1996
Chapter 6 The Spectrin Cytoskeleton and Organization of Polarized Epithelial Cell Membranes
Devarajan P, Morrow J. Chapter 6 The Spectrin Cytoskeleton and Organization of Polarized Epithelial Cell Membranes. Current Topics In Membranes 1996, 43: 97-128. DOI: 10.1016/s0070-2161(08)60386-x.Peer-Reviewed Original ResearchIntegral membrane proteinsPeripheral plasma membraneCultured epithelial cellsEpithelial cellsAnti-spectrin antibodiesEukaryotic cellsNonerythroid cellsMembrane proteinsSpectrin cytoskeletonEpithelial cell membranesPlasma membraneExperimental removalCell shapeDifferent isoformsMembrane stabilitySpectrinCell membraneCytoskeletonPostsynaptic densityPostsynaptic membraneMembrane instabilityCerebellar granule cellsSkeletal muscleMembraneCells
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 subsetsNucleusAnaphaseProphase
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