2004
A Neutralizing Anti-Nogo66 Receptor Monoclonal Antibody Reverses Inhibition of Neurite Outgrowth by Central Nervous System Myelin*
Li W, Walus L, Rabacchi SA, Jirik A, Chang E, Schauer J, Zheng BH, Benedetti NJ, Liu BP, Choi E, Worley D, Silvian L, Mo W, Mullen C, Yang W, Strittmatter SM, Sah DW, Pepinsky B, Lee DH. A Neutralizing Anti-Nogo66 Receptor Monoclonal Antibody Reverses Inhibition of Neurite Outgrowth by Central Nervous System Myelin*. Journal Of Biological Chemistry 2004, 279: 43780-43788. PMID: 15297463, DOI: 10.1074/jbc.m401803200.Peer-Reviewed Original ResearchConceptsOligodendrocyte myelin glycoproteinRat dorsal root ganglion neuronsDorsal root ganglion neuronsMonoclonal antibodiesMyelin glycoproteinNeurite outgrowthMyelin proteinsUseful therapeutic approachCNS myelin substrateNogo66 receptorCentral nervous system myelinGanglion neuronsTherapeutic approachesCNS repairMyelin substrateCentral nervous system myelin proteinsInhibitory effectNgR1AntibodiesNeurite growthMyelinSystem myelinReverses inhibitionMolecular epitopes
2000
Identification of the Nogo inhibitor of axon regeneration as a Reticulon protein
GrandPré T, Nakamura F, Vartanian T, Strittmatter S. Identification of the Nogo inhibitor of axon regeneration as a Reticulon protein. Nature 2000, 403: 439-444. PMID: 10667797, DOI: 10.1038/35000226.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAxonsCattleCell DivisionCell LineCentral Nervous SystemChick EmbryoCloning, MolecularConsensus SequenceEscherichia coliGrowth InhibitorsHumansMembrane ProteinsMolecular Sequence DataMyelin ProteinsNerve RegenerationNogo ProteinsOligodendrogliaPC12 CellsRatsRecombinant ProteinsSequence Homology, Amino AcidConceptsCentral nervous systemPeripheral nervous systemCNS white matterAxonal regenerationAxon regenerationNervous systemWhite matterAdult central nervous systemMammalian axon regenerationIN-1 antibodiesReticulon 1Dorsal root ganglion growth conesFunctional recoverySpinal cordSchwann cellsCNS axonsExtracellular domainAxonal extensionNogoAxon extensionGrowth conesOligodendrocytesInhibitory activityReticulon 4Moderate degree
1997
Brain CRMP Forms Heterotetramers Similar to Liver Dihydropyrimidinase
Wang L, Strittmatter S. Brain CRMP Forms Heterotetramers Similar to Liver Dihydropyrimidinase. Journal Of Neurochemistry 1997, 69: 2261-2269. PMID: 9375656, DOI: 10.1046/j.1471-4159.1997.69062261.x.Peer-Reviewed Original Research
1994
An intrinsic guanine nucleotide exchange inhibitor in Gi2 alpha. Significance of G-protein self-suppression which antagonizes receptor signal.
Okamoto T, Murayama Y, Strittmatter SM, Katada T, Asano S, Ogata E, Nishimoto I. An intrinsic guanine nucleotide exchange inhibitor in Gi2 alpha. Significance of G-protein self-suppression which antagonizes receptor signal. Journal Of Biological Chemistry 1994, 269: 13756-13759. PMID: 8188651, DOI: 10.1016/s0021-9258(17)36711-x.Peer-Reviewed Original ResearchConceptsIntrinsic guanineHeterotrimeric G-protein familyG proteinsReceptor signalsGi2 alphaG protein familyProto-oncogene productProtein familyC-terminusResidues 338Alpha subunitReceptor polypeptideBasal activityAlpha activationPolypeptideGuanineReceptor stimulationAlphaExchange inhibitorInhibitorsReceptorsTerminusSubunitsProteinGi2
1993
GAP-43 augments G protein-coupled receptor transduction in Xenopus laevis oocytes.
