2001
Caspase 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[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 strategiesPeptidesMembraneCellsOrganelles
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