1997
Of Membrane Stability and Mosaics: The Spectrin Cytoskeleton
Morrow J, Rimm D, Kennedy S, Cianci C, Sinard J, Weed S. Of Membrane Stability and Mosaics: The Spectrin Cytoskeleton. 1997, 485-540. DOI: 10.1002/cphy.cp140111.Peer-Reviewed Original ResearchNon-erythroid cellsMembrane skeletonRed cell membrane skeletonSpectrin membrane skeletonCell membrane skeletonErythrocyte membrane skeletonMembrane organizersProtein 4.1Spectrin cytoskeletonAdhesion proteinsCytoskeletal elementsSpectrin skeletonMembrane stabilityMosaic modelSpectrinProteinCellsDematinDynaminStomatinPallidinCytoskeletonAnkyrinAdducinTropomodulin
1995
Reduced alpha-catenin and E-cadherin expression in breast cancer.
Rimm DL, Sinard JH, Morrow JS. Reduced alpha-catenin and E-cadherin expression in breast cancer. Laboratory Investigation 1995, 72: 506-12. PMID: 7745946.Peer-Reviewed Original ResearchConceptsE-cadherinSteady-state levelsE-cadherin expressionHomotypic cell adhesion proteinMetastatic diseaseCell adhesion proteinsHuman E-cadherinCell-cell interactionsCytoplasmic proteinsTime of biopsyAdhesion proteinsAggressive tumor behaviorAdhesive functionEffector elementsAdhesion cascadeAbsent E-cadherin expressionTypes of cancerJunctional complexesProteinBreast cancerEpithelial tumorsSensitive markerTumor behaviorExpressionCancer
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
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