2003
Identification of the primary caspase 3 cleavage site in alpha II-spectrin during apoptosis
Williams S, Smith A, Cianci C, Morrow J, Brown T. Identification of the primary caspase 3 cleavage site in alpha II-spectrin during apoptosis. Apoptosis 2003, 8: 353-361. PMID: 12815278, DOI: 10.1023/a:1024168901003.Peer-Reviewed Original ResearchConceptsCaspase-3 cleavage siteCleavage sitePrimary cleavage siteII-spectrinCytoskeletal integrityAlpha II spectrinMembrane stabilityCaspase-3Cleavage of alphaApoptotic cell deathCaspase-3 activationMature B cellsConsensus sitesDeletion analysisTranscriptional inhibitorMajor proteinsLikely altersApoptotic bodiesCell deathProteinStructural conformationActinomycin DSpectrinNew insightsApoptosis
2000
Spectrin tethers and mesh in the biosynthetic pathway.
De Matteis M, Morrow J. Spectrin tethers and mesh in the biosynthetic pathway. Journal Of Cell Science 2000, 113 ( Pt 13): 2331-43. PMID: 10852813, DOI: 10.1242/jcs.113.13.2331.Peer-Reviewed Original ResearchConceptsSecretory pathwayMembrane proteinsSmall GTPase ArfEarly secretory pathwayDynamics of organellesGolgi dynamicsProtein traffickingOrganelle functionGolgi structurePhosphoinositide levelsGolgi membranesBiosynthetic pathwayMacromolecular complexesCytosolic proteinsAdapter moleculeSpectrin skeletonIntracellular transportOrganellesSpectrinDirect interactionProteinKey playersRecent discoveryGolgiSimilar role
1998
The role of ankyrin and spectrin in membrane transport and domain formation
De Matteis M, Morrow J. The role of ankyrin and spectrin in membrane transport and domain formation. Current Opinion In Cell Biology 1998, 10: 542-549. PMID: 9719877, DOI: 10.1016/s0955-0674(98)80071-9.Peer-Reviewed Original ResearchConceptsAnterograde protein traffickingRole of ankyrinADP-ribosylation factorGolgi integrityProtein traffickingSpecific functional domainsSpectrin functionSecretory pathwayMotor proteinsFunctional domainsGolgi complexMembrane transportNovel insightsSpectrinRecent discoveryDomain formationAnkyrinTraffickingProteinPathwayFunctionComplexesDiscoveryDomainIdentificationADP ribosylation factor regulates spectrin binding to the Golgi complex
Godi A, Santone I, Pertile P, Devarajan P, Stabach P, Morrow J, Di Tullio G, Polishchuk R, Petrucci T, Luini A, De Matteis M. ADP ribosylation factor regulates spectrin binding to the Golgi complex. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 8607-8612. PMID: 9671725, PMCID: PMC21123, DOI: 10.1073/pnas.95.15.8607.Peer-Reviewed Original ResearchConceptsADP-ribosylation factorGolgi complexRibosylation factorG proteinsVesicular stomatitis virus G proteinPleckstrin homology domainSmall G proteinsPH domain interactionBinding of spectrinVirus G proteinGolgi spectrinHomology domainPH domainCoat proteinDocking siteDomain interactionsGolgiEndoplasmic reticulumPtdInsP2 levelsDomain IPhospholipase DSpectrinGolgi fractionsProteinPtdInsP2
1997
Of Membrane Stability and Mosaics: The Spectrin Cytoskeleton
Morrow J, Rimm D, Kennedy S, Cianci C, Sinard J, Weed S. Of Membrane Stability and Mosaics: The Spectrin Cytoskeleton. 1997, 485-540. DOI: 10.1002/cphy.cp140111.Peer-Reviewed Original ResearchNon-erythroid cellsMembrane skeletonRed cell membrane skeletonSpectrin membrane skeletonCell membrane skeletonErythrocyte membrane skeletonMembrane organizersProtein 4.1Spectrin cytoskeletonAdhesion proteinsCytoskeletal elementsSpectrin skeletonMembrane stabilityMosaic modelSpectrinProteinCellsDematinDynaminStomatinPallidinCytoskeletonAnkyrinAdducinTropomodulin
1994
Ankyrin binds to two distinct cytoplasmic domains of Na,K-ATPase alpha subunit.
