1998
Dynamic Interaction of PTPμ with Multiple Cadherins In Vivo
Brady-Kalnay S, Mourton T, Nixon J, Pietz G, Kinch M, Chen H, Brackenbury R, Rimm D, Del Vecchio R, Tonks N. Dynamic Interaction of PTPμ with Multiple Cadherins In Vivo. Journal Of Cell Biology 1998, 141: 287-296. PMID: 9531566, PMCID: PMC2132733, DOI: 10.1083/jcb.141.1.287.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, MonoclonalCadherinsCell LineCell Line, TransformedCerebellumCross ReactionsElectrophoresis, Polyacrylamide GelHumansImmunoblottingMiceProtein Tyrosine PhosphatasesRatsReceptor-Like Protein Tyrosine Phosphatases, Class 2Receptor-Like Protein Tyrosine Phosphatases, Class 8Recombinant Fusion ProteinsRecombinant ProteinsSpodopteraTransfectionConceptsReversible tyrosine phosphorylationCadherin-catenin complexTyrosine phosphorylationE-cadherinWC5 cellsTemperature-sensitive mutant formPresence of cadherinCadherin functionV-SrcCytoplasmic segmentMultiple cadherinsCadherin-4PTPmuSf9 cellsMutant formsRegulatory mechanismsAdhesive functionCadherinN-cadherinPhosphorylationDirect interaction
1990
Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. II. Assembly properties of tails with NH2- and COOH-terminal deletions.
Sinard JH, Rimm DL, Pollard TD. Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. II. Assembly properties of tails with NH2- and COOH-terminal deletions. Journal Of Cell Biology 1990, 111: 2417-2426. PMID: 2177477, PMCID: PMC2116375, DOI: 10.1083/jcb.111.6.2417.Peer-Reviewed Original ResearchMeSH KeywordsAcanthamoebaAnimalsBase SequenceBinding SitesChromatographyChromatography, DEAE-CelluloseChromatography, GelChromosome DeletionCloning, MolecularDurapatiteElectrophoresis, Polyacrylamide GelEscherichia coliHydroxyapatitesKineticsMacromolecular SubstancesMagnesiumMicroscopy, ElectronMolecular Sequence DataMolecular WeightMyosinsPotassium ChlorideRecombinant Fusion ProteinsScattering, RadiationConceptsFusion proteinMyosin IIMyosin-II tailAntiparallel tetramersAmino acidsAmino acid residuesNative myosin IIRecombinant fusion proteinSequence altersAcid residuesTail sequencesNH2-terminalNonhelical domainAcanthamoeba myosin IIFunctional regionsProteinParacrystal formationAntiparallel dimerAssembly propertiesDimerization mechanismResiduesTerminal deletionDeletionAssemblyTight packing
1989
Purification and characterization of an Acanthamoeba nuclear actin-binding protein.
Rimm DL, Pollard TD. Purification and characterization of an Acanthamoeba nuclear actin-binding protein. Journal Of Cell Biology 1989, 109: 585-591. PMID: 2760108, PMCID: PMC2115709, DOI: 10.1083/jcb.109.2.585.Peer-Reviewed Original ResearchMeSH KeywordsAcanthamoebaActinsAnimalsAntibodies, MonoclonalCell FractionationCross ReactionsDNAElectrophoresis, Polyacrylamide GelMolecular WeightMyosinsNuclear ProteinsPeptide MappingProtein BindingConceptsActin-binding proteinsMyosin ITwo-dimensional peptide mapsAcanthamoeba myosin ICell fractionationATP-insensitive mannerCross-reactive proteinNuclear localizationAffinity-purified antibodiesAbsence of actinMyosin I.Actin filamentsProteinPeptide mapsMonoclonal antibodiesATPase activityPolyclonal antiserumProteolytic productsStokes radiusPolyclonal antibodiesCross-reactive monoclonal antibodiesColumn chromatographyPolypeptideActinDNA