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
[42] ADP-ribosylation factor (ARF) as regulator of spectrin assembly at Golgi complex
De Matteis M, Morrow J. [42] ADP-ribosylation factor (ARF) as regulator of spectrin assembly at Golgi complex. Methods In Enzymology 2001, 329: 405-416. PMID: 11210560, DOI: 10.1016/s0076-6879(01)29101-0.Peer-Reviewed Original ResearchMeSH KeywordsADP-Ribosylation FactorsAnimalsCell LineCell Membrane PermeabilityCoat Protein Complex IDNA PrimersElectrophoresis, Polyacrylamide GelEscherichia coliFluorescent Antibody TechniqueGenetic VectorsGolgi ApparatusIntracellular MembranesPeptide FragmentsProtein BindingRecombinant Fusion ProteinsSpectrinConceptsADP-ribosylation factorGolgi membranesSpectrin peptidesPermeabilized cultured cellsBinding of spectrinCultured cell linesDifferent functional domainsSpectrin assemblySequence motifsRibosylation factorIndirect immunofluorescent microscopyFunctional domainsIntracellular distributionCultured cellsSpectrinΒIII spectrinImmunofluorescence analysisCell linesGolgiImmunofluorescent microscopyExperimental strategiesPeptidesMembraneCellsOrganelles
2000
Development and characterization of antibodies specific to caspase-3-produced alpha II-spectrin 120 kDa breakdown product: marker for neuronal apoptosis
Nath R, Huggins M, Glantz S, Morrow J, McGinnis K, Nadimpalli R, Wang K. Development and characterization of antibodies specific to caspase-3-produced alpha II-spectrin 120 kDa breakdown product: marker for neuronal apoptosis. Neurochemistry International 2000, 37: 351-361. PMID: 10825575, DOI: 10.1016/s0197-0186(00)00040-1.Peer-Reviewed Original ResearchConceptsWestern blotRat cerebellar granule neuronsHuman neuroblastoma SH-SY5Y cellsNeuroblastoma SH-SY5Y cellsSpectrin breakdown productsCerebellar granule neuronsSH-SY5Y cellsApoptotic neuronsCharacterization of antibodiesNeuronal apoptosisNeurodegenerative conditionsGranule neuronsBreakdown productsImmunocytochemical studySH-SY5YII-spectrinWithdrawal-induced apoptosisAntibodiesNeuronsCaspase-3Apoptotic deathPowerful markerChicken antibodiesApoptosisAlpha-spectrin
1997
Site-Directed Mutagenesis of αII Spectrin at Codon 1175 Modulates Its μ-Calpain Susceptibility †
Stabach P, Cianci C, Glantz S, Zhang Z, Morrow J. Site-Directed Mutagenesis of αII Spectrin at Codon 1175 Modulates Its μ-Calpain Susceptibility †. Biochemistry 1997, 36: 57-65. PMID: 8993318, DOI: 10.1021/bi962034i.Peer-Reviewed Original ResearchConceptsSite-directed mutagenesisAlpha II spectrinCalpain cleavage sitesCleavage siteII-spectrinHelix CRecombinant GST-fusion proteinsBona fide proteinGST fusion proteinTriple-helical motifsStrict substrate specificityFamily of Ca2Protein kinase CDynamic molecular modelingStructural repeatsProminent substrateDifferent amino acidsSubstrate specificityIntracellular proteolysisPenultimate residueCysteine proteasesKinase CMost proteasesSteroid receptor activationSpectrin
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
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 Research
1989
An 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
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 ResearchConceptsLong-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 fragmentsPotentiationProtease
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 mappingCalmodulinMechanisms of cytoskeletal regulation: Functional and antigenic diversity in human erythrocyte and brain beta spectrin
Harris A, Anderson J, Yurchenco P, Green L, Ainger K, Morrow J. Mechanisms of cytoskeletal regulation: Functional and antigenic diversity in human erythrocyte and brain beta spectrin. Journal Of Cellular Biochemistry 1986, 30: 51-69. PMID: 2420811, DOI: 10.1002/jcb.240300107.Peer-Reviewed Original Research
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 Research
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 Research
1980
Identification of functional domains of human erythrocyte spectrin.
Morrow J, Speicher D, Knowles W, Hsu C, Marchesi V. Identification of functional domains of human erythrocyte spectrin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 6592-6596. PMID: 6935670, PMCID: PMC350332, DOI: 10.1073/pnas.77.11.6592.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesErythrocyte MembraneErythrocytesHumansMacromolecular SubstancesMembrane ProteinsPeptide FragmentsSpectrinConceptsHuman erythrocyte spectrinErythrocyte membrane vesiclesMembrane vesiclesBinding of spectrinErythrocyte spectrinHigh-affinity membraneCleavage of spectrinFunctional domainsCytoplasmic surfaceDimeric spectrinProtein receptorsPolypeptide chainTerminal regionSpectrinTemperature-dependent associationUnique polypeptide chainsNoncovalent associationTerminal portionAlpha chainBeta chainIdentification of proteolytically resistant domains of human erythrocyte spectrin.
Speicher D, Morrow J, Knowles W, Marchesi V. Identification of proteolytically resistant domains of human erythrocyte spectrin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 5673-5677. PMID: 7003593, PMCID: PMC350131, DOI: 10.1073/pnas.77.10.5673.Peer-Reviewed Original Research
1974
Ligand-dependent aggregation of chicken hemoglobin AI
Morrow J, Wittebort R, Gurd F. Ligand-dependent aggregation of chicken hemoglobin AI. Biochemical And Biophysical Research Communications 1974, 60: 1058-1065. PMID: 4429560, DOI: 10.1016/0006-291x(74)90420-3.Peer-Reviewed Original Research