2008
Myo2p, a class V myosin in budding yeast, associates with a large ribonucleic acid–protein complex that contains mRNAs and subunits of the RNA-processing body
Chang W, Zaarour RF, Reck-Peterson S, Rinn J, Singer RH, Snyder M, Novick P, Mooseker MS. Myo2p, a class V myosin in budding yeast, associates with a large ribonucleic acid–protein complex that contains mRNAs and subunits of the RNA-processing body. RNA 2008, 14: 491-502. PMID: 18218704, PMCID: PMC2248268, DOI: 10.1261/rna.665008.Peer-Reviewed Original ResearchMeSH KeywordsActinsAdenosine TriphosphatasesBase SequenceDNA PrimersMacromolecular SubstancesMyosin Heavy ChainsMyosin Type VOligonucleotide Array Sequence AnalysisOrganellesPolyribosomesRibonucleoproteinsRNA Processing, Post-TranscriptionalRNA, FungalRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSecretory VesiclesVacuolesConceptsRNA processing bodiesClass V myosinsP-bodiesRelease of mRNAProcessing bodiesOrganelle traffickingSpindle orientationMotor mutantsMyo2-66Ribosomal subunitMyo2pProtein subunitsPartial colocalizationMicroarray analysisSubunitsSedimentation analysisYeastMRNAComplexesMyosinMutantsPolysomesTraffickingRNAColocalization
1993
Brain myosin-V is a two-headed unconventional myosin with motor activity
Cheney R, O'Shea M, Heuser J, Coelho M, Wolenski J, Espreafico E, Forscher P, Larson R, Mooseker M. Brain myosin-V is a two-headed unconventional myosin with motor activity. Cell 1993, 75: 13-23. PMID: 8402892, DOI: 10.1016/s0092-8674(05)80080-7.Peer-Reviewed Original Research
1992
Localization of capping protein in chicken epithelial cells by immunofluorescence and biochemical fractionation.
Schafer D, Mooseker M, Cooper J. Localization of capping protein in chicken epithelial cells by immunofluorescence and biochemical fractionation. Journal Of Cell Biology 1992, 118: 335-346. PMID: 1629237, PMCID: PMC2290044, DOI: 10.1083/jcb.118.2.335.Peer-Reviewed Original ResearchMeSH KeywordsActin Depolymerizing FactorsActinsAnimalsAntibodiesCells, CulturedChick EmbryoChickensCochleaDestrinElectrophoresis, Polyacrylamide GelEpithelial CellsEpitheliumFluorescent Antibody TechniqueIntestinesKidneyMacromolecular SubstancesMicrofilament ProteinsMicrovilliMusclesPigment Epithelium of EyeSubcellular FractionsConceptsIntestinal epithelial cellsNuclei of cellsBiochemical fractionationJunctional complexesActin filamentsCell-cell junctional complexesSingle intestinal epithelial cellsBarbed endsEpithelial cellsSensory epitheliumCell-cell contactIntact intestinal epithelial cellsAffinity-purified polyclonal antibodiesProtein bindsCapping proteinIntestinal epitheliumZonula adherensCell junctionsChick embryo kidney cellsPattern coincidentEmbryo kidney cellsProteinConfocal microscopyKidney cellsIsolated intestinal epithelial cells
1989
Characterization of intestinal microvillar membrane disks: detergent-resistant membrane sheets enriched in associated brush border myosin I (110K-calmodulin).
Mooseker M, Conzelman K, Coleman T, Heuser J, Sheetz M. Characterization of intestinal microvillar membrane disks: detergent-resistant membrane sheets enriched in associated brush border myosin I (110K-calmodulin). Journal Of Cell Biology 1989, 109: 1153-1161. PMID: 2527857, PMCID: PMC2115773, DOI: 10.1083/jcb.109.3.1153.Peer-Reviewed Original Research
1987
Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding.
Mische S, Mooseker M, Morrow J. Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding. Journal Of Cell Biology 1987, 105: 2837-2845. PMID: 3693401, PMCID: PMC2114693, DOI: 10.1083/jcb.105.6.2837.Peer-Reviewed Original ResearchMeSH KeywordsActinsCalmodulin-Binding ProteinsErythrocyte MembraneHumansKineticsMacromolecular SubstancesMembrane ProteinsMolecular WeightPhosphoproteinsProtein BindingSpectrinConceptsSpectrin-actin bindingNucleation of actin polymerization by villin and elongation at subcritical monomer concentration.
Weber A, Northrop J, Bishop M, Ferrone F, Mooseker M. Nucleation of actin polymerization by villin and elongation at subcritical monomer concentration. Biochemistry 1987, 26: 2528-36. PMID: 3607030, DOI: 10.1021/bi00383a019.Peer-Reviewed Original ResearchKinetics of actin elongation and depolymerization at the pointed end.
Weber A, Northrop J, Bishop M, Ferrone F, Mooseker M. Kinetics of actin elongation and depolymerization at the pointed end. Biochemistry 1987, 26: 2537-44. PMID: 3607031, DOI: 10.1021/bi00383a020.Peer-Reviewed Original Research
1986
Different calcium dependence of the capping and cutting activities of villin.
Northrop J, Weber A, Mooseker M, Franzini-Armstrong C, Bishop M, Dubyak G, Tucker M, Walsh T. Different calcium dependence of the capping and cutting activities of villin. Journal Of Biological Chemistry 1986, 261: 9274-9281. PMID: 3087992, DOI: 10.1016/s0021-9258(18)67650-1.Peer-Reviewed Original Research
1984
Calcium dependence of villin-induced actin depolymerization.
Walsh T, Weber A, Davis K, Bonder E, Mooseker M. Calcium dependence of villin-induced actin depolymerization. Biochemistry 1984, 23: 6099-102. PMID: 6525347, DOI: 10.1021/bi00320a030.Peer-Reviewed Original ResearchEffect of villin on the kinetics of actin polymerization.
Walsh T, Higgins J, Weber A, Bonder E, Mooseker M. Effect of villin on the kinetics of actin polymerization. Biochemistry 1984, 23: 2613-21. PMID: 6432033, DOI: 10.1021/bi00307a012.Peer-Reviewed Original Research
1983
Actin from Thyone sperm assembles on only one end of an actin filament: a behavior regulated by profilin.
Tilney L, Bonder E, Coluccio L, Mooseker M. Actin from Thyone sperm assembles on only one end of an actin filament: a behavior regulated by profilin. Journal Of Cell Biology 1983, 97: 112-124. PMID: 6863386, PMCID: PMC2112487, DOI: 10.1083/jcb.97.1.112.Peer-Reviewed Original Research
1980
Regulation of microvillus structure: calcium-dependent solation and cross-linking of actin filaments in the microvilli of intestinal epithelial cells.
Mooseker M, Graves T, Wharton K, Falco N, Howe C. Regulation of microvillus structure: calcium-dependent solation and cross-linking of actin filaments in the microvilli of intestinal epithelial cells. Journal Of Cell Biology 1980, 87: 809-822. PMID: 6893989, PMCID: PMC2110803, DOI: 10.1083/jcb.87.3.809.Peer-Reviewed Original Research