2013
Neuroprotective Role of a Brain-Enriched Tyrosine Phosphatase, STEP, in Focal Cerebral Ischemia
Deb I, Manhas N, Poddar R, Rajagopal S, Allan AM, Lombroso PJ, Rosenberg GA, Candelario-Jalil E, Paul S. Neuroprotective Role of a Brain-Enriched Tyrosine Phosphatase, STEP, in Focal Cerebral Ischemia. Journal Of Neuroscience 2013, 33: 17814-17826. PMID: 24198371, PMCID: PMC3818554, DOI: 10.1523/jneurosci.2346-12.2013.Peer-Reviewed Original ResearchConceptsIschemic brain damageStriatal-enriched phosphataseBrain damageNeuroprotective roleBrain injuryP38 MAPK activationSustained p38 MAPK activationIschemic brain injuryFocal cerebral ischemiaOnset of reperfusionHypoxia-reoxygenation injuryP38 MAPKMAPK activationIschemic strokeNeurological deficitsCerebral ischemiaStroke therapyKO miceRat modelP38 MAPK pathwayCultured neuronsNeuronal culturesGenetic deletionSecondary activationInjurySubstrate-Based Fragment Identification for the Development of Selective, Nonpeptidic Inhibitors of Striatal-Enriched Protein Tyrosine Phosphatase
Baguley TD, Xu HC, Chatterjee M, Nairn AC, Lombroso PJ, Ellman JA. Substrate-Based Fragment Identification for the Development of Selective, Nonpeptidic Inhibitors of Striatal-Enriched Protein Tyrosine Phosphatase. Journal Of Medicinal Chemistry 2013, 56: 7636-7650. PMID: 24083656, PMCID: PMC3875168, DOI: 10.1021/jm401037h.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiphenyl CompoundsBlood-Brain BarrierBoronic AcidsCells, CulturedCerebral CortexHumansNeuronsPermeabilityPhosphorous AcidsProtein Tyrosine Phosphatases, Non-ReceptorRatsRats, Sprague-DawleySmall Molecule LibrariesStereoisomerismStructure-Activity RelationshipSubstrate SpecificityConceptsSubstrate Activity ScreeningProtein tyrosine phosphatase activityProtein tyrosine phosphataseTyrosine phosphatase activityGlutamate receptor internalizationOptimization of fragmentsTyrosine phosphataseDual specificityReceptor internalizationDevelopment of SelectiveSTEP inhibitorPhosphatase activityAlzheimer's diseaseIonotropic glutamate receptorsSubstrate-based approachNonpeptidic inhibitorsPotential targetAD mouse modelDrug discoveryRat cortical neuronsActivity screeningCortical neuronsGlutamate receptorsMouse modelNeuropsychiatric disorders
2010
Aβ-Mediated NMDA Receptor Endocytosis in Alzheimer's Disease Involves Ubiquitination of the Tyrosine Phosphatase STEP61
Kurup P, Zhang Y, Xu J, Venkitaramani DV, Haroutunian V, Greengard P, Nairn AC, Lombroso PJ. Aβ-Mediated NMDA Receptor Endocytosis in Alzheimer's Disease Involves Ubiquitination of the Tyrosine Phosphatase STEP61. Journal Of Neuroscience 2010, 30: 5948-5957. PMID: 20427654, PMCID: PMC2868326, DOI: 10.1523/jneurosci.0157-10.2010.Peer-Reviewed Original ResearchMeSH KeywordsAgedAged, 80 and overAlzheimer DiseaseAmyloid beta-PeptidesAnimalsCell LineCells, CulturedCerebral CortexEndocytosisHumansIn Vitro TechniquesMiceMice, KnockoutMice, TransgenicMiddle AgedNeuronsProtein Tyrosine Phosphatases, Non-ReceptorRatsRats, Sprague-DawleyReceptors, N-Methyl-D-AspartateUbiquitinated ProteinsUbiquitinationConceptsAlzheimer's diseaseAbeta treatmentNR2B subunitProtein tyrosine Phosphatase 61Cognitive deficitsNMDA receptor internalizationHuman AD brainsMouse cortical culturesNR1/NR2B receptorsNMDA receptor endocytosisIonotropic glutamate receptorsTyrosine phosphatase STEP61AD brainCortical slicesCortical culturesGlutamate receptorsNR2B receptorsPostsynaptic terminalsPrefrontal cortexNeuronal membranesElevated levelsCortexReceptor internalizationUbiquitin-proteasome systemStep activity