Strittmatter SM, Cannon SC, Ross EM, Higashijima T, Fishman MC. GAP-43 augments G protein-coupled receptor transduction in Xenopus laevis oocytes. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 5327-5331. PMID: 7685122, PMCID: PMC46709, DOI: 10.1073/pnas.90.11.5327.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcholineAnimalsCalciumCattleChloride ChannelsFemaleGAP-43 ProteinGrowth SubstancesGTP-Binding ProteinsHumansInositol 1,4,5-TrisphosphateIon Channel GatingIon ChannelsKineticsMembrane GlycoproteinsMembrane PotentialsMembrane ProteinsNerve Tissue ProteinsOocytesReceptors, MuscarinicRecombinant ProteinsSignal TransductionXenopus laevisConceptsGAP-43Receptor transductionG protein-coupled receptor agonistsCalcium-activated chloride channelXenopus laevis oocytesProtein GAP-43Neuronal protein GAP-43Receptor agonistInjection of inositolLaevis oocytesReceptor stimulationOocyte responseGrowth cone motilityChloride channelsSignal transductionIntracellular regulatorsIntracellular signalsMolecular mechanismsTransductionOocytesHigh levelsAgonists
1992
Palmitoylation alters protein activity: blockade of G(o) stimulation by GAP‐43.
Sudo Y, Valenzuela D, Beck‐Sickinger A, Fishman MC, Strittmatter SM. Palmitoylation alters protein activity: blockade of G(o) stimulation by GAP‐43. The EMBO Journal 1992, 11: 2095-2102. PMID: 1534749, PMCID: PMC556676, DOI: 10.1002/j.1460-2075.1992.tb05268.x.Peer-Reviewed Original ResearchConceptsHeterotrimeric G proteinsProtein-protein interactionsMembrane associationFatty acylationGAP-43Cysteine residuesHydrophobicity of proteinsN-terminusAddition of palmitateG proteinsPalmitoylationNeuronal proteinsProteinGAP-43 proteinTerminal peptidesActive poolResiduesPeptidesCysteineMembraneActivityActivationPool
1991
An intracellular guanine nucleotide release protein for G0. GAP-43 stimulates isolated alpha subunits by a novel mechanism.
Strittmatter SM, Valenzuela D, Sudo Y, Linder ME, Fishman MC. An intracellular guanine nucleotide release protein for G0. GAP-43 stimulates isolated alpha subunits by a novel mechanism. Journal Of Biological Chemistry 1991, 266: 22465-22471. PMID: 1834672, DOI: 10.1016/s0021-9258(18)54595-6.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBrainCattleGAP-43 ProteinGTP-Binding ProteinsGuanine NucleotidesGuanosine 5'-O-(3-Thiotriphosphate)Guanosine DiphosphateGuanosine TriphosphateKineticsLiposomesMacromolecular SubstancesMembrane GlycoproteinsNADNerve Tissue ProteinsPertussis ToxinPhosphatidylcholinesPhosphoproteinsProtein BindingRatsRecombinant ProteinsVirulence Factors, BordetellaConceptsG proteinsMembrane-associated G proteinsGAP-43Novel mechanismG protein-coupled receptorsG protein-coupled membrane receptorsIntracellular guanine nucleotidesGuanine nucleotidesProtein-coupled receptorsCytosolic faceGTP gamma S bindingRegions of neuronsGTPase activityGDP releaseAlpha s.Alpha subunitAlpha i1Alpha oMembrane receptorsNeuronal proteinsBeta gammaGTP gamma SProteinGamma S bindingGrowth cones
1988
Characterization of a neutral, divalent cation-sensitive endopeptidase: a possible role in neuropeptide processing.
Supattapone S, Strittmatter SM, Fricker LD, Snyder SH. Characterization of a neutral, divalent cation-sensitive endopeptidase: a possible role in neuropeptide processing. Brain Research 1988, 427: 173-81. PMID: 3382941, DOI: 10.1016/0169-328x(88)90063-0.Peer-Reviewed Original ResearchConceptsCorpus striatumBrain regionsTissue distributionBovine adrenal chromaffin granulesAdrenal chromaffin granulesHomogeneous tissue distributionPossible roleNeuropeptide processingDensity gradient fractionationSucrose density gradient fractionationEndopeptidaseLeu-ArgChromaffin granulesHigh levelsBasic amino acidsTrypsin-like endopeptidaseEnzyme activityHippocampusStriatum
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
[3H]guanidinoethylmercaptosuccinic acid binding to tissue homogenates. Selective labeling of enkephalin convertase.
Strittmatter SM, Lynch DR, Snyder SH. [3H]guanidinoethylmercaptosuccinic acid binding to tissue homogenates. Selective labeling of enkephalin convertase. Journal Of Biological Chemistry 1984, 259: 11812-11817. PMID: 6434531, DOI: 10.1016/s0021-9258(20)71284-6.Peer-Reviewed Original Research
1982
Physical separation and characterization of two types of benzodiazepine receptors.
Lo MM, Strittmatter SM, Snyder SH. Physical separation and characterization of two types of benzodiazepine receptors. Proceedings Of The National Academy Of Sciences Of The United States Of America 1982, 79: 680-684. PMID: 6281778, PMCID: PMC345810, DOI: 10.1073/pnas.79.2.680.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