2000
The light chain composition of chicken brain myosin‐Va: Calmodulin, myosin‐II essential light chains, and 8‐kDa dynein light chain/PIN
Espindola F, Suter D, Partata L, Cao T, Wolenski J, Cheney R, King S, Mooseker M. The light chain composition of chicken brain myosin‐Va: Calmodulin, myosin‐II essential light chains, and 8‐kDa dynein light chain/PIN. Cytoskeleton 2000, 47: 269-281. PMID: 11093248, DOI: 10.1002/1097-0169(200012)47:4<269::aid-cm2>3.0.co;2-g.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsBrainCalmodulinCalpainCarrier ProteinsCells, CulturedChick EmbryoChickensDrosophila ProteinsDyneinsElectrophoresis, Polyacrylamide GelFlagellaGanglia, SpinalImmunoglobulin GIntermediate Filament ProteinsMiceMicroscopy, FluorescenceMolecular Sequence DataMyosin Heavy ChainsMyosin Light ChainsMyosin Type VMyosinsNeuronsProtein BindingProtein Structure, TertiarySequence Analysis, Protein
1998
Human myosin-IXb is a mechanochemically active motor and a GAP for rho
Post P, Bokoch G, Mooseker M. Human myosin-IXb is a mechanochemically active motor and a GAP for rho. Journal Of Cell Science 1998, 111: 941-950. PMID: 9490638, DOI: 10.1242/jcs.111.7.941.Peer-Reviewed Original ResearchActinsAdenosine TriphosphateAlternative SplicingAmino Acid SequenceAnimalsCalciumCalmodulinGTP PhosphohydrolasesGTPase-Activating ProteinsGTP-Binding ProteinsHumansLeukocytesMolecular Sequence DataMuscle ContractionMyosinsProtein BindingProteinsRas GTPase-Activating ProteinsRas ProteinsRatsRho GTP-Binding Proteins
1994
Porcine myosin-VI: characterization of a new mammalian unconventional myosin.
Hasson T, Mooseker M. Porcine myosin-VI: characterization of a new mammalian unconventional myosin. Journal Of Cell Biology 1994, 127: 425-440. PMID: 7929586, PMCID: PMC2120210, DOI: 10.1083/jcb.127.2.425.Peer-Reviewed Original Research
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 ResearchCalcium-calmodulin and regulation of brush border myosin-I MgATPase and mechanochemistry
Wolenski J, Hayden S, Forscher P, Mooseker. Calcium-calmodulin and regulation of brush border myosin-I MgATPase and mechanochemistry. Journal Of Cell Biology 1993, 122: 613-621. PMID: 8335688, PMCID: PMC2119657, DOI: 10.1083/jcb.122.3.613.Peer-Reviewed Original Research
1992
Biochemical and immunological characterization of p190-calmodulin complex from vertebrate brain: a novel calmodulin-binding myosin.
Espindola F, Espreafico E, Coelho M, Martins A, Costa F, Mooseker M, Larson R. Biochemical and immunological characterization of p190-calmodulin complex from vertebrate brain: a novel calmodulin-binding myosin. Journal Of Cell Biology 1992, 118: 359-368. PMID: 1378447, PMCID: PMC2290054, DOI: 10.1083/jcb.118.2.359.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAnimalsAnimals, NewbornBrainCalmodulinCalmodulin-Binding ProteinsChickensCytoskeletal ProteinsElectrophoresis, Polyacrylamide GelEmbryonic and Fetal DevelopmentEpitopesFemaleImmunohistochemistryMaleMolecular WeightMyosinsNerve Tissue ProteinsOrgan SpecificityPurkinje CellsRabbitsRatsSpecies SpecificityConceptsCalmodulin-dependent kinase IIAdult forebrainMammalian brainPurkinje cellsImmunocytochemical studyDendritic extensionsRat tissuesImmunological characterizationImmunological evidencePost coitusImmunological recognitionCerebellumPolyclonal antibodiesBrainVertebrate brainMAbsEpitopesMg-ATPase activityKinase IIP190Brush border myosin IAction activationCa2Activity characteristicsForebrainUnconventional myosins
Cheney R, Mooseker M. Unconventional myosins. Current Opinion In Cell Biology 1992, 4: 27-35. PMID: 1558751, DOI: 10.1016/0955-0674(92)90055-h.Peer-Reviewed Original Research
1989
Partial deduced sequence of the 110-kD-calmodulin complex of the avian intestinal microvillus shows that this mechanoenzyme is a member of the myosin I family.
Garcia A, Coudrier E, Carboni J, Anderson J, Vandekerkhove J, Mooseker M, Louvard D, Arpin M. Partial deduced sequence of the 110-kD-calmodulin complex of the avian intestinal microvillus shows that this mechanoenzyme is a member of the myosin I family. Journal Of Cell Biology 1989, 109: 2895-2903. PMID: 2687288, PMCID: PMC2115973, DOI: 10.1083/jcb.109.6.2895.Peer-Reviewed Original ResearchThe 110-kD protein-calmodulin complex of the intestinal microvillus (brush border myosin I) is a mechanoenzyme.
