2002
The Spectrin-Ankyrin Skeleton Controls CD45 Surface Display and Interleukin-2 Production
Pradhan D, Morrow J. The Spectrin-Ankyrin Skeleton Controls CD45 Surface Display and Interleukin-2 Production. Immunity 2002, 17: 303-315. PMID: 12354383, DOI: 10.1016/s1074-7613(02)00396-5.Peer-Reviewed Original ResearchMeSH KeywordsAnkyrinsCD3 ComplexCell MembraneHumansInterleukin-2Jurkat CellsLeukocyte Common AntigensLymphocyte ActivationMacromolecular SubstancesMembrane GlycoproteinsNeoplasm ProteinsPeptide FragmentsProtein BindingProtein Interaction MappingProtein IsoformsProtein Structure, TertiaryRecombinant Fusion ProteinsSpectrinStructure-Activity RelationshipT-LymphocytesTransfectionConceptsJurkat T cellsT cell receptor stimulationCell receptor stimulationCytoplasmic domainSurface recruitmentBetaI spectrinSpectrin peptidesT cell activationSurface displayIntracellular poolUnexpected contributionAnkyrinSpectrinCell activationReceptor stimulationCD45T cellsCellsInterleukin-2 productionGlycoproteinRecruitmentT lymphocyte functionActivationLymphocyte functionPool
2001
Spectrin Oligomerization is Cooperatively Coupled to Membrane Assembly: A Linkage Targeted by Many Hereditary Hemolytic Anemias?
Giorgi M, Cianci C, Gallagher P, Morrow J. Spectrin Oligomerization is Cooperatively Coupled to Membrane Assembly: A Linkage Targeted by Many Hereditary Hemolytic Anemias? Experimental And Molecular Pathology 2001, 70: 215-230. PMID: 11418000, DOI: 10.1006/exmp.2001.2377.Peer-Reviewed Original Research
1997
α-Catenin Can Form Asymmetric Homodimeric Complexes and/or Heterodimeric Complexes with ॆ-Catenin*
Koslov E, Maupin P, Pradhan D, Morrow J, Rimm D. α-Catenin Can Form Asymmetric Homodimeric Complexes and/or Heterodimeric Complexes with ॆ-Catenin*. Journal Of Biological Chemistry 1997, 272: 27301-27306. PMID: 9341178, DOI: 10.1074/jbc.272.43.27301.Peer-Reviewed Original ResearchConceptsMembrane adhesion complexesHomodimeric complexCadherin moleculesAdhesion complexesAdhesive complexesHeterodimeric complexΑ-cateninOligomeric stateSurface plasmon resonance assaysMultimeric stateResidues 54Relative stoichiometryBiophysical techniquesMolecular massCell adhesionAmino acidsRecombinant moleculesHuman alphaRotary shadowingResonance assaysPrecise stoichiometryComplexesCytoskeletonCateninHomodimer
1994
A partial structural repeat forms the heterodimer self-association site of all beta-spectrins
Kennedy S, Weed S, Forget B, Morrow J. A partial structural repeat forms the heterodimer self-association site of all beta-spectrins. Journal Of Biological Chemistry 1994, 269: 11400-11408. PMID: 8157672, DOI: 10.1016/s0021-9258(19)78138-1.Peer-Reviewed Original ResearchAmino Acid SequenceBase SequenceBinding SitesCloning, MolecularDNA PrimersErythrocytesEscherichia coliGlutathione TransferaseHumansKineticsMacromolecular SubstancesModels, StructuralMolecular Sequence DataProtein Structure, SecondaryRecombinant Fusion ProteinsRecombinant ProteinsRepetitive Sequences, Nucleic AcidSpectrin
1993
Calmodulin-binding domain of recombinant erythrocyte beta-adducin.
Scaramuzzino D, Morrow J. Calmodulin-binding domain of recombinant erythrocyte beta-adducin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 3398-3402. PMID: 8475088, PMCID: PMC46307, DOI: 10.1073/pnas.90.8.3398.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBinding SitesBlood ProteinsCalmodulinCalmodulin-Binding ProteinsCalpainCattleCloning, MolecularDNAErythrocytesKineticsMacromolecular SubstancesMolecular Sequence DataOligodeoxyribonucleotidesPhosphorylationProtein Structure, SecondaryRecombinant ProteinsRestriction MappingTrypsinConceptsCaM-binding activityBeta-adducinBundles F-actinProtease-sensitive domainsCAMP-dependent kinaseCaM-binding domainPartial cDNA cloneBinding of spectrinAmino acid codeDependent CaM bindingProtein kinase CSingle letter amino acid codeCaM-binding sequenceProtease-resistant corePEST sequenceCovalent phosphorylationShares structural featuresCDNA clonesCortical cytoskeletonHeterodimeric proteinStructural basisConsensus sequenceMammalian erythrocytesProtease sensitivityBind calmodulin
1992
Karyoplasmic interaction selection strategy: a general strategy to detect protein-protein interactions in mammalian cells.
