2001
Dynactin-Dependent, Dynein-Driven Vesicle Transport in the Absence of Membrane Proteins A Role for Spectrin and Acidic Phospholipids
Muresan V, Stankewich M, Steffen W, Morrow J, Holzbaur E, Schnapp B. Dynactin-Dependent, Dynein-Driven Vesicle Transport in the Absence of Membrane Proteins A Role for Spectrin and Acidic Phospholipids. Molecular Cell 2001, 7: 173-183. PMID: 11172722, DOI: 10.1016/s1097-2765(01)00165-4.Peer-Reviewed Original ResearchConceptsVesicle transportAcidic phospholipidsAxonal vesiclesProtein-free liposomesAbsence of membranesPH domainDependent motilityCytosolic factorsDynactinSpectrinEssential roleSpectrin polypeptidesVesiclesMembranePhospholipidsAxonal transportMotilitySoluble componentsContext of liposomesDyneinCytosolPolypeptideTransportRoleRetrograde axonal transport
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 ResearchMeSH KeywordsBicarbonatesCarbon DioxideHemoglobinsHumansHydrogen-Ion ConcentrationKineticsMagnetic Resonance SpectroscopyConceptsCarbamino 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 CO2Spectrin 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
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 functionCarbon 13 Nuclear Magnetic Resonance of Pentapeptides of Glycine Containing Central Residues of Methionine, Proline, Arginine, and Lysine
Keim P, Vigna R, Nigen A, Morrow J, Gurd F. Carbon 13 Nuclear Magnetic Resonance of Pentapeptides of Glycine Containing Central Residues of Methionine, Proline, Arginine, and Lysine. Journal Of Biological Chemistry 1974, 249: 4149-4156. PMID: 4850872, DOI: 10.1016/s0021-9258(19)42496-4.Peer-Reviewed Original ResearchMeSH KeywordsArginineCarbon IsotopesGlycineHydrogen-Ion ConcentrationHydroxylysineLysineMagnetic Resonance SpectroscopyMethionineMolecular ConformationOligopeptidesProlinePyrrolidinesConceptsChemical shiftsCarbon-13 nuclear magnetic resonanceLysine peptidesPyrrolidine ringNuclear magnetic resonance spectroscopyState of protonationChemical shift assignmentsNuclear magnetic resonanceSide chain groupsCentral residuesMagnetic resonance spectroscopyAdjacent glycine residuesΕ-amino groupSpin-lattice relaxation timePeptide backboneShift assignmentsChain groupsRatio of transConformational flexibilitySide chainsTrans formResonance spectroscopyNatural abundancePK valuesCarbon nuclei13C NMR Studies of the Interaction of Hb and Carbonic Anhydrase with 13CO2
Gurd F, Morrow J, Keim P, Visscher R, Marshall R. 13C NMR Studies of the Interaction of Hb and Carbonic Anhydrase with 13CO2. Advances In Experimental Medicine And Biology 1974, 48: 109-124. PMID: 4215298, DOI: 10.1007/978-1-4684-0943-7_6.Peer-Reviewed Original ResearchConceptsMetal-protein interactionsInteraction of CO2NMR studiesHydrated derivativeNMR spectrometerSmall moleculesInteraction of HbCarbonate saltsBuffer componentsBicarbonate ionsCarbonic anhydraseCO2NMRUnquestionable importanceCommon strategySpeciesProteinIonsInsolubilityMoleculesSaltInteractionDerivativesBicarbonateSpectrometer
1973
Carbon 13 Nuclear Magnetic Resonance of Pentapeptides of Glycine Containing Central Residues of Serine, Threonine, Aspartic and Glutamic Acids, Asparagine, and Glutamine
Keim P, Vigna R, Morrow J, Marshall R, Gurd F. Carbon 13 Nuclear Magnetic Resonance of Pentapeptides of Glycine Containing Central Residues of Serine, Threonine, Aspartic and Glutamic Acids, Asparagine, and Glutamine. Journal Of Biological Chemistry 1973, 248: 7811-7818. PMID: 4750428, DOI: 10.1016/s0021-9258(19)43261-4.Peer-Reviewed Original ResearchConceptsChemical shiftsGroup protonationCarbon-13 nuclear magnetic resonanceNuclear magnetic resonance spectroscopyState of protonationSide chain groupsNuclear magnetic resonanceNatural abundance 13CAmino group protonationPK valuesCentral residuesMagnetic resonance spectroscopySpin-lattice relaxation timeAspartic acid (RGD) peptideGlutamic acid peptideΒ-carbonChain groupsResonance spectroscopyProtonationSensitive resonancePH dependenceDissociation constantsEffect of aggregationCarbon nucleiGlutamic acidInteraction of 13CO2 and Bicarbonate with Human Hemoglobin Preparations
Morrow J, Keim P, Visscher R, Marshall R, Gurd F. Interaction of 13CO2 and Bicarbonate with Human Hemoglobin Preparations. Proceedings Of The National Academy Of Sciences Of The United States Of America 1973, 70: 1414-1418. PMID: 4514311, PMCID: PMC433509, DOI: 10.1073/pnas.70.5.1414.Peer-Reviewed Original ResearchCarbon 13 Nuclear Magnetic Resonance Spectroscopy of Myoglobins Carboxymethylated with Enriched [2-13C]Bromoacetate
Nigen A, Keim P, Marshall R, Morrow J, Vigna R, Gurd F. Carbon 13 Nuclear Magnetic Resonance Spectroscopy of Myoglobins Carboxymethylated with Enriched [2-13C]Bromoacetate. Journal Of Biological Chemistry 1973, 248: 3724-3732. PMID: 4735715, DOI: 10.1016/s0021-9258(19)43986-0.Peer-Reviewed Original Research