Mooseker M, Coleman T. The 110-kD protein-calmodulin complex of the intestinal microvillus (brush border myosin I) is a mechanoenzyme. Journal Of Cell Biology 1989, 108: 2395-2400. PMID: 2525564, PMCID: PMC2115599, DOI: 10.1083/jcb.108.6.2395.Peer-Reviewed Original Research
1987
Assembly of the intestinal brush border: appearance and redistribution of microvillar core proteins in developing chick enterocytes.
Shibayama T, Carboni J, Mooseker M. Assembly of the intestinal brush border: appearance and redistribution of microvillar core proteins in developing chick enterocytes. Journal Of Cell Biology 1987, 105: 335-344. PMID: 2956268, PMCID: PMC2114914, DOI: 10.1083/jcb.105.1.335.Peer-Reviewed Original ResearchThe 110-kD protein-calmodulin complex of the intestinal microvillus is an actin-activated MgATPase.
Conzelman K, Mooseker M. The 110-kD protein-calmodulin complex of the intestinal microvillus is an actin-activated MgATPase. Journal Of Cell Biology 1987, 105: 313-324. PMID: 2956266, PMCID: PMC2114910, DOI: 10.1083/jcb.105.1.313.Peer-Reviewed Original Research
1986
Reevaluation of the hydrophobic nature of the 110‐kD calmodulin‐, actin‐, and membrane‐binding protein of the intestinal microvillus
Conzelman K, Mooseker M. Reevaluation of the hydrophobic nature of the 110‐kD calmodulin‐, actin‐, and membrane‐binding protein of the intestinal microvillus. Journal Of Cellular Biochemistry 1986, 30: 271-279. PMID: 3700495, DOI: 10.1002/jcb.240300308.Peer-Reviewed Original Research
1985
Organization, Chemistry, and Assembly of the Cytoskeletal Apparatus of the Intestinal Brush Border
Mooseker M. Organization, Chemistry, and Assembly of the Cytoskeletal Apparatus of the Intestinal Brush Border. Annual Review Of Cell And Developmental Biology 1985, 1: 209-241. PMID: 3916317, DOI: 10.1146/annurev.cb.01.110185.001233.Peer-Reviewed Original Research
1984
Brush border cytoskeleton and integration of cellular functions.
Mooseker M, Bonder E, Conzelman K, Fishkind D, Howe C, Keller T. Brush border cytoskeleton and integration of cellular functions. Journal Of Cell Biology 1984, 99: 104s-112s. PMID: 6378918, PMCID: PMC2275581, DOI: 10.1083/jcb.99.1.104s.Peer-Reviewed Original ResearchCalcium-dependent regulation of cytoskeletal structure and contractility in the intestinal brush border.
Mooseker M. Calcium-dependent regulation of cytoskeletal structure and contractility in the intestinal brush border. Progress In Clinical And Biological Research 1984, 168: 179-86. PMID: 6542665.Peer-Reviewed Original Research
1983
Actin binding proteins of the brush border
Mooseker M. Actin binding proteins of the brush border. Cell 1983, 35: 11-13. PMID: 6313218, DOI: 10.1016/0092-8674(83)90202-7.Peer-Reviewed Original ResearchCharacterization of the 110-kdalton actin-calmodulin-, and membrane-binding protein from microvilli of intestinal epithelial cells.
Howe C, Mooseker M. Characterization of the 110-kdalton actin-calmodulin-, and membrane-binding protein from microvilli of intestinal epithelial cells. Journal Of Cell Biology 1983, 97: 974-985. PMID: 6311843, PMCID: PMC2112603, DOI: 10.1083/jcb.97.4.974.Peer-Reviewed Original Research
1982
Ca++-calmodulin-dependent phosphorylation of myosin, and its role in brush border contraction in vitro.
Keller T, Mooseker M. Ca++-calmodulin-dependent phosphorylation of myosin, and its role in brush border contraction in vitro. Journal Of Cell Biology 1982, 95: 943-959. PMID: 6897550, PMCID: PMC2112925, DOI: 10.1083/jcb.95.3.943.Peer-Reviewed Original ResearchConceptsBrush border contractionBrush borderIntestinal epithelial cellsEpithelial cellsCalmodulin activityBrush border proteinsMyosin light chain kinaseContractionDegrees CLight chain kinaseLight chainCalmodulin-dependent phosphorylationBrush border myosinPhosphorylationDalton light chainChain kinaseTerminal webAnalysis of cytoskeletal proteins and Ca2+-dependent regulation of structure in intestinal brush borders from rachitic chicks
Howe C, Keller T, Mooseker M, Wasserman R. Analysis of cytoskeletal proteins and Ca2+-dependent regulation of structure in intestinal brush borders from rachitic chicks. Proceedings Of The National Academy Of Sciences Of The United States Of America 1982, 79: 1134-1138. PMID: 6951164, PMCID: PMC345915, DOI: 10.1073/pnas.79.4.1134.Peer-Reviewed Original Research
1980
Brush-border calmodulin. A major component of the isolated microvillus core.
Howe C, Mooseker M, Graves T. Brush-border calmodulin. A major component of the isolated microvillus core. Journal Of Cell Biology 1980, 85: 916-923. PMID: 6893051, PMCID: PMC2111444, DOI: 10.1083/jcb.85.3.916.Peer-Reviewed Original Research