Fearon E, Finkel T, Gillison M, Kennedy S, Casella J, Tomaselli G, Morrow J, Van Dang C. Karyoplasmic interaction selection strategy: a general strategy to detect protein-protein interactions in mammalian cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 7958-7962. PMID: 1387709, PMCID: PMC49834, DOI: 10.1073/pnas.89.17.7958.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCHO CellsCricetinaeCytoplasmDNA-Binding ProteinsFlow CytometryFungal ProteinsHerpes Simplex Virus Protein Vmw65Hybrid CellsMacromolecular SubstancesMolecular Sequence DataProtein BindingRecombinant ProteinsSaccharomyces cerevisiae ProteinsTranscription FactorsTransfectionViral ProteinsConceptsProtein-protein interactionsMammalian cellsChimeric proteinReporter geneYeast transcriptional activator GAL4KISS systemSpecific protein-protein interactionsTranscriptional activator GAL4Transcriptional activation domainNovel protein interactionsDNA-binding domainTranscriptional activation functionSpecific interactionsActivator GAL4Activation domainProtein interactionsResultant transcriptionCDNA librarySelectable markerGAL4Drug resistance markersCell surfaceProteinTranscriptionGenes
1990
Radiolabel‐transfer cross‐linking demonstrates that protein 4.1 binds to the N‐terminal region of β spectrin and to actin in binary interactions
BECKER P, SCHWARTZ M, MORROW J, Samuel E. Radiolabel‐transfer cross‐linking demonstrates that protein 4.1 binds to the N‐terminal region of β spectrin and to actin in binary interactions. The FEBS Journal 1990, 193: 827-836. PMID: 2249696, DOI: 10.1111/j.1432-1033.1990.tb19406.x.Peer-Reviewed Original ResearchCalmodulin 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
1989
Calmodulin Regulates Fodrin Susceptibility to Cleavage by Calciumdependent Protease I
Harris A, Croall D, Morrow J. Calmodulin Regulates Fodrin Susceptibility to Cleavage by Calciumdependent Protease I. Journal Of Biological Chemistry 1989, 264: 17401-17408. PMID: 2551900, DOI: 10.1016/s0021-9258(18)71508-1.Peer-Reviewed Original ResearchConceptsAlpha subunitProtease IAbsence of CaMRegulated proteolysisEukaryotic cellsRegulation of plasticityCortical cytoskeletonCalmodulin bindingQuaternary structureBeta subunitSubunitsTetrameric formCalcium-dependent proteolysisFodrinProteolysisCaM antagonistsAlpha-fodrinFunctional evidenceDifferential susceptibilityCaM.Fodrin proteolysisIsotonic bufferCytoskeletonClose proximityCalmodulinAn unusual beta-spectrin associated with clustered acetylcholine receptors.
Bloch R, Morrow J. An unusual beta-spectrin associated with clustered acetylcholine receptors. Journal Of Cell Biology 1989, 108: 481-493. PMID: 2645300, PMCID: PMC2115447, DOI: 10.1083/jcb.108.2.481.Peer-Reviewed Original Research
1987
Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding.
Mische S, Mooseker M, Morrow J. Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding. Journal Of Cell Biology 1987, 105: 2837-2845. PMID: 3693401, PMCID: PMC2114693, DOI: 10.1083/jcb.105.6.2837.Peer-Reviewed Original ResearchMeSH KeywordsActinsCalmodulin-Binding ProteinsErythrocyte MembraneHumansKineticsMacromolecular SubstancesMembrane ProteinsMolecular WeightPhosphoproteinsProtein BindingSpectrinConceptsSpectrin-actin bindingAbnormal oxidant sensitivity and beta-chain structure of spectrin in hereditary spherocytosis associated with defective spectrin-protein 4.1 binding.
Becker P, Morrow J, Lux S. Abnormal oxidant sensitivity and beta-chain structure of spectrin in hereditary spherocytosis associated with defective spectrin-protein 4.1 binding. Journal Of Clinical Investigation 1987, 80: 557-565. PMID: 3611357, PMCID: PMC442269, DOI: 10.1172/jci113104.Peer-Reviewed Original ResearchThe interaction of calmodulin with human erythrocyte spectrin. Inhibition of protein 4.1-stimulated actin binding.
Anderson J, Morrow J. The interaction of calmodulin with human erythrocyte spectrin. Inhibition of protein 4.1-stimulated actin binding. Journal Of Biological Chemistry 1987, 262: 6365-6372. PMID: 3571263, DOI: 10.1016/s0021-9258(18)45579-2.Peer-Reviewed Original Research
1986
A calmodulin and α-subunit binding domain in human erythrocyte spectrin
Sears D, Marchesi V, Morrow J. A calmodulin and α-subunit binding domain in human erythrocyte spectrin. Biochimica Et Biophysica Acta 1986, 870: 432-442. PMID: 3697360, DOI: 10.1016/0167-4838(86)90251-7.Peer-Reviewed Original ResearchConceptsCalmodulin binding siteSpectrin-actin membrane skeletonBinding sitesSubunit-subunit associationMr fragmentTwo-dimensional peptide mappingPutative calmodulin binding siteErythrocyte spectrinNon-erythroid spectrinCleavage of spectrinHuman erythrocyte spectrinProtein 4.1Cyanogen bromide cleavageMembrane skeletonActin bindingCalmodulin bindingNH2 terminusBind calmodulinNative conditionsBeta subunitCalmodulin regulationTerminal regionSpectrinPeptide mappingCalmodulin
1983
Molecular and functional changes in spectrin from patients with hereditary pyropoikilocytosis.
