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
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
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
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 proximityCalmodulin
1988
A 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 ResearchBeta spectrin bestows protein 4.1 sensitivity on spectrin-actin interactions.
Coleman T, Harris A, Mische S, Mooseker M, Morrow J. Beta spectrin bestows protein 4.1 sensitivity on spectrin-actin interactions. Journal Of Cell Biology 1987, 104: 519-526. PMID: 3818791, PMCID: PMC2114562, DOI: 10.1083/jcb.104.3.519.Peer-Reviewed Original Research
1984
Mechanisms of cytoskeletal regulation. Modulation of aortic endothelial cell spectrin by the extracellular matrix.
Pratt B, Harris A, Morrow J, Madri J. Mechanisms of cytoskeletal regulation. Modulation of aortic endothelial cell spectrin by the extracellular matrix. American Journal Of Pathology 1984, 117: 349-54. PMID: 6507585, PMCID: PMC1900592.Peer-Reviewed Original ResearchConceptsAortic endothelial cellsEndothelial cellsCultured aortic endothelial cellsSurface receptorsCalf aortic endothelial cellsVascular responsesExtracellular matrixVariety of stimuliPeripheral localizationWound repairReceptorsTransducers of informationMembrane receptorsCellsFibrillar formSpectrin distributionIntracellular distributionNonerythroid spectrinNeoplasiaInjuryFibronectin substrate
1972
Carbon 13 Nuclear Magnetic Resonance Spectroscopy of Myoglobins and Ribonuclease A Carboxymethylated with Enriched [2-13C]Bromoacetate
Nigen A, Keim P, Marshall R, Morrow J, Gurd F. Carbon 13 Nuclear Magnetic Resonance Spectroscopy of Myoglobins and Ribonuclease A Carboxymethylated with Enriched [2-13C]Bromoacetate. Journal Of Biological Chemistry 1972, 247: 4100-4102. PMID: 5033404, DOI: 10.1016/s0021-9258(19)45145-4.Peer-Reviewed Original ResearchConceptsCarbon-13 nuclear magnetic resonance spectroscopyNuclear magnetic resonance spectroscopyNuclear magnetic resonanceΑ-carbon atomNuclear magnetic resonance signalsMagnetic resonance spectroscopyEnriched adductsChemical shiftsBovine pancreatic ribonuclease APancreatic ribonuclease AResonance spectroscopyCarbon atomsDetermination of T1Resonance signalsRibonuclease AMagnetic resonance signalDetailed interpretationMagnetic resonanceSmall proteinsResonanceSpectroscopyDeterminationAdductsAtomsCarboxymethylated