1999
An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin
Zhou D, Mooseker M, Galán J. An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 10176-10181. PMID: 10468582, PMCID: PMC17862, DOI: 10.1073/pnas.96.18.10176.Peer-Reviewed Original ResearchConceptsActin-bundling activityT-plastinBacterial-host cell contactHost cell signal transduction pathwaysHost cellsType III secretion systemBacterial effector proteinsActin-binding proteinsSignal transduction pathwaysBacterial effectorsMembrane rufflesEffector proteinsActin cytoskeletonMembrane rufflingSecretion systemSalmonella proteinsBacterial entryBacterial internalizationSalmonella entrySignaling processesActin filamentsF-actinNonphagocytic cellsProteinCell contact
1989
Phosphorylation of the tight-junction protein ZO-1 in two strains of Madin-Darby canine kidney cells which differ in transepithelial resistance
Stevenson B, Anderson J, Braun I, Mooseker M. Phosphorylation of the tight-junction protein ZO-1 in two strains of Madin-Darby canine kidney cells which differ in transepithelial resistance. Biochemical Journal 1989, 263: 597-599. PMID: 2597123, PMCID: PMC1133468, DOI: 10.1042/bj2630597.Peer-Reviewed Original ResearchZO-1 and cingulin: tight junction proteins with distinct identities and localizations
Stevenson B, Heintzelman M, Anderson J, Citi S, Mooseker M. ZO-1 and cingulin: tight junction proteins with distinct identities and localizations. American Journal Of Physiology 1989, 257: c621-c628. PMID: 2679124, DOI: 10.1152/ajpcell.1989.257.4.c621.Peer-Reviewed Original ResearchConceptsCell-cell contactPlasma membraneHepatoma tissue cultureZO-1MDCK cellsMadin-Darby canine kidney cellsCanine kidney cellsSubconfluent MDCK cellsSingle polypeptideCingulinHepatoma cell lineMolecular massChicken small intestineDistinct localizationImmunoblot analysisJunctional membranesImmunofluorescent localizationCell linesKidney cellsJunction proteinsKidney distalTight junctionsChicken intestineConfluent monolayersProteinZO-1 mRNA and protein expression during tight junction assembly in Caco-2 cells.
Anderson J, Van Itallie C, Peterson M, Stevenson B, Carew E, Mooseker M. ZO-1 mRNA and protein expression during tight junction assembly in Caco-2 cells. Journal Of Cell Biology 1989, 109: 1047-1056. PMID: 2670954, PMCID: PMC2115763, DOI: 10.1083/jcb.109.3.1047.Peer-Reviewed Original ResearchHepatic 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
Tight junction structure and ZO-1 content are identical in two strains of Madin-Darby canine kidney cells which differ in transepithelial resistance.
Stevenson B, Anderson J, Goodenough D, Mooseker M. Tight junction structure and ZO-1 content are identical in two strains of Madin-Darby canine kidney cells which differ in transepithelial resistance. Journal Of Cell Biology 1988, 107: 2401-2408. PMID: 3058723, PMCID: PMC2115690, DOI: 10.1083/jcb.107.6.2401.Peer-Reviewed Original ResearchCharacterization 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 ResearchA domain of synapsin I involved with actin bundling shares immunologic cross‐reactivity with villin
Petrucci T, Mooseker M, Morrow J. A domain of synapsin I involved with actin bundling shares immunologic cross‐reactivity with villin. Journal Of Cellular Biochemistry 1988, 36: 25-35. PMID: 3125185, DOI: 10.1002/jcb.240360104.Peer-Reviewed Original ResearchConceptsBovine synapsin ISynapsin IActin binding proteinsPeptide mappingTwo-dimensional peptide mapsSmall synaptic vesiclesPhosphorylation controlBundling proteinActin bindingUnrelated proteinsActin bundlesActin filamentsNeuronal phosphoproteinSynapsin I.Binding proteinVivo roleSynaptic vesiclesParent proteinProteinPeptide mapsChymotryptic digestionVillinPeptide fragmentsCross reactFragments
1987
Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding.
Mische S, Mooseker M, Morrow J. Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding. Journal Of Cell Biology 1987, 105: 2837-2845. PMID: 3693401, PMCID: PMC2114693, DOI: 10.1083/jcb.105.6.2837.Peer-Reviewed Original Research