2009
Extrasynaptic NMDA Receptors Couple Preferentially to Excitotoxicity via Calpain-Mediated Cleavage of STEP
Xu J, Kurup P, Zhang Y, Goebel-Goody SM, Wu PH, Hawasli AH, Baum ML, Bibb JA, Lombroso PJ. Extrasynaptic NMDA Receptors Couple Preferentially to Excitotoxicity via Calpain-Mediated Cleavage of STEP. Journal Of Neuroscience 2009, 29: 9330-9343. PMID: 19625523, PMCID: PMC2737362, DOI: 10.1523/jneurosci.2212-09.2009.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAnimalsBrainCalpainCell DeathCells, CulturedCyclin-Dependent Kinase 5EndocytosisGlutamic AcidIn Vitro TechniquesMiceMice, KnockoutMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3NeuronsP38 Mitogen-Activated Protein KinasesProtein Tyrosine Phosphatases, Non-ReceptorRatsRats, Sprague-DawleyReceptors, N-Methyl-D-AspartateSynapsesConceptsStriatal-enriched protein tyrosine phosphataseCalpain cleavage sitesP38 activationCell deathCleavage siteExtracellular signal-regulated kinase 1/2Protein tyrosine phosphataseSignal-regulated kinase 1/2Promotes cell survivalActivation of p38Tyrosine phosphataseSubstrate bindingKinase 1/2ERK1/2 activationCalpain cleavageCell survivalNovel mechanismCalpain-mediated proteolysisReceptors coupleP38NMDAR stimulationPostsynaptic terminalsValid targetCleavage productsSTEP substrates
2008
The Tyrosine Phosphatase STEP Mediates AMPA Receptor Endocytosis after Metabotropic Glutamate Receptor Stimulation
Zhang Y, Venkitaramani DV, Gladding CM, Zhang Y, Kurup P, Molnar E, Collingridge GL, Lombroso PJ. The Tyrosine Phosphatase STEP Mediates AMPA Receptor Endocytosis after Metabotropic Glutamate Receptor Stimulation. Journal Of Neuroscience 2008, 28: 10561-10566. PMID: 18923032, PMCID: PMC2586105, DOI: 10.1523/jneurosci.2666-08.2008.Peer-Reviewed Original ResearchConceptsStriatal-enriched protein tyrosine phosphataseProtein tyrosine phosphataseTyrosine phosphataseAMPAR internalizationMitogen-activated protein kinasePhosphoinositide-3-kinase (PI3K) pathwayAMPA receptor endocytosisTyrosine dephosphorylationAMPA receptor traffickingReceptor endocytosisProtein kinaseKinase pathwayStimulation of mGluR5Receptor traffickingNMDAR endocytosisAMPAR traffickingEndocytosisMetabotropic glutamate receptor stimulationTraffickingSurface expressionInternalizationGlutamate receptor stimulationSynaptic plasticityCentral eventPhosphatase
2007
Status Epilepticus-Induced Somatostatinergic Hilar Interneuron Degeneration Is Regulated by Striatal Enriched Protein Tyrosine Phosphatase
Choi YS, Lin SL, Lee B, Kurup P, Cho HY, Naegele JR, Lombroso PJ, Obrietan K. Status Epilepticus-Induced Somatostatinergic Hilar Interneuron Degeneration Is Regulated by Striatal Enriched Protein Tyrosine Phosphatase. Journal Of Neuroscience 2007, 27: 2999-3009. PMID: 17360923, PMCID: PMC2701360, DOI: 10.1523/jneurosci.4913-06.2007.Peer-Reviewed Original ResearchConceptsStriatal-enriched protein tyrosine phosphataseERK/MAPK activationProtein tyrosine phosphataseCell deathTyrosine phosphataseExtracellular signal-regulated kinase/mitogen-activated protein kinase pathwayKinase/mitogen-activated protein kinase pathwayMAPK activationMAPK pathwayERK/MAPK signalingMitogen-activated protein kinase pathwayStriatal enriched protein tyrosine phosphataseProtein kinase pathwayNeuroprotective responseKinase pathwayImmediate early gene expressionKey regulatorMAPK signalingGene expressionMolecular mechanismsVivo disruptionSignificant rescuePathwayPhosphataseActivation
