2003
Myosin-V motility: these levers were made for walking
Tyska M, Mooseker M. Myosin-V motility: these levers were made for walking. Trends In Cell Biology 2003, 13: 447-451. PMID: 12946621, DOI: 10.1016/s0962-8924(03)00172-7.Peer-Reviewed Original Research
2001
The Yeast Class V Myosins, Myo2p and Myo4p, Are Nonprocessive Actin-Based Motors
Reck-Peterson S, Tyska M, Novick P, Mooseker M. The Yeast Class V Myosins, Myo2p and Myo4p, Are Nonprocessive Actin-Based Motors. Journal Of Cell Biology 2001, 153: 1121-1126. PMID: 11381095, PMCID: PMC2174330, DOI: 10.1083/jcb.153.5.1121.Peer-Reviewed Original ResearchActinsAdenosine TriphosphateAnimalsAntibodiesBrainCalciumCalmodulin-Binding ProteinsCarrier ProteinsChickensFungal ProteinsKineticsMicroscopy, VideoMolecular Motor ProteinsMovementMyosin Heavy ChainsMyosin Type IIMyosin Type VMyosinsNerve Tissue ProteinsProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe Proteins
2000
Myosin-V stepping kinetics: A molecular model for processivity
Rief M, Rock R, Mehta A, Mooseker M, Cheney R, Spudich J. Myosin-V stepping kinetics: A molecular model for processivity. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 9482-9486. PMID: 10944217, PMCID: PMC16890, DOI: 10.1073/pnas.97.17.9482.Peer-Reviewed Original Research
1999
Myosin-V is a processive actin-based motor
Mehta A, Rock R, Rief M, Spudich J, Mooseker M, Cheney R. Myosin-V is a processive actin-based motor. Nature 1999, 400: 590-593. PMID: 10448864, DOI: 10.1038/23072.Peer-Reviewed Original Research
1995
Molecular motors, membrane movements and physiology: emerging roles for myosins
Hasson T, Mooseker M. Molecular motors, membrane movements and physiology: emerging roles for myosins. Current Opinion In Cell Biology 1995, 7: 587-594. PMID: 7495580, DOI: 10.1016/0955-0674(95)80017-4.Peer-Reviewed Original ResearchConceptsMembrane protein functionMolecular motorsProtein functionSignal transductionNovel myosinOrganelle transportATP hydrolysisActin filamentsCell locomotionLarge familyMembrane movementUbiquitous associationMechanical forcesActinMyosinMembrane phenomenaTransductionMechanoenzymesMechanoregulationPhysiologyRolePhagocytosisMembraneFilamentsFamily
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 web