1994
Differential regulation of skeletal muscle myosin‐II and brush border myosin‐I enzymology and mechanochemistry by bacterially produced tropomyosin isoforms
Fanning A, Wolenski J, Mooseker M, Izant J. Differential regulation of skeletal muscle myosin‐II and brush border myosin‐I enzymology and mechanochemistry by bacterially produced tropomyosin isoforms. Cytoskeleton 1994, 29: 29-45. PMID: 7820856, DOI: 10.1002/cm.970290104.Peer-Reviewed Original ResearchMeSH KeywordsActinsAmino Acid SequenceAnimalsCa(2+) Mg(2+)-ATPaseCarrier ProteinsCell MovementChick EmbryoDNA, ComplementaryEscherichia coliIntestinal MucosaMicrofilament ProteinsMicrovilliMolecular Sequence DataMolecular WeightMuscle ProteinsMyosinsProtein BindingRecombinant Fusion ProteinsRecombinant ProteinsSequence HomologySpecies SpecificityTropomyosinVertebratesXenopusConceptsAlpha-tropomyosinMuscle myosin IIMyosin enzymologyMyosin isoformsTwo- toStriated MuscleMgATPase activityDifferential regulationBrush border myosinDetectable effectIsoformsLow affinityChimeric tropomyosinsMuscle tropomyosinMuscle alpha-tropomyosinSkeletal muscle myosin IIActinTropomyosin isoformsMuscle myosinF-actin
1993
An in vitro model for the analysis of intestinal brush border assembly. II. Changes in expression and localization of brush border proteins during cell contact-induced brush border assembly in Caco-2BBe cells.
Peterson M, Bement W, Mooseker M. An in vitro model for the analysis of intestinal brush border assembly. II. Changes in expression and localization of brush border proteins during cell contact-induced brush border assembly in Caco-2BBe cells. Journal Of Cell Science 1993, 105 ( Pt 2): 461-72. PMID: 8408277, DOI: 10.1242/jcs.105.2.461.Peer-Reviewed Original ResearchActinsAdenocarcinomaAmino Acid SequenceAnimalsBiomarkersBirdsCarrier ProteinsCattleCell CommunicationCell PolarityClone CellsColonic NeoplasmsCytoskeletonGene Expression Regulation, NeoplasticHumansIntestinal MucosaMicrofilament ProteinsMicrovilliMolecular Sequence DataMyosinsNeoplasm ProteinsOligo-1,6-GlucosidaseSequence AlignmentSequence Homology, Amino AcidSpecies SpecificitySucraseTumor Cells, Cultured
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 characteristicsForebrain
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 Research
1988
Characterization of ZO-1, a protein component of the tight junction from mouse liver and Madin-Darby canine kidney cells.
Anderson J, Stevenson B, Jesaitis L, Goodenough D, Mooseker M. Characterization of ZO-1, a protein component of the tight junction from mouse liver and Madin-Darby canine kidney cells. Journal Of Cell Biology 1988, 106: 1141-1149. PMID: 2452168, PMCID: PMC2115004, DOI: 10.1083/jcb.106.4.1141.Peer-Reviewed Original ResearchCharacterization of villin from the intestinal brush border of the rat, and comparative analysis with avian villin
Alicea H, Mooseker M. Characterization of villin from the intestinal brush border of the rat, and comparative analysis with avian villin. Cytoskeleton 1988, 9: 60-72. PMID: 3356045, DOI: 10.1002/cm.970090107.Peer-Reviewed Original Research