2006
The Striatal-Enriched Protein Tyrosine Phosphatase Gates Long-Term Potentiation and Fear Memory in the Lateral Amygdala
Paul S, Olausson P, Venkitaramani DV, Ruchkina I, Moran TD, Tronson N, Mills E, Hakim S, Salter MW, Taylor JR, Lombroso PJ. The Striatal-Enriched Protein Tyrosine Phosphatase Gates Long-Term Potentiation and Fear Memory in the Lateral Amygdala. Biological Psychiatry 2006, 61: 1049-1061. PMID: 17081505, PMCID: PMC1853327, DOI: 10.1016/j.biopsych.2006.08.005.Peer-Reviewed Original ResearchMeSH KeywordsAcoustic StimulationAminoacetonitrileAmygdalaAnimalsBehavior, AnimalCells, CulturedConditioning, ClassicalCycloheximideElectric StimulationEnzyme InhibitorsFearFemaleImmunohistochemistryIn Vitro TechniquesLong-Term PotentiationMemoryMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3NeostriatumPatch-Clamp TechniquesPoint MutationPregnancyProtein Synthesis InhibitorsProtein Tyrosine PhosphatasesRatsRats, Sprague-DawleyTranslocation, GeneticConceptsStriatal-enriched protein tyrosine phosphataseERK1/2 activationMitogen-activated protein kinaseProtein tyrosine phosphataseDe novo translationActivation of ERK1/2Tyrosine phosphataseProtein bindsKinase signalingProtein kinaseSequential recruitmentAmygdala-dependent memory formationERK pathwayMemory formationPrimary cell culturesNuclear translocationBiphasic activationLong-term potentiationTranslation blockTAT-STEPERKCell culturesERK1/2ActivationPathway
2002
Genetics of Childhood Disorders: XXXV. Autoimmune Disorders, Part 8: Animal Models for Noninflammatory Autoimmune Disorders of the Brain
HALLETT J, KIESSLING L, Lombroso P. Genetics of Childhood Disorders: XXXV. Autoimmune Disorders, Part 8: Animal Models for Noninflammatory Autoimmune Disorders of the Brain. Journal Of The American Academy Of Child & Adolescent Psychiatry 2002, 41: 223-225. PMID: 11837413, DOI: 10.1097/00004583-200202000-00017.Peer-Reviewed Original Research
2001
Antibodies against neural, nuclear, cytoskeletal, and streptococcal epitopes in children and adults with Tourette’s syndrome, Sydenham’s chorea, and autoimmune disorders
Morshed S, Parveen S, Leckman J, Mercadante M, Kiss M, Miguel E, Arman A, Yazgan Y, Fujii T, Paul S, Peterson B, Zhang H, King R, Scahill L, Lombroso P. Antibodies against neural, nuclear, cytoskeletal, and streptococcal epitopes in children and adults with Tourette’s syndrome, Sydenham’s chorea, and autoimmune disorders. Biological Psychiatry 2001, 50: 566-577. PMID: 11690591, DOI: 10.1016/s0006-3223(01)01096-4.Peer-Reviewed Original ResearchConceptsTotal antinuclear antibodiesAntinuclear antibodiesAutoimmune disordersTourette syndromeAnticytoskeletal antibodiesAntineural antibodiesStreptococcal infectionT patientsTS patientsBeta-hemolytic streptococcal infectionPrior streptococcal infectionHemolytic streptococcal infectionAntistreptolysin O titerIndirect immunofluorescent assayLevels of immunoreactivityWestern blot techniqueMean rankClinical characteristicsSydenham's choreaO titerPatient groupSC patientsIgG antibodiesIgG classNormal controls
