1990
Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. I. High resolution epitope mapping and characterization of monoclonal antibody binding sites.
Rimm DL, Kaiser DA, Bhandari D, Maupin P, Kiehart DP, Pollard TD. Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. I. High resolution epitope mapping and characterization of monoclonal antibody binding sites. Journal Of Cell Biology 1990, 111: 2405-2416. PMID: 1703536, PMCID: PMC2116414, DOI: 10.1083/jcb.111.6.2405.Peer-Reviewed Original ResearchIdentification 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
Location of the head-tail junction of myosin.
Rimm DL, Sinard JH, Pollard TD. Location of the head-tail junction of myosin. Journal Of Cell Biology 1989, 108: 1783-1789. PMID: 2715178, PMCID: PMC2115540, DOI: 10.1083/jcb.108.5.1783.Peer-Reviewed Original ResearchMeSH KeywordsAcanthamoebaAnimalsCloning, MolecularDNAMicroscopy, ElectronModels, StructuralMyosinsProtein ConformationRecombinant ProteinsRestriction MappingConceptsMyosin IIHeptad repeatAcanthamoeba myosin IIHead-tail junctionCoiled-coil structureHydrophobic amino acidsNative myosin IIIdentical polypeptidesNH2 terminusMyosin-II tailNonmuscle myosinProteolytic separationLines of evidenceShort tailAmino acidsPosition 847RepeatsMyosinResiduesTailMyosin moleculesHeptadTerminusMonoclonal antibodiesPolypeptide
1986
Characterization of alpha‐actinin from Acanthamoeba
Pollard T, Tseng P, Rimm D, Bichell D, Williams R, Sinard J, Sato M. Characterization of alpha‐actinin from Acanthamoeba. Cytoskeleton 1986, 6: 649-661. PMID: 2948678, DOI: 10.1002/cm.970060613.Peer-Reviewed Original ResearchConceptsCross-linking proteinsActin filamentsActin filament cross-linking proteinCross-link actin filamentsCross-links actin filamentsAmino acid compositionAmoeba proteinApparent molecular weightActin polymerizationGlobular domainElectrophoretic variantsNative proteinCell extractsActin monomersPure proteinProteinGel electrophoresisAmoebaeCytoplasmic matrixStokes radiusMolecular weightPolypeptideAcid compositionIndirect fluorescent antibody stainingAntibody staining