2001
[42] ADP-ribosylation factor (ARF) as regulator of spectrin assembly at Golgi complex
De Matteis M, Morrow J. [42] ADP-ribosylation factor (ARF) as regulator of spectrin assembly at Golgi complex. Methods In Enzymology 2001, 329: 405-416. PMID: 11210560, DOI: 10.1016/s0076-6879(01)29101-0.Peer-Reviewed Original ResearchMeSH KeywordsADP-Ribosylation FactorsAnimalsCell LineCell Membrane PermeabilityCoat Protein Complex IDNA PrimersElectrophoresis, Polyacrylamide GelEscherichia coliFluorescent Antibody TechniqueGenetic VectorsGolgi ApparatusIntracellular MembranesPeptide FragmentsProtein BindingRecombinant Fusion ProteinsSpectrinConceptsADP-ribosylation factorGolgi membranesSpectrin peptidesPermeabilized cultured cellsBinding of spectrinCultured cell linesDifferent functional domainsSpectrin assemblySequence motifsRibosylation factorIndirect immunofluorescent microscopyFunctional domainsIntracellular distributionCultured cellsSpectrinΒIII spectrinImmunofluorescence analysisCell linesGolgiImmunofluorescent microscopyExperimental strategiesPeptidesMembraneCellsOrganellesCaspase Remodeling of the Spectrin Membrane Skeleton during Lens Development and Aging*
Lee A, Morrow J, Fowler V. Caspase Remodeling of the Spectrin Membrane Skeleton during Lens Development and Aging*. Journal Of Biological Chemistry 2001, 276: 20735-20742. PMID: 11278555, DOI: 10.1074/jbc.m009723200.Peer-Reviewed Original ResearchConceptsLens fiber cellsFiber cellsMembrane blebbingMembrane skeletonLens developmentAlpha-spectrinSpectrin membrane skeletonMembrane skeleton componentsChick lens developmentCell-cell fusionApoptotic cellsOldest fiber cellsMembrane associationClassical apoptosisApoptotic processSpecific proteolysisTerminal differentiationAdult lensSpectrin fragmentsMembrane interdigitationsBlebbingCytoskeletal protein alpha-spectrinPermanent remodelingSkeleton componentsSpectrin
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