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
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
1989
Ankyrin links fodrin to the alpha subunit of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells.
Morrow J, Cianci C, Ardito T, Mann A, Kashgarian M. Ankyrin links fodrin to the alpha subunit of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells. Journal Of Cell Biology 1989, 108: 455-465. PMID: 2537316, PMCID: PMC2115445, DOI: 10.1083/jcb.108.2.455.Peer-Reviewed Original ResearchConceptsMadin-Darby canine kidney cellsCanine kidney cellsK-ATPaseAlpha subunitMolecular mechanismsMDCK cellsMinor membrane proteinsDistribution of fodrinErythrocyte ankyrinConfluent MDCK cellsBinding of ankyrinKidney cellsHuman erythrocyte ankyrinRenal epithelial cellsCytoplasmic domainNonerythroid cellsMembrane proteinsCortical cytoskeletonBasolateral domainMembrane skeletonPolarized distributionAnkyrinBasolateral marginsCell developmentErythrocyte band 3
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 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
1986
Limited proteolysis of the erythrocyte membrane skeleton by calcium-dependent proteinases
Croall D, Morrow J, DeMartino G. Limited proteolysis of the erythrocyte membrane skeleton by calcium-dependent proteinases. Biochimica Et Biophysica Acta 1986, 882: 287-296. PMID: 3015225, DOI: 10.1016/0304-4165(86)90250-3.Peer-Reviewed Original ResearchA 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
Mechanisms of cytoskeletal regulation: modulation of membrane affinity in avian brush border and erythrocyte spectrins.
Howe C, Sacramone L, Mooseker M, Morrow J. Mechanisms of cytoskeletal regulation: modulation of membrane affinity in avian brush border and erythrocyte spectrins. Journal Of Cell Biology 1985, 101: 1379-1385. PMID: 2931438, PMCID: PMC2113910, DOI: 10.1083/jcb.101.4.1379.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 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
The 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 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
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