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
1995
Identification of two alternatively spliced transcripts of STEP: a subfamily of brain-enriched protein tyrosine phosphatases
Sharma E, Zhao F, Bult A, Lombroso P. Identification of two alternatively spliced transcripts of STEP: a subfamily of brain-enriched protein tyrosine phosphatases. Brain Research 1995, 32: 87-93. PMID: 7494467, DOI: 10.1016/0169-328x(95)00066-2.Peer-Reviewed Original ResearchConceptsTyrosine phosphatase domainPhosphatase domainProtein tyrosineSpliced transcriptsExon-intron organizationProtein tyrosine phosphataseOpen reading frameTyrosine phosphataseReading frameDistinct functionsGenomic DNANorthern analysisSTEP geneSTEP isoformsMolecular massTranscriptsSTEP61ProteinMouse brainTyrosineCentral nervous systemSubfamiliesGenesNervous systemMonoclonal antibodiesCellular 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 isoforms