Knowles W, Morrow J, Speicher D, Zarkowsky H, Mohandas N, Mentzer W, Shohet S, Marchesi V. Molecular and functional changes in spectrin from patients with hereditary pyropoikilocytosis. Journal Of Clinical Investigation 1983, 71: 1867-1877. PMID: 6863544, PMCID: PMC370392, DOI: 10.1172/jci110942.Peer-Reviewed Original ResearchMeSH KeywordsAdultAnemia, Hemolytic, CongenitalErythrocytesFemaleHot TemperatureHumansMacromolecular SubstancesMaleMembrane ProteinsPeptide FragmentsProtein DenaturationSpectrinTrypsin[23] Erythrocyte membrane proteins: Detection of spectrin oligomers by gel electrophoresis
Morrow J, Haigh W. [23] Erythrocyte membrane proteins: Detection of spectrin oligomers by gel electrophoresis. Methods In Enzymology 1983, 96: 298-304. PMID: 6656632, DOI: 10.1016/s0076-6879(83)96027-5.Peer-Reviewed Original ResearchMeSH KeywordsElectrophoresis, Polyacrylamide GelErythrocyte MembraneHumansIndicators and ReagentsMacromolecular SubstancesMolecular WeightRosaniline DyesSpectrinConceptsSodium dodecyl sulfateDodecyl sulfateGel electrophoresisPolyacrylamide gel electrophoresisGelMembrane proteinsProtein-protein associationSlab gelsOligomersSecond dimensionSpectrin oligomersElectrophoretic analysisPrincipal structural proteinPreparationErythrocyte membrane skeletonPolyacrylamide gel electrophoretic analysisErythrocyte membrane proteinsElectrophoresisGel electrophoretic analysisNondenaturing gelMembrane skeletonDistinct polypeptidesStructural proteinsSpectrin moleculesMolecules
1982
A structural model of human erythrocyte spectrin. Alignment of chemical and functional domains.
Speicher D, Morrow J, Knowles W, Marchesi V. A structural model of human erythrocyte spectrin. Alignment of chemical and functional domains. Journal Of Biological Chemistry 1982, 257: 9093-9101. PMID: 7096353, DOI: 10.1016/s0021-9258(18)34247-9.Peer-Reviewed Original ResearchConceptsNumerous small peptidesPeptide mapping techniquesChemical domainsPeptide segmentsMolecular weightChemical cleavageSized peptidesTwo-dimensional peptide mapping techniquesSmall peptidesIntact moleculeUnique peptidesPhosphorylated amino acidsFurther proteolytic cleavageOverlap peptidesPolypeptide segmentsIntermediate-sized peptidesMoleculesMild trypsin digestionTrypsin digestionTwo-dimensional peptide mapsPeptidesStructural modelSpectrin subunitsCleavagePeptide mapsMonoclonal antibodies as probes of domain structure of the spectrin alpha subunit.
Yurchenco P, Speicher D, Morrow J, Knowles W, Marchesi V. Monoclonal antibodies as probes of domain structure of the spectrin alpha subunit. Journal Of Biological Chemistry 1982, 257: 9102-9107. PMID: 7096354, DOI: 10.1016/s0021-9258(18)34248-0.Peer-Reviewed Original ResearchAntibodies, MonoclonalHumansMacromolecular SubstancesMembrane ProteinsMolecular WeightPeptide FragmentsSpectrinTrypsinThe Polymeric State of Actin in the Human Erythrocyte Cytoskeleton
Atkinson M, Morrow J, Marchesi V. The Polymeric State of Actin in the Human Erythrocyte Cytoskeleton. Journal Of Cellular Biochemistry 1982, 18: 493-505. PMID: 7200988, DOI: 10.1002/jcb.1982.240180410.Peer-Reviewed Original ResearchMeSH KeywordsActinsChemical PhenomenaChemistryCytoskeletonErythrocyte MembraneErythrocytesHumansMacromolecular SubstancesMolecular WeightPhalloidine
1981
Self-assembly of spectrin oligomers in vitro: a basis for a dynamic cytoskeleton.
Morrow J, Marchesi V. Self-assembly of spectrin oligomers in vitro: a basis for a dynamic cytoskeleton. Journal Of Cell Biology 1981, 88: 463-468. PMID: 7204503, PMCID: PMC2111738, DOI: 10.1083/jcb.88.2.463.Peer-Reviewed Original Research