Devarajan P, Scaramuzzino D, Morrow J. Ankyrin binds to two distinct cytoplasmic domains of Na,K-ATPase alpha subunit. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 2965-2969. PMID: 8159688, PMCID: PMC43495, DOI: 10.1073/pnas.91.8.2965.Peer-Reviewed Original ResearchConceptsK-ATPase alpha subunitMembrane transport proteinsCytoplasmic domainAlpha subunitK-ATPaseTransport proteinsIntegral membrane transport proteinsDomain IIPutative cytoplasmic domainInteraction of ankyrinDistinct cytoplasmic domainsATPase domainHuman erythrocyte spectrinSignificant homologyUbiquitous proteinSpectrin cytoskeletonRecombinant fusion proteinPrimary sequenceAnkyrinFusion proteinChannel proteinsClear functionSubunitsProteinSpectrin binds
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 subsetsNucleusAnaphaseProphaseKaryoplasmic interaction selection strategy: a general strategy to detect protein-protein interactions in mammalian cells.
Fearon E, Finkel T, Gillison M, Kennedy S, Casella J, Tomaselli G, Morrow J, Van Dang C. Karyoplasmic interaction selection strategy: a general strategy to detect protein-protein interactions in mammalian cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 7958-7962. PMID: 1387709, PMCID: PMC49834, DOI: 10.1073/pnas.89.17.7958.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCHO CellsCricetinaeCytoplasmDNA-Binding ProteinsFlow CytometryFungal ProteinsHerpes Simplex Virus Protein Vmw65Hybrid CellsMacromolecular SubstancesMolecular Sequence DataProtein BindingRecombinant ProteinsSaccharomyces cerevisiae ProteinsTranscription FactorsTransfectionViral ProteinsConceptsProtein-protein interactionsMammalian cellsChimeric proteinReporter geneYeast transcriptional activator GAL4KISS systemSpecific protein-protein interactionsTranscriptional activator GAL4Transcriptional activation domainNovel protein interactionsDNA-binding domainTranscriptional activation functionSpecific interactionsActivator GAL4Activation domainProtein interactionsResultant transcriptionCDNA librarySelectable markerGAL4Drug resistance markersCell surfaceProteinTranscriptionGenes
1989
Functional 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
1988
A domain of synapsin I involved with actin bundling shares immunologic cross‐reactivity with villin
Petrucci T, Mooseker M, Morrow J. A domain of synapsin I involved with actin bundling shares immunologic cross‐reactivity with villin. Journal Of Cellular Biochemistry 1988, 36: 25-35. PMID: 3125185, DOI: 10.1002/jcb.240360104.Peer-Reviewed Original ResearchConceptsBovine synapsin ISynapsin IActin binding proteinsPeptide mappingTwo-dimensional peptide mapsSmall synaptic vesiclesPhosphorylation controlBundling proteinActin bindingUnrelated proteinsActin bundlesActin filamentsNeuronal phosphoproteinSynapsin I.Binding proteinVivo roleSynaptic vesiclesParent proteinProteinPeptide mapsChymotryptic digestionVillinPeptide fragmentsCross reactFragments
1987
Characterization of intestinal brush border cytoskeletal proteins of normal and neoplastic human epithelial cells. A comparison with the avian brush border.
Carboni J, Howe C, West A, Barwick K, Mooseker M, Morrow J. Characterization of intestinal brush border cytoskeletal proteins of normal and neoplastic human epithelial cells. A comparison with the avian brush border. American Journal Of Pathology 1987, 129: 589-600. PMID: 3425692, PMCID: PMC1899811.Peer-Reviewed Original ResearchConceptsMicrovillar actin bundlesActin binding proteinsHuman brush borderIntestinal epithelial cell brush bordersEpithelial cell brush bordersBrush borderMicrovillar proteinsHuman epithelial cellsCytoskeletal matrixCytoskeletal proteinsMultiple proteinsActin bundlesImmunolocalization studiesSpectrin isoformsMammalian sourcesMajor proteinsDifferentiation stateBinding proteinProtein myosinProteinTerminal webCell brush borderCytoskeletonNeoplastic stateMature enterocytes
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
1974
13C 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