2000
The Dopamine/D1 Receptor Mediates the Phosphorylation and Inactivation of the Protein Tyrosine Phosphatase STEP via a PKA-Dependent Pathway
Paul S, Snyder G, Yokakura H, Picciotto M, Nairn A, Lombroso P. The Dopamine/D1 Receptor Mediates the Phosphorylation and Inactivation of the Protein Tyrosine Phosphatase STEP via a PKA-Dependent Pathway. Journal Of Neuroscience 2000, 20: 5630-5638. PMID: 10908600, PMCID: PMC6772528, DOI: 10.1523/jneurosci.20-15-05630.2000.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCatalytic DomainCorpus StriatumCyclic AMP-Dependent Protein KinasesEnzyme ActivationIn Vitro TechniquesMaleMolecular Sequence DataNeuronsPhosphoproteinsPhosphorus RadioisotopesPhosphorylationProtein Tyrosine PhosphatasesProtein Tyrosine Phosphatases, Non-ReceptorRatsRats, Sprague-DawleyReceptors, Dopamine D1Signal TransductionConceptsProtein tyrosine phosphatase familyCAMP-dependent protein kinaseTryptic phosphopeptide mappingPotential phosphorylation sitesUnique N-terminalProtein-protein interactionsMembrane-associated proteinsRole of phosphorylationTyrosine phosphatase familyAmino acid sequenceSite-directed mutagenesisAmino acid sequencingPKA-dependent pathwayTyrosine phosphatase STEPPhosphatase familyPhosphopeptide mappingPhosphorylation sitesAlternative splicingSubcellular compartmentsProtein kinaseTerminal domainEquivalent residuesCytosolic proteinsSpecific residuesAcid sequence
1999
Hypoxia‐Ischemia in Perinatal Rat Brain Induces the Formation of a Low Molecular Weight Isoform of Striatal Enriched Tyrosine Phosphatase (STEP)
Gurd J, Bissoon N, Nguyen T, Lombroso P, Rider C, Beesley P, Vannucci S. Hypoxia‐Ischemia in Perinatal Rat Brain Induces the Formation of a Low Molecular Weight Isoform of Striatal Enriched Tyrosine Phosphatase (STEP). Journal Of Neurochemistry 1999, 73: 1990-1994. PMID: 10537057, DOI: 10.1046/j.1471-4159.1999.01990.x.Peer-Reviewed Original ResearchConceptsHypoxia-ischemiaP21 ratsRat brainIschemia-induced elevationP21 rat brainUnilateral hypoxia-ischemiaCerebral hypoxia-ischemiaPerinatal rat brainResult of ischemiaCalcium-dependent proteolysisLow molecular weight isoformsInterval of recoveryP7 ratsContralateral sideMolecular weight isoformsNT2/D1 cellsCalcium ionophoreLow Mr isoformPostsynaptic densityRatsBrainCalpain IWeight isoformsIschemiaPhosphorylation levelsCalcium‐Dependent Cleavage of Striatal Enriched Tyrosine Phosphatase (STEP)
Nguyen T, Paul S, Xu Y, Gurd J, Lombroso P. Calcium‐Dependent Cleavage of Striatal Enriched Tyrosine Phosphatase (STEP). Journal Of Neurochemistry 1999, 73: 1995-2001. PMID: 10537058, DOI: 10.1046/j.1471-4159.1999.01995.x.Peer-Reviewed Original ResearchConceptsPostsynaptic densityTransient hypoxia-ischemiaPrimary neuronal culturesNeuronal precursor cellsCalcium-dependent cleavageHypoxia-ischemiaStriatal neuronsNeuronal insultsRat striatumNeuronal culturesCalcium ionophoreCalpain inhibitorsSTEP61Precursor cellsLow molecular weight formMolecular weight formsPhosphorylation levelsSmaller isoformSignificant increaseTyrosine phosphorylation levelsRapid appearanceCalpain treatmentRapid influxWeight formsCells
1997
STEP: a family of brain-enriched PTPs. Alternative splicing produces transmembrane, cytosolic and truncated isoforms.
