1993
Cloning of a Secretory Gelsolin from Drosophila melanogaster
Heintzelman M, Frankel S, Artavanis-Tsakonas S, Mooseker M. Cloning of a Secretory Gelsolin from Drosophila melanogaster. Journal Of Molecular Biology 1993, 230: 709-716. PMID: 8386771, DOI: 10.1006/jmbi.1993.1191.Peer-Reviewed Original ResearchConceptsSecretory gelsolinAcid sequenceThird instar Drosophila larvaeDeduced amino acid sequenceFull-length complementary DNAInstar Drosophila larvaeClass of proteinsActin-binding proteinsAmino acid sequenceAmino acid residuesGelsolin sequenceThird chromosomeDrosophila melanogasterGelsolin familyCytoplasmic proteinsSignal peptideSingle geneDrosophila larvaeRepeat structureActin filamentsMonomeric actinAcid residuesBarbed endsPrimary structureNorthern blot
1988
Characterization 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
1987
Nucleation 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
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 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 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 web
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