2011
Intercellular protein movement in syncytial Drosophila follicle cells
Airoldi SJ, McLean PF, Shimada Y, Cooley L. Intercellular protein movement in syncytial Drosophila follicle cells. Journal Of Cell Science 2011, 124: 4077-4086. PMID: 22135360, PMCID: PMC3244987, DOI: 10.1242/jcs.090456.Peer-Reviewed Original ResearchConceptsImaginal disc cellsRing canalsFollicle cellsPavarotti kinesin-like proteinDrosophila follicle cellsIntercellular protein movementEgg chamber developmentKinesin-like proteinMitotic cleavage furrowsLive-cell confocal microscopyDisc cellsBroad functional significanceDrosophila germlineGermline cellsCytoplasmic proteinsSomatic cellsProtein movementCleavage furrowFunctional significanceChamber developmentSyncytial organizationConfocal microscopyGermlineProteinCells
2000
Physical and genetic interaction of filamin with presenilin in Drosophila
Guo Y, Zhang S, Sokol N, Cooley L, Boulianne G. Physical and genetic interaction of filamin with presenilin in Drosophila. Journal Of Cell Science 2000, 113: 3499-3508. PMID: 10984440, DOI: 10.1242/jcs.113.19.3499.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAlzheimer DiseaseAmino Acid SequenceAnimalsBlotting, WesternCarrier ProteinsCloning, MolecularContractile ProteinsDrosophila melanogasterEmbryo, NonmammalianFemaleFilaminsGene Expression Regulation, DevelopmentalHumansInsect ProteinsLarvaMaleMembrane ProteinsMicrofilament ProteinsMolecular Sequence DataPresenilin-1Presenilin-2Protein BindingProtein IsoformsProtein Structure, TertiaryRecombinant Fusion ProteinsRNA, MessengerTwo-Hybrid System TechniquesConceptsN-terminal actin-binding domainOverall amino acid identityOverexpression of presenilinFamilial Alzheimer's diseaseTransmembrane domain proteinActin-binding domainAmino acid identityLarge hydrophilic loopDrosophila filaminDomain proteinsGenetic interactionsAlternative splicingHydrophilic loopAcid identityTerminal domainDrosophilaHuman filaminChromosome 3Spliced formsFilaminAdult phenotypeLoop regionPresenilinNovel familyLong form
1999
Drosophila quail, a villin-related protein, bundles actin filaments in apoptotic nurse cells
Matova N, Mahajan-Miklos S, Mooseker M, Cooley L. Drosophila quail, a villin-related protein, bundles actin filaments in apoptotic nurse cells. Development 1999, 126: 5645-5657. PMID: 10572041, DOI: 10.1242/dev.126.24.5645.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActinsAmino Acid SequenceAnimalsApoptosisBiological TransportCalciumCarrier ProteinsCloning, MolecularCytoplasmDrosophila melanogasterEscherichia coliHumansInsect ProteinsMicrofilament ProteinsMolecular Sequence DataRecombinant Fusion ProteinsSequence Homology, Amino AcidConceptsEgg chambersNurse cellsFilamentous actinActin filamentsCytoplasm transportNuclear envelopeQuail proteinGermline-specific proteinsMutant egg chambersNurse cell apoptosisActin bundle assemblyNew actin filamentsApoptotic nurse cellsActin-regulating proteinsBundles actin filamentsHuman villinDrosophila germlineSequence homologyBiochemical experimentsActin bundlesElevated cytoplasmic calciumProteinVillinActinAbundant network
1994
The villin-like protein encoded by the Drosophila quail gene is required for actin bundle assembly during oogenesis
Mahajan-Miklos S, Cooley L. The villin-like protein encoded by the Drosophila quail gene is required for actin bundle assembly during oogenesis. Cell 1994, 78: 291-301. PMID: 8044841, DOI: 10.1016/0092-8674(94)90298-4.Peer-Reviewed Original ResearchConceptsVillin-like proteinNurse cellsActin filament bundlesQuail geneMutant egg chambersActin bundle assemblyFilament bundlesEgg chambersFemale sterilityAdult fliesCytoplasmic transportFilamentous actinGene resultsBundle assemblyActin filamentsQuail proteinProtein villinAbsorptive epithelial cellsStriking colocalizationProteinOogenesisVillinEpithelial cellsGenesCellsDrosophila singed, a fascin homolog, is required for actin bundle formation during oogenesis and bristle extension.
Cant K, Knowles BA, Mooseker MS, Cooley L. Drosophila singed, a fascin homolog, is required for actin bundle formation during oogenesis and bristle extension. Journal Of Cell Biology 1994, 125: 369-380. PMID: 8163553, PMCID: PMC2120035, DOI: 10.1083/jcb.125.2.369.Peer-Reviewed Original ResearchConceptsActin filament bundle formationActin filament bundlesSevere mutantsBundle formationFilament bundlesActin bundle formationBundles actin filamentsNurse cell nucleiDrosophila homologBristle phenotypeSocket cellsFemale sterileEgg chambersRing canalsCytoplasm transportSea urchin eggsNurse cellsActin bundlesCellular extensionsSevere allelesActin filamentsDrosophilaMutantsMigratory cellsFilopodial extensions
1986
The additional guanylate at the 5' terminus of Escherichia coli tRNAHis is the result of unusual processing by RNase P.
Orellana O, Cooley L, Söll D. The additional guanylate at the 5' terminus of Escherichia coli tRNAHis is the result of unusual processing by RNase P. Molecular And Cellular Biology 1986, 6: 525-529. PMID: 3023854, PMCID: PMC367542, DOI: 10.1128/mcb.6.2.525.Peer-Reviewed Original Research
1984
Transcriptionally active and inactive gene repeats within the D. meianogaster 5S RNA gene cluster
Sharp S, Garcia A, Cooley L, Söll D. Transcriptionally active and inactive gene repeats within the D. meianogaster 5S RNA gene cluster. Nucleic Acids Research 1984, 12: 7617-7632. PMID: 6093044, PMCID: PMC320189, DOI: 10.1093/nar/12.20.7617.Peer-Reviewed Original ResearchConceptsEfficiency of transcriptionRRNA gene copiesHigh transcription efficiencyTwo-nucleotide deletionD. melanogasterGene repeatRNA genesGene clusterPrimary transcriptGene copiesTranscription functionTranscription efficiencyTemplate activityCell extractsTranscriptionDNAPosition 28Position 86DNA typesRepeat unitsDeletionSame sequenceMelanogasterRRNAGenes