Bult A, Zhao F, Dirkx R, Raghunathan A, Solimena M, Lombroso P. STEP: a family of brain-enriched PTPs. Alternative splicing produces transmembrane, cytosolic and truncated isoforms. European Journal Of Cell Biology 1997, 72: 337-44. PMID: 9127733.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceAnimalsBase SequenceBlotting, NorthernBlotting, WesternBrainCalcium-Binding ProteinsCalnexinCHO CellsCricetinaeFemaleFluorescent Antibody Technique, IndirectMembrane ProteinsMolecular Sequence DataProtein Tyrosine PhosphatasesProtein Tyrosine Phosphatases, Non-ReceptorRatsSynaptophysinTransfectionConceptsProtein tyrosine phosphataseCatalytic phosphatase domainProtein tyrosine kinase familyHydrophobic amino acid sequenceAlternative splicing mechanismAmino acid sequencePrevious biochemical studiesTyrosine kinase familyStop codon upstreamPhosphatase domainCytosolic variantAlternative splicingMembrane compartmentsTyrosine phosphataseKinase familySplicing mechanismSubcellular localizationCytosolic proteinsAcid sequenceN-terminusInactive variantContinuous sucrose gradientSTEP isoformsPolyproline domainEndoplasmic reticulum
1996
STEP61: A Member of a Family of Brain-Enriched PTPs Is Localized to the Endoplasmic Reticulum
Bult A, Zhao F, Dirkx R, Sharma E, Lukacsi E, Solimena M, Naegele J, Lombroso P. STEP61: A Member of a Family of Brain-Enriched PTPs Is Localized to the Endoplasmic Reticulum. Journal Of Neuroscience 1996, 16: 7821-7831. PMID: 8987810, PMCID: PMC6579237, DOI: 10.1523/jneurosci.16-24-07821.1996.Peer-Reviewed Original ResearchConceptsNovel N-terminal regionEnzymatic activityEndoplasmic reticulumPutative transmembrane domainsIntrinsic membrane proteinsExtended N-terminusAmino acid sequenceN-terminal regionDistinctive intracellular distributionsProtein tyrosineCytosolic variantTransmembrane domainMembrane compartmentsMembrane proteinsAcid sequenceSubcellular fractionationN-terminusRecombinant proteinsTransfection experimentsSTEP61Intracellular distributionProteinReticulumImmunocytochemical labelingFamilyTransient compartmental expression of a family of protein tyrosine phosphatases in the developing striatum
Raghunathan A, Matthews G, Lombroso P, Naegele J. Transient compartmental expression of a family of protein tyrosine phosphatases in the developing striatum. Brain Research 1996, 91: 190-199. PMID: 8852369, DOI: 10.1016/0165-3806(95)00176-x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, NorthernBlotting, WesternCalbindinsCell CountDopamine and cAMP-Regulated Phosphoprotein 32Enzyme InhibitorsFemaleGene Expression Regulation, DevelopmentalIsoenzymesNeostriatumNerve Tissue ProteinsNeuronsPhosphoproteinsPostpartum PeriodPregnancyProtein Tyrosine PhosphatasesRatsRats, Inbred StrainsS100 Calcium Binding Protein GSubstance PSubstantia NigraTime FactorsTranscription, GeneticConceptsPatch neuronsPostnatal weekTwo-color immunofluorescent stainingTyrosine hydroxylase-immunoreactive fibersDopaminoceptive brain regionsCalbindin-positive neuronsHydroxylase-immunoreactive fibersStriatum of ratsDopamine islandsPostnatal day 1Most striatal neuronsFirst postnatal weekEarly postnatal developmentMatrix neuronsStriatal afferentsStriatal neuronsImmunoreactive fibersSubstance PLateral striatumDay 1StriatumPostnatal developmentBrain regionsNeuronsCompartmental expression
1995
Molecular Cloning of the Human Homolog of a Striatum-Enriched Phosphatase (STEP) Gene and Chromosomal Mapping of the Human and Murine Loci
Li X, Luna J, Lombroso P, Francke U. Molecular Cloning of the Human Homolog of a Striatum-Enriched Phosphatase (STEP) Gene and Chromosomal Mapping of the Human and Murine Loci. Genomics 1995, 28: 442-449. PMID: 7490079, DOI: 10.1006/geno.1995.1173.Peer-Reviewed Original ResearchConceptsSrc homology domain 3STEP geneTyrosine phosphataseSomatic cell hybrid analysisHuman fetal brain cDNA libraryFetal brain cDNA libraryPhosphatase catalytic domainCell hybrid analysisProtein tyrosine phosphataseAmino acid domainProline-rich regionCandidate disease genesBrain cDNA libraryUsher syndrome type 1CAmino acid levelsChromosomal mappingPhosphatase geneMutant lociHuman homologTrue homologsMolecular cloningCatalytic domainAcid domainMurine locusCDNA libraryCellular and molecular characterization of a brain-enriched protein tyrosine phosphatase
