2005
Coexpression of β1,6-N-Acetylglucosaminyltransferase V Glycoprotein Substrates Defines Aggressive Breast Cancers with Poor Outcome
Siddiqui SF, Pawelek J, Handerson T, Lin CY, Dickson RB, Rimm DL, Camp RL. Coexpression of β1,6-N-Acetylglucosaminyltransferase V Glycoprotein Substrates Defines Aggressive Breast Cancers with Poor Outcome. Cancer Epidemiology Biomarkers & Prevention 2005, 14: 2517-2523. PMID: 16284372, DOI: 10.1158/1055-9965.epi-05-0464.Peer-Reviewed Original ResearchConceptsSubstrate proteinsEpidermal growth factor receptorGrowth factor receptorLAMP-1Glycoprotein substratesFactor receptorComplex oligosaccharide side chainsN-cadherin expressionTumor progressionOligosaccharide side chainsBeta1 integrin expressionGnT-VN-cadherinUnsupervised hierarchical clusteringN-acetylglucosaminyltransferaseMatriptaseDistinct clustersProteinProtein expressionTumor metastasisExpressionHigh expressionAggressive breast cancerLow expressionSide chains
2001
Truncated DCC Reduces N-Cadherin/Catenin Expression and Calcium-Dependent Cell Adhesion in Neuroblastoma Cells
Reyes-Múgica M, Meyerhardt J, Rzasa J, Rimm D, Johnson K, Wheelock M, Reale M. Truncated DCC Reduces N-Cadherin/Catenin Expression and Calcium-Dependent Cell Adhesion in Neuroblastoma Cells. Laboratory Investigation 2001, 81: 201-210. PMID: 11232642, DOI: 10.1038/labinvest.3780228.Peer-Reviewed Original ResearchMeSH KeywordsAlpha CateninBeta CateninCadherinsCalciumCell AdhesionCell Adhesion MoleculesCell AggregationColorectal NeoplasmsCytoskeletal ProteinsDCC ReceptorDesmogleinsDesmoplakinsGene Expression Regulation, NeoplasticGenes, DCCHumansNeuroblastomaReceptors, Cell SurfaceRecombinant ProteinsSequence DeletionTrans-ActivatorsTransfectionTumor Cells, CulturedTumor Suppressor ProteinsConceptsCalcium-dependent cell adhesionCell adhesionN-cadherinCell-cell contactCalcium-dependent aggregationCell aggregation studiesNorthern blot analysisNeuroblastoma cellsDCC proteinProtein functionNeural developmentFunctional linkColorectal cancer (DCC) proteinCellular migrationHuman neuroblastoma cell lineNeuroblastoma cell linesProteinBlot analysisCancer proteinsProtein levelsCell processesCell linesOverexpressionCatenin expressionDiminished expression
1999
Frequent mutation and nuclear localization of beta-catenin in anaplastic thyroid carcinoma