2000
Identification and Characterization of Human SLP-2, a Novel Homologue of Stomatin (Band 7.2b) Present in Erythrocytes and Other Tissues*
Wang Y, Morrow J. Identification and Characterization of Human SLP-2, a Novel Homologue of Stomatin (Band 7.2b) Present in Erythrocytes and Other Tissues*. Journal Of Biological Chemistry 2000, 275: 8062-8071. PMID: 10713127, DOI: 10.1074/jbc.275.11.8062.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntibody SpecificityBlood ProteinsCloning, MolecularCytoskeletonDNA, ComplementaryErythrocyte MembraneHumansMembrane ProteinsMolecular Sequence DataMultigene FamilyNerve Tissue ProteinsProtein BindingProtein BiosynthesisProtein Structure, TertiarySequence Analysis, DNASequence Analysis, ProteinSequence Homology, Amino AcidTissue DistributionConceptsIntegral membrane proteinsMembrane proteinsStomatin homologueSLP-1SLP-2Human stomatinCholesterol-rich lipid raftsLipid domain organizationTerminal hydrophobic domainAmino acid sequenceCultured COS cellsMature human erythrocytesSDS-polyacrylamide gel electrophoresis analysisErythrocyte membrane proteinsDomain organizationNonerythroid tissuesLipid raftsStomatin genePeripheral cytoskeletonChromosome 9p13StomatinAcid sequenceGel electrophoresis analysisCOS cellsRelated proteins
1993
Cloning of a Portion of the Chromosomal Gene and cDNA for Human β-Fodrin, the Nonerythroid Form of β-Spectrin
Chang J, Scarpa A, Eddy R, Byers M, Harris A, Morrow J, Watkins P, Shows T, Forget B. Cloning of a Portion of the Chromosomal Gene and cDNA for Human β-Fodrin, the Nonerythroid Form of β-Spectrin. Genomics 1993, 17: 287-293. PMID: 8406479, DOI: 10.1006/geno.1993.1323.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBrainCarrier ProteinsChromosome MappingChromosomes, Human, Pair 2Cloning, MolecularDNA ProbesDNA, ComplementaryExonsHumansHybrid CellsIntronsMiceMicrofilament ProteinsMolecular Sequence DataNerve Tissue ProteinsOligonucleotide ProbesRestriction MappingSequence Homology, Amino AcidSpectrinConceptsAmino acid sequenceAcid sequenceNonerythroid formsDNA sequencesSimilar exon/intron organizationGenomic DNAExon/intron organizationSomatic hybrid cell linesCell cDNA libraryHuman genomic librarySingle-copy DNA fragmentsSingle-copy probesComposite DNA sequenceDNA sequence analysisHybrid cell linesIntron organizationChromosomal localizationGenomic clonesGenomic libraryGenomic fragmentChromosomal genesCDNA clonesCDNA libraryChromosome 2Nucleotide sequence
1991
Actin and tubulin binding domains of synapsins Ia and Ib.
Petrucci T, Morrow J. Actin and tubulin binding domains of synapsins Ia and Ib. Biochemistry 1991, 30: 413-22. PMID: 1899024, DOI: 10.1021/bi00216a016.Peer-Reviewed Original Research
1990
Calmodulin and calcium-dependent protease I coordinately regulate the interaction of fodrin with actin.
Harris A, Morrow J. Calmodulin and calcium-dependent protease I coordinately regulate the interaction of fodrin with actin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1990, 87: 3009-3013. PMID: 2326262, PMCID: PMC53823, DOI: 10.1073/pnas.87.8.3009.Peer-Reviewed Original Research
1988
Proteolytic processing of human brain alpha spectrin (fodrin): identification of a hypersensitive site
Harris A, Morrow J. Proteolytic processing of human brain alpha spectrin (fodrin): identification of a hypersensitive site. Journal Of Neuroscience 1988, 8: 2640-2651. PMID: 3074159, PMCID: PMC6569499, DOI: 10.1523/jneurosci.08-07-02640.1988.Peer-Reviewed Original ResearchMeSH KeywordsBrainCalmodulinCarrier ProteinsErythrocytesHumansMicrofilament ProteinsNerve Tissue ProteinsPeptide FragmentsPeptide HydrolasesPeptide MappingTrypsinConceptsLong-term potentiationBrain spectrinCalcium-dependent mechanismCalcium-dependent neutral proteaseCalcium-dependent proteaseCentral molecular mechanismsSite of actionReceptor functionPostsynaptic membraneCalcium-dependent mannerFurther investigationMolecular mechanismsGel overlay techniqueAlpha subunitNeutral proteaseNonerythroid spectrinImportant moleculesProteolytic processingCleavage fragmentsPotentiationProteaseA domain of synapsin I involved with actin bundling shares immunologic cross‐reactivity with villin
Petrucci T, Mooseker M, Morrow J. A domain of synapsin I involved with actin bundling shares immunologic cross‐reactivity with villin. Journal Of Cellular Biochemistry 1988, 36: 25-35. PMID: 3125185, DOI: 10.1002/jcb.240360104.Peer-Reviewed Original ResearchConceptsBovine synapsin ISynapsin IActin binding proteinsPeptide mappingTwo-dimensional peptide mapsSmall synaptic vesiclesPhosphorylation controlBundling proteinActin bindingUnrelated proteinsActin bundlesActin filamentsNeuronal phosphoproteinSynapsin I.Binding proteinVivo roleSynaptic vesiclesParent proteinProteinPeptide mapsChymotryptic digestionVillinPeptide fragmentsCross reactFragments
1987
Synapsin I: an actin-bundling protein under phosphorylation control.
Petrucci T, Morrow J. Synapsin I: an actin-bundling protein under phosphorylation control. Journal Of Cell Biology 1987, 105: 1355-1363. PMID: 3115996, PMCID: PMC2114810, DOI: 10.1083/jcb.105.3.1355.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBrainCattleKineticsMicrotubule-Associated ProteinsMicrotubulesNerve Tissue ProteinsPhosphoproteinsPhosphorylationSynapsinsConceptsMicrotubule-binding activity