2005
A role for myosin VI in postsynaptic structure and glutamate receptor endocytosis
Osterweil E, Wells D, Mooseker M. A role for myosin VI in postsynaptic structure and glutamate receptor endocytosis. Journal Of Cell Biology 2005, 168: 329-338. PMID: 15657400, PMCID: PMC2171578, DOI: 10.1083/jcb.200410091.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex 2Adaptor Proteins, Signal TransducingAdenosine TriphosphateAlpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic AcidAnimalsAstrocytesBrainBrain ChemistryDendritesDendritic SpinesDiscs Large Homolog 1 ProteinDyneinsEndocytosisFemaleGlial Fibrillary Acidic ProteinGuanylate KinasesInsulinMaleMembrane ProteinsMiceMice, Inbred C57BLMice, Mutant StrainsMicrofilament ProteinsMicroscopy, ElectronMyosin Heavy ChainsMyosin VIIaMyosinsNerve Tissue ProteinsNeuronsReceptors, AMPAReceptors, GlutamateSucroseSynapsesSynaptic MembranesSynaptosomesTransferrinConceptsHippocampal neuronsDendritic spinesIsoxazole propionic acid-type glutamate receptorsWild-type hippocampal neuronsShort dendritic spinesNumber of synapsesSynapse lossNeurons displaySynapse numberGlutamate receptorsNervous systemNonneuronal cellsPostsynaptic structuresSynaptic structurePostsynaptic densityDominant negative disruptionSignificant deficitsAstrogliosisNeuronsBrainMYO6SpineSynapsesReceptor endocytosisMyosin VI
1998
Molecular Genetic Dissection of Mouse Unconventional Myosin-VA: Head Region Mutations
Huang J, Cope M, Mermall V, Strobel M, Kendrick-Jones J, Russell L, Mooseker M, Copeland N, Jenkins N. Molecular Genetic Dissection of Mouse Unconventional Myosin-VA: Head Region Mutations. Genetics 1998, 148: 1951-1961. PMID: 9560408, PMCID: PMC1460099, DOI: 10.1093/genetics/148.4.1951.Peer-Reviewed Original ResearchMolecular Genetic Dissection of Mouse Unconventional Myosin-VA: Tail Region Mutations
Huang J, Mermall V, Strobel M, Russell L, Mooseker M, Copeland N, Jenkins N. Molecular Genetic Dissection of Mouse Unconventional Myosin-VA: Tail Region Mutations. Genetics 1998, 148: 1963-1972. PMID: 9560409, PMCID: PMC1460104, DOI: 10.1093/genetics/148.4.1963.Peer-Reviewed Original ResearchConceptsMyosin VaMolecular genetic dissectionMammalian myosinGenetic dissectionProper foldingTail mutationsAlternative splicingColor locusDilute allelesSequencing approachSpecific functionsMutationsTail functionRegion mutationsFirst extensive collectionRT-PCRExtensive collectionSplicingLociTailFoldingIsoformsAllelesCargoSequence
1997
Effects of shaker‐1 mutations on myosin‐VIIa protein and mRNA expression
Hasson T, Walsh J, Cable J, Mooseker M, Brown S, Steel K. Effects of shaker‐1 mutations on myosin‐VIIa protein and mRNA expression. Cytoskeleton 1997, 37: 127-138. PMID: 9186010, DOI: 10.1002/(sici)1097-0169(1997)37:2<127::aid-cm5>3.0.co;2-5.Peer-Reviewed Original ResearchConceptsShaker-1 mutationsWild-type levelsNorthern blot analysisMammalian diseasesActin cytoskeletonMyosin VIIaShaker-1 miceGene expressionUnconventional myosinMRNA expressionProteinMyosin-VIIa mutationsImmunoblot analysisMotor domainRange of expressionMutationsBlot analysisAllelesProtein expressionTissue functionExpressionLife spanSH1Inner earLight microscopic level
1996
Myosin VIIA mutation screening in 189 Usher syndrome type 1 patients.
Weston M, Kelley P, Overbeck L, Wagenaar M, Orten D, Hasson T, Chen Z, Corey D, Mooseker M, Sumegi J, Cremers C, Moller C, Jacobson S, Gorin M, Kimberling W. Myosin VIIA mutation screening in 189 Usher syndrome type 1 patients. American Journal Of Human Genetics 1996, 59: 1074-83. PMID: 8900236, PMCID: PMC1914835.Peer-Reviewed Original ResearchConceptsCongenital profound hearing lossMyosin-VIIa mutationsType 1 patientsProfound hearing lossUsher syndrome type 1BUnique mutationsPresence of mutationsAutosomal recessive disorderVestibular abnormalitiesMyosin VIIA geneHearing lossRetinitis pigmentosaPatientsType 1bI casesRecessive disorderSingle caseCompound heterozygotesPremature stop codonSimple heterozygotesGreater percentageUnrelated control samplesDisordersMutant allelesCurrent studyMapping of Unconventional Myosins in Mouse and Human
Hasson T, Skowron J, Gilbert D, Avraham K, Perry W, Bement W, Anderson B, Sherr E, Chen Z, Greene L, Ward D, Corey D, Mooseker M, Copeland N, Jenkins N. Mapping of Unconventional Myosins in Mouse and Human. Genomics 1996, 36: 431-439. PMID: 8884266, DOI: 10.1006/geno.1996.0488.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 characteristicsForebrain
1989
Hepatic immunohistochemical localization of the tight junction protein ZO-1 in rat models of cholestasis.
