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-spectrinIdentification and Characterization of βV Spectrin, a Mammalian Ortholog of Drosophila βHSpectrin* 210
Stabach P, Morrow J. Identification and Characterization of βV Spectrin, a Mammalian Ortholog of Drosophila βHSpectrin* 210. Journal Of Biological Chemistry 2000, 275: 21385-21395. PMID: 10764729, DOI: 10.1074/jbc.c000159200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCaenorhabditis elegansCloning, MolecularConsensus SequenceDNA, ComplementaryDrosophilaDrosophila ProteinsExonsGene LibraryHumansIntronsMammalsMolecular Sequence DataMolecular WeightOrgan SpecificityPhylogenyRatsRecombinant ProteinsRepetitive Sequences, Amino AcidRetinaSequence AlignmentSequence Homology, Amino AcidSpectrinTumor Cells, CulturedViral ProteinsConceptsDrosophila orthologMammalian orthologsSpectrin repeatsPleckstrin homology domainComplete cDNA sequenceActin-binding domainSelf-association domainAmino acids 85Amino acid sequenceBeta-spectrin geneHuman retina cDNA libraryRetina cDNA libraryFly counterpartMammalian spectrinsCaenorhabditis elegansHomology domainEpithelial cell populationsSH3 domainApical domainCDNA sequenceCDNA libraryOrthologsPolarized epitheliumBeta spectrinAcid sequence
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
1995
Autoantibodies specific for villin found in patients with colon cancer and other colitides
Rimm D, Holland T, Morrow J, Anderson J. Autoantibodies specific for villin found in patients with colon cancer and other colitides. Digestive Diseases And Sciences 1995, 40: 389-395. PMID: 7851204, DOI: 10.1007/bf02065426.Peer-Reviewed Original ResearchConceptsColon cancerActive autoimmune responseSpecific gastrointestinal diseasesLevels of autoantibodiesColon cancer patients´ seraCancer patient seraIntestinal epithelial cellsCryptic antigensAutoimmune responseGastrointestinal pathologyColonic diseaseGastrointestinal diseasesPatient seraNormal controlsPathological significanceWestern blotDisease statesEpithelial cellsNoninvasive approachUnique noninvasive approachAntibodiesAutoantibodiesBrush borderPatientsCancer
1992
Cytostellin: a novel, highly conserved protein that undergoes continuous redistribution during the cell cycle
Warren S, Landolfi A, Curtis C, Morrow J. Cytostellin: a novel, highly conserved protein that undergoes continuous redistribution during the cell cycle. Journal Of Cell Science 1992, 103: 381-388. PMID: 1478941, DOI: 10.1242/jcs.103.2.381.Peer-Reviewed Original ResearchConceptsMitotic spindle apparatusSpindle apparatusLower eukaryotic cellsOnset of prophaseEukaryotic cellsDaughter cellsCytoplasmic proteinsMammalian cellsMonoclonal antibody H5Interphase nucleiTelophase cellsNuclease digestionCell cycleImmunofluorescence microscopyImmunoblot analysisCell processesProteinNascent nucleiSalt extractionImmunoaffinity chromatographyCellsDistinct subsetsNucleusAnaphaseProphase
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 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 ResearchAbnormal 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
1985
Mechanism of cytoskeletal regulation (I): functional differences correlate with antigenic dissimilarity in human brain and erythrocyte spectrin
Harris A, Green L, Ainger K, Morrow J. Mechanism of cytoskeletal regulation (I): functional differences correlate with antigenic dissimilarity in human brain and erythrocyte spectrin. Biochimica Et Biophysica Acta 1985, 830: 147-158. PMID: 2410030, DOI: 10.1016/0167-4838(85)90022-6.Peer-Reviewed Original Research
1983
[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 ResearchConceptsSodium 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
Monoclonal 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 ResearchA 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 mapsThe 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 Research
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 ResearchSpectrin oligomers: A structural feature of the erythrocyte cytoskeleton
Morrow J, Haigh W, Marchesi V. Spectrin oligomers: A structural feature of the erythrocyte cytoskeleton. Journal Of Cellular Biochemistry 1981, 17: 275-287. PMID: 7328675, DOI: 10.1002/jsscb.380170308.Peer-Reviewed Original ResearchConceptsMembrane skeletonRed cell membrane skeletonCell membrane skeletonProtein-protein associationSpectrin associationsHigh molecular weight oligomersErythrocyte cytoskeletonNumerous membranePhysiological conditionsTriton XMolecular weight oligomersStructural featuresCytoskeletonWeight oligomersSpectrinTropomyosinMembraneAssembly