Boulanger L, Lombroso P, Raghunathan A, During M, Wahle P, Naegele. Cellular and molecular characterization of a brain-enriched protein tyrosine phosphatase. Journal Of Neuroscience 1995, 15: 1532-1544. PMID: 7869116, PMCID: PMC6577844, DOI: 10.1523/jneurosci.15-02-01532.1995.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, MonoclonalAxonsBlotting, WesternBrainCerebral CortexCorpus StriatumImmunohistochemistryIn Situ HybridizationMiceMice, Inbred BALB CNeuronsPeptide FragmentsProtein Tyrosine PhosphatasesProtein Tyrosine Phosphatases, Non-ReceptorRatsRNA, MessengerSynaptic TransmissionTissue DistributionConceptsSubstantia nigraAdult rat brainCombination of immunocytochemistrySitu hybridization studiesProjection neuronsBasal gangliaCaudate putamenPresynaptic axonsStriatal enriched protein tyrosine phosphataseRat brainBrain regionsImmunocytochemical stainingLesion experimentsWestern blotLesion studiesWestern blottingMonoclonal antibodiesMRNA expression patternsImmunoreactive formsImmunoreactive bandsProtein tyrosine phosphataseNigraSitu hybridizationHybridization studiesSTEP isoformsA Neuronal Protein Tyrosine Phosphatase Induced by Nerve Growth Factor (∗)
Sharma E, Lombroso P. A Neuronal Protein Tyrosine Phosphatase Induced by Nerve Growth Factor (∗). Journal Of Biological Chemistry 1995, 270: 49-53. PMID: 7814416, DOI: 10.1074/jbc.270.1.49.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceDNAEnzyme InductionIntracellular Signaling Peptides and ProteinsMolecular Sequence DataNerve Growth FactorsNerve Tissue ProteinsNeuronsPC12 CellsProtein Tyrosine PhosphatasesRatsReceptor-Like Protein Tyrosine Phosphatases, Class 7Recombinant Fusion ProteinsSequence Homology, Amino AcidConceptsNerve growth factorNGF treatmentGrowth factorNon-receptor protein tyrosine phosphataseRat brainNeuronal growthProtein tyrosine phosphataseMRNA levelsBrainNorthern blot analysisPC12 cellsBlot analysisTyrosine phosphataseTreatmentPhosphataseExpressionFusion proteinTyrosine phosphatase activity
1993
A protein tyrosine phosphatase expressed within dopaminoceptive neurons of the basal ganglia and related structures
Lombroso P, Naegele, Sharma E, Lerner M. A protein tyrosine phosphatase expressed within dopaminoceptive neurons of the basal ganglia and related structures. Journal Of Neuroscience 1993, 13: 3064-3074. PMID: 8331384, PMCID: PMC6576687, DOI: 10.1523/jneurosci.13-07-03064.1993.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBasal GangliaBase SequenceBlotting, WesternBrainChromatography, AffinityCorpus StriatumDopamine and cAMP-Regulated Phosphoprotein 32FemaleGene ExpressionImmune SeraImmunohistochemistryKineticsMaleMolecular Sequence DataMolecular WeightNerve Tissue ProteinsNeuronsOligodeoxyribonucleotidesOligonucleotides, AntisenseOrgan SpecificityPhosphoproteinsPolymerase Chain ReactionProtein Tyrosine PhosphatasesProtein Tyrosine Phosphatases, Non-ReceptorRatsReceptors, DopamineRecombinant Fusion Proteins
1991
Molecular characterization of a protein-tyrosine-phosphatase enriched in striatum.
Lombroso P, Murdoch G, Lerner M. Molecular characterization of a protein-tyrosine-phosphatase enriched in striatum. Proceedings Of The National Academy Of Sciences Of The United States Of America 1991, 88: 7242-7246. PMID: 1714595, PMCID: PMC52270, DOI: 10.1073/pnas.88.16.7242.Peer-Reviewed Original ResearchConceptsDeduced amino acid sequenceAmino acid consensus sequenceAmino acid sequenceApparent molecular massRat striatal cDNA librarySingle geneVitro translationCDNA clonesStrong homologyCDNA libraryCytoplasmic membraneAcid sequenceRNA transcriptsN-terminusMolecular characterizationRNA analysisMolecular massAmino acidsProteinPhosphataseMRNASequenceHomologyGenesTerminus