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
1998
Structure of the Ankyrin-binding Domain of α-Na,K-ATPase*
Zhang Z, Devarajan P, Dorfman A, Morrow J. Structure of the Ankyrin-binding Domain of α-Na,K-ATPase*. Journal Of Biological Chemistry 1998, 273: 18681-18684. PMID: 9668035, DOI: 10.1074/jbc.273.30.18681.Peer-Reviewed Original ResearchConceptsK-ATPaseUbiquitous membrane proteinsSecond cytoplasmic domainSpecific macromolecular interactionsMadin-Darby canine kidney cellsAlpha-NACanine kidney cellsCytoplasmic domainThree-dimensional structureMembrane proteinsGlutathione S-transferasePlasma membraneRegulatory proteinsAnkyrinAmino acids bindFusion proteinResidues 142Trisphosphate receptorVectorial transportSurface loopsMacromolecular interactionsMultiple ankyrinHydrophilic faceS-transferaseFusion peptide
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
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
Contributions of the β‐subunit to spectrin structure and function
Coleman T, Fishkind D, Mooseker M, Morrow J. Contributions of the β‐subunit to spectrin structure and function. Cytoskeleton 1989, 12: 248-263. PMID: 2524283, DOI: 10.1002/cm.970120406.Peer-Reviewed Original ResearchFunctional diversity among spectrin isoforms
Coleman T, Fishkind D, Mooseker M, Morrow J. Functional diversity among spectrin isoforms. Cytoskeleton 1989, 12: 225-247. PMID: 2655937, DOI: 10.1002/cm.970120405.Peer-Reviewed Original ResearchConceptsSpectrin isoformsBeta subunitMembrane skeletal proteinsFunctional diversityUbiquitous familySubcellular localizationMembrane linkageCommon alpha subunitSkeletal proteinsAlpha subunitNonerythroid spectrinStructural comparisonCell typesMajor functional differencesSpectrinFunctional differencesSubunitsIsoformsFunctional propertiesSummary of studiesProteinDiversityObserved differencesOwn laboratoryLinkage
1987
Abnormal 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 Research
1977
Quantitative determination of carbamino adducts of alpha and beta chains in human adult hemoglobin in presence and absence of carbon monoxide and 2,3-diphosphoglycerate.
Matthew J, Morrow J, Wittebort R, Gurd F. Quantitative determination of carbamino adducts of alpha and beta chains in human adult hemoglobin in presence and absence of carbon monoxide and 2,3-diphosphoglycerate. Journal Of Biological Chemistry 1977, 252: 2234-2244. PMID: 14958, DOI: 10.1016/s0021-9258(17)40546-1.Peer-Reviewed Original Research
1976
Carbon 13 resonances of 13CO2 carbamino adducts of alpha and beta chains in human adult hemoglobin.
Morrow J, Matthew J, Wittebort R, Gurd F. Carbon 13 resonances of 13CO2 carbamino adducts of alpha and beta chains in human adult hemoglobin. Journal Of Biological Chemistry 1976, 251: 477-484. PMID: 1395, DOI: 10.1016/s0021-9258(17)33904-2.Peer-Reviewed Original Research
1975
Nuclear Magnetic Resonance Studies Of Hemoglobin: Functional State Correlations And Isotopic Enrichment Strategie
Morrow J, Gurd F, Ho C. Nuclear Magnetic Resonance Studies Of Hemoglobin: Functional State Correlations And Isotopic Enrichment Strategie. Critical Reviews In Biochemistry 1975, 3: 221-287. PMID: 3388, DOI: 10.3109/10409237509105453.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino AcidsAnimalsBinding SitesCarboxyhemoglobinHemeHemoglobinsHemoglobins, AbnormalHorsesHumansHydrogen-Ion ConcentrationIronMagnetic Resonance SpectroscopyMethemoglobinModels, MolecularMyoglobinOxyhemoglobinsProtein BindingProtein ConformationSpecies SpecificityWhales
1974
CO2 Adducts of Certain Amino Acids, Peptides, and Sperm Whale Myoglobin Studied by Carbon 13 and Proton Nuclear Magnetic Resonance
Morrow J, Keim P, Gurd F. CO2 Adducts of Certain Amino Acids, Peptides, and Sperm Whale Myoglobin Studied by Carbon 13 and Proton Nuclear Magnetic Resonance. Journal Of Biological Chemistry 1974, 249: 7484-7494. PMID: 4436319, DOI: 10.1016/s0021-9258(19)81264-4.Peer-Reviewed Original ResearchConceptsNuclear magnetic resonanceAmino acidsProton nuclear magnetic resonanceDeuterium isotope effectChemical shiftsCO2 adductCertain amino acidsSperm whale myoglobinNMR measurementsMagnetic resonanceCarbon-13Fast exchangeMost amino acidsEquilibrium constantsCarbamino adductsIsotope effectWhale myoglobinStructural consequencesAdductsAcidPeptidesAccurate determinationNMRResonanceSensitive functionLigand-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