCircuitry formationNeural circuitry formationMouse brainReceptor 1LOT formationNeural regenerationNgR1Key moleculesCone collapseMiceFluorophore-assisted light inactivationGrowth inhibitorAntagonistBrainMyelinNogo
2009
Cellular Prion Protein Mediates the Toxicity of β-Amyloid Oligomers: Implications for Alzheimer Disease
Nygaard HB, Strittmatter SM. Cellular Prion Protein Mediates the Toxicity of β-Amyloid Oligomers: Implications for Alzheimer Disease. JAMA Neurology 2009, 66: 1325-1328. PMID: 19901162, PMCID: PMC2849161, DOI: 10.1001/archneurol.2009.223.Peer-Reviewed Original ResearchMeSH KeywordsAlzheimer DiseaseAmyloid beta-PeptidesAnimalsBinding SitesHumansPeptide FragmentsPrPC ProteinsConceptsAlzheimer's diseaseCellular prion proteinPathogenesis of ADBeta-amyloid plaquesAge-related dementiaSoluble oligomeric assembliesPrion proteinPotential clinical implicationsBeta-amyloid oligomersΒ-amyloid oligomersHigh-affinity receptorCommon causeSynaptic plasticityTherapeutic interventionsClinical implicationsAbeta oligomersNovel targetRecent evidenceToxic effectsDiseasePathogenesisDementiaAbetaPlaquesBrainLGI1-associated epilepsy through altered ADAM23-dependent neuronal morphology
Owuor K, Harel NY, Englot DJ, Hisama F, Blumenfeld H, Strittmatter SM. LGI1-associated epilepsy through altered ADAM23-dependent neuronal morphology. Molecular And Cellular Neuroscience 2009, 42: 448-457. PMID: 19796686, PMCID: PMC2783222, DOI: 10.1016/j.mcn.2009.09.008.Peer-Reviewed Original ResearchConceptsNeuronal morphologyAutosomal dominant partial epilepsyCA1 pyramidal neuronsSeizure thresholdSpontaneous seizuresPartial epilepsyPyramidal neuronsDendritic arborizationLGI1PSD-95LGI1 geneEpilepsy genesADAM23ADPEAFADAM22EpilepsyNeurite outgrowthIon channelsBrain genesUnbiased screenAuditory featuresOutgrowthSeizuresArborizationRelated proteins
2005
Nogo-A Interacts with the Nogo-66 Receptor through Multiple Sites to Create an Isoform-Selective Subnanomolar Agonist
Hu F, Liu BP, Budel S, Liao J, Chin J, Fournier A, Strittmatter SM. Nogo-A Interacts with the Nogo-66 Receptor through Multiple Sites to Create an Isoform-Selective Subnanomolar Agonist. Journal Of Neuroscience 2005, 25: 5298-5304. PMID: 15930377, PMCID: PMC2855126, DOI: 10.1523/jneurosci.5235-04.2005.Peer-Reviewed Original ResearchMeSH KeywordsAlkaline PhosphataseAnimalsAxonsBinding SitesCell LineChick EmbryoChlorocebus aethiopsGlutathione TransferaseGPI-Linked ProteinsHumansIn Vitro TechniquesLigandsMiceMyelin ProteinsNogo ProteinsNogo Receptor 1PeptidesProtein IsoformsProtein Structure, TertiaryReceptors, Cell SurfaceRecombinant Fusion Proteins
2004
Neogenin mediates the action of repulsive guidance molecule
Rajagopalan S, Deitinghoff L, Davis D, Conrad S, Skutella T, Chedotal A, Mueller BK, Strittmatter SM. Neogenin mediates the action of repulsive guidance molecule. Nature Cell Biology 2004, 6: 756-762. PMID: 15258590, DOI: 10.1038/ncb1156.Peer-Reviewed Original ResearchConceptsRepulsive guidance moleculeRetinal ganglion cell axonsGuidance moleculesGanglion cell axonsDorsal root ganglion axonsTemporal retinal axonsVisual map formationReceptor mechanismsCell axonsNeogenin expressionRetinal axonsGanglion axonsAxonal responsivenessOptic tectumChick retinaNeogeninSub-nanomolar affinityAxonsAxonal guidanceNeogenin functionsResponsive stateNeural tubeMap formationExpressionRetina
2002
Myelin-Associated Glycoprotein as a Functional Ligand for the Nogo-66 Receptor
Liu BP, Fournier A, GrandPré T, Strittmatter SM. Myelin-Associated Glycoprotein as a Functional Ligand for the Nogo-66 Receptor. Science 2002, 297: 1190-1193. PMID: 12089450, DOI: 10.1126/science.1073031.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonsBinding SitesChick EmbryoCloning, MolecularCOS CellsGanglia, SpinalGene LibraryGPI-Linked ProteinsLigandsMiceMyelin ProteinsMyelin-Associated GlycoproteinNerve RegenerationNeuritesNeuronsNogo ProteinsNogo Receptor 1Peptide FragmentsPhosphatidylinositol Diacylglycerol-LyaseProtein Structure, TertiaryReceptors, Cell SurfaceRecombinant Fusion ProteinsSialic AcidsTransfectionType C Phospholipases
2001
Identification of a receptor mediating Nogo-66 inhibition of axonal regeneration
Fournier A, GrandPre T, Strittmatter S. Identification of a receptor mediating Nogo-66 inhibition of axonal regeneration. Nature 2001, 409: 341-346. PMID: 11201742, DOI: 10.1038/35053072.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAmino Acid SequenceAnimalsAxonsBinding SitesCell DivisionCell LineChickensCloning, MolecularCOS CellsDNA, ComplementaryGene ExpressionGPI-Linked ProteinsGrowth ConesHumansMiceMolecular Sequence DataMyelin ProteinsNerve RegenerationNogo ProteinsNogo Receptor 1Protein Structure, TertiaryReceptors, Cell SurfaceRecombinant Fusion ProteinsConceptsNogo-66Axonal regenerationHuman CNS injuryNogo-66 receptorAxonal inhibitionAdult vertebrate CNSUnresponsive neuronsCentral nervous system myelinCNS injuryReceptor expressionAxon regenerationEnhanced recoveryGlycophosphatidylinositol-linked proteinAxonal extensionNogoNeuronsReceptorsSystem myelinAxonal surfaceInhibitionCell typesVertebrate CNSExtracellular domainHigh affinityCell morphology
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
1989
Localization of angiotensin converting enzyme in the ciliary epithelium of the rat eye.
Strittmatter SM, Braas KM, Snyder SH. Localization of angiotensin converting enzyme in the ciliary epithelium of the rat eye. Investigative Ophthalmology & Visual Science 1989, 30: 2209-14. PMID: 2551838.Peer-Reviewed Original ResearchConceptsCiliary epitheliumRat eyesLocalization of angiotensinAnti-ACE antibodiesAqueous humor productionACE immunoreactivityACE inhibitorsPotent ACE inhibitorPosterior chamberChoroid plexusImmunocytochemical stainingMonoclonal antibodiesChoroidal epitheliumVentricular surfaceEpitheliumAngiotensinHumor productionEyesMajor siteACEAntibodiesLow levelsHigh levelsPlexusImmunoreactivity
1986
Characterization of angiotensin converting enzyme by [3H]captopril binding.
Strittmatter SM, Snyder SH. Characterization of angiotensin converting enzyme by [3H]captopril binding. Molecular Pharmacology 1986, 29: 142-8. PMID: 3005826.Peer-Reviewed Original ResearchConceptsEnzyme-inhibitor interactionsActive site Zn2Dissociation rate constantsPure enzyme preparationCatalysisEnzyme moleculesNM-1 min-1Characterization of angiotensinRate constantsEnzyme preparationSubstrate catalysisSedimentation experimentsGel filtrationIonsMin-1Polypeptide chainBinding sitesIsomerizationMonophasic associationBindingZn2L-leucineMoleculesChloridePurification
1985
Enkephalin Convertase Demonstrated in the Pituitary and Adrenal Gland by 3HGuanidinoethylmercaptosuccinic Acid Autoradiography: Dehydration Decreases Neurohypophyseal Levels*
STRITTMATTER S, LYNCH D, DE SOUZA E, SNYDER S. Enkephalin Convertase Demonstrated in the Pituitary and Adrenal Gland by 3HGuanidinoethylmercaptosuccinic Acid Autoradiography: Dehydration Decreases Neurohypophyseal Levels*. Endocrinology 1985, 117: 1667-1674. PMID: 3928337, DOI: 10.1210/endo-117-4-1667.Peer-Reviewed Original ResearchConceptsPituitary lobeBrattleboro ratsPmol/Acid autoradiographyAdrenal glandAdrenal medullaEnkephalin convertaseArginine vasopressin treatmentAnterior pituitary lobeIntermediate pituitary lobePosterior pituitary lobeNeurohypophyseal levelsSplanchnic denervationHaloperidol treatmentParaventricular nucleusAdrenal cortexMagnocellular portionControl animalsSupraoptic nucleusIntermediate lobeRatsVasopressin treatmentBovine adrenal medullaAdrenal medullary enzymesLobeIsolation and characterization of an olfactory receptor protein for odorant pyrazines.
Pevsner J, Trifiletti RR, Strittmatter SM, Snyder SH. Isolation and characterization of an olfactory receptor protein for odorant pyrazines. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 3050-3054. PMID: 2986147, PMCID: PMC397704, DOI: 10.1073/pnas.82.9.3050.Peer-Reviewed Original Research
1984
Angiotensin-Converting Enzyme in the Male Rat Reproductive System: Autoradiographic Visualization with [3H]Captopril*
STRITTMATTER S, SNYDER S. Angiotensin-Converting Enzyme in the Male Rat Reproductive System: Autoradiographic Visualization with [3H]Captopril*. Endocrinology 1984, 115: 2332-2341. PMID: 6094156, DOI: 10.1210/endo-115-6-2332.Peer-Reviewed Original ResearchConceptsACE activityMale rat reproductive systemRat reproductive systemSoluble ACE activityAutoradiographic silver grainsStages I-VIIIInitial segmentMale ratsAutoradiographic visualizationPharmacological profileTesticular slicesBasal epitheliumSilver grainsLuminal labellingReproductive tractInterstitial tissueMonoclonal antibodiesVas deferensSeminiferous tubulesLevel of bindingReproductive systemLuminal surfaceEpithelium
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
1980
Properties of the separated catalytic and regulatory units of brain adenylate cyclase.
Strittmatter S, Neer EJ. Properties of the separated catalytic and regulatory units of brain adenylate cyclase. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 6344-6348. PMID: 6935648, PMCID: PMC350280, DOI: 10.1073/pnas.77.11.6344.Peer-Reviewed Original Research