Anderson J, Glade J, Stevenson B, Boyer J, Mooseker M. Hepatic immunohistochemical localization of the tight junction protein ZO-1 in rat models of cholestasis. American Journal Of Pathology 1989, 134: 1055-62. PMID: 2719075, PMCID: PMC1879891.Peer-Reviewed Original ResearchConceptsZO-1 proteinZO-1Tight junctionsConsecutive daily subcutaneous injectionsFrozen sectionsReflux of bileDaily subcutaneous injectionsBile duct obstructionCommon bile ductMale Sprague-DawleyHepatocyte tight junctionsBile duct ligation resultsTight junction protein ZO-1Cholestatic modelsDuct obstructionBile ductSubcutaneous injectionCholestatic liverRat modelEthinyl estradiolSprague-DawleyProtein ZO-1Immunoperoxidase stainingZO-1 stainingImmunohistochemical localization
1988
Localization of villin, a cytoskeletal protein specific to microvilli, in human ileum and colon and in colonic neoplasms
West A, Isaac C, Carboni J, Morrow J, Mooseker M, Barwick K. Localization of villin, a cytoskeletal protein specific to microvilli, in human ileum and colon and in colonic neoplasms. Gastroenterology 1988, 94: 343-352. PMID: 3335311, DOI: 10.1016/0016-5085(88)90421-0.Peer-Reviewed Original Research
1986
Cytochalasin B slows but does not prevent monomer addition at the barbed end of the actin filament.
Bonder E, Mooseker M. Cytochalasin B slows but does not prevent monomer addition at the barbed end of the actin filament. Journal Of Cell Biology 1986, 102: 282-288. PMID: 3941155, PMCID: PMC2114038, DOI: 10.1083/jcb.102.1.282.Peer-Reviewed Original Research
1985
Actin assembly and filament cross‐linking in the presence of TW 260/240, the tissue‐specific spectrin of the chicken intestinal brush border
Fishkind D, Mooseker M, Bonder E. Actin assembly and filament cross‐linking in the presence of TW 260/240, the tissue‐specific spectrin of the chicken intestinal brush border. Cytoskeleton 1985, 5: 311-322. PMID: 4042144, DOI: 10.1002/cm.970050404.Peer-Reviewed Original Research
1983
Direct measurement of critical concentrations and assembly rate constants at the two ends of an actin filament
Bonder E, Fishkind D, Mooseker M. Direct measurement of critical concentrations and assembly rate constants at the two ends of an actin filament. Cell 1983, 34: 491-501. PMID: 6684506, DOI: 10.1016/0092-8674(83)90382-3.Peer-Reviewed Original ResearchActin 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 ResearchDirect electron microscopic visualization of barbed end capping and filament cutting by intestinal microvillar 95-kdalton protein (villin): a new actin assembly assay using the limulus acrosomal process
Bonder E, Mooseker M. Direct electron microscopic visualization of barbed end capping and filament cutting by intestinal microvillar 95-kdalton protein (villin): a new actin assembly assay using the limulus acrosomal process. Journal Of Cell Biology 1983, 96: 1097-1107. PMID: 6682116, PMCID: PMC2112331, DOI: 10.1083/jcb.96.4.1097.Peer-Reviewed Original Research
1976
Actin filament-membrane attachment: are membrane particles involved?
Tilney L, Mooseker M. Actin filament-membrane attachment: are membrane particles involved? Journal Of Cell Biology 1976, 71: 402-416. PMID: 1033184, PMCID: PMC2109749, DOI: 10.1083/jcb.71.2.402.Peer-Reviewed Original Research
1973
MICROTUBULES: EVIDENCE FOR 13 PROTOFILAMENTS
Tilney L, Bryan J, Bush D, Fujiwara K, Mooseker M, Murphy D, Snyder D. MICROTUBULES: EVIDENCE FOR 13 PROTOFILAMENTS. Journal Of Cell Biology 1973, 59: 267-275. PMID: 4805001, PMCID: PMC2109099, DOI: 10.1083/jcb.59.2.267.Peer-Reviewed Original ResearchTHE POLYMERIZATION OF ACTIN: ITS ROLE IN THE GENERATION OF THE ACROSOMAL PROCESS OF CERTAIN ECHINODERM SPERM
Tilney L, Hatano S, Ishikawa H, Mooseker M. THE POLYMERIZATION OF ACTIN: ITS ROLE IN THE GENERATION OF THE ACROSOMAL PROCESS OF CERTAIN ECHINODERM SPERM. Journal Of Cell Biology 1973, 59: 109-126. PMID: 4356568, PMCID: PMC2110911, DOI: 10.1083/jcb.59.1.109.Peer-Reviewed Original ResearchConceptsSperm actinAcrosomal processGel electrophoresisUnreacted spermSodium dodecyl sulfate gel electrophoresisDodecyl sulfate gel electrophoresisMuscle myosinMuscle F-actinPolymerization of actinHeavy meromyosin bindingSulfate gel electrophoresisEchinoderm spermF-actinSDS gel electrophoresisMonomeric stateDetergent Triton XSkeletal muscle myosinActinAcrosomal regionBundles of microfilamentsAcrosomal capMicrofilamentsSame molecular weightSperm extractsEgg jelly