1998
Simultaneous Degradation of αII- and βII-Spectrin by Caspase 3 (CPP32) in Apoptotic Cells*
Wang K, Posmantur R, Nath R, McGinnis K, Whitton M, Talanian R, Glantz S, Morrow J. Simultaneous Degradation of αII- and βII-Spectrin by Caspase 3 (CPP32) in Apoptotic Cells*. Journal Of Biological Chemistry 1998, 273: 22490-22497. PMID: 9712874, DOI: 10.1074/jbc.273.35.22490.Peer-Reviewed Original Research
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
1994
A partial structural repeat forms the heterodimer self-association site of all beta-spectrins
Kennedy S, Weed S, Forget B, Morrow J. A partial structural repeat forms the heterodimer self-association site of all beta-spectrins. Journal Of Biological Chemistry 1994, 269: 11400-11408. PMID: 8157672, DOI: 10.1016/s0021-9258(19)78138-1.Peer-Reviewed Original ResearchAmino Acid SequenceBase SequenceBinding SitesCloning, MolecularDNA PrimersErythrocytesEscherichia coliGlutathione TransferaseHumansKineticsMacromolecular SubstancesModels, StructuralMolecular Sequence DataProtein Structure, SecondaryRecombinant Fusion ProteinsRecombinant ProteinsRepetitive Sequences, Nucleic AcidSpectrin
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
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
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
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 ResearchSynapsin 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 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
1981
[29] Measurement of CO2 binding: The 13C NMR method
Morrow J, Matthew J, Gurd F. [29] Measurement of CO2 binding: The 13C NMR method. Methods In Enzymology 1981, 76: 496-511. PMID: 6799730, DOI: 10.1016/0076-6879(81)76139-1.Peer-Reviewed Original ResearchConceptsCarbamino adductsSingle carbon resonancesSensitivity of NMRNuclear magnetic resonance methodsUnique chemical speciesNMR spectraNMR methodsMagnetic resonance methodsR-NHNMR experimentsChemical speciesForm of CO2NMR spectrometerProtein samplesAdductsNMRFree induction decay signalResonance methodProteinCO2Average lifetimePowerful methodDecay signalResonanceMeasurements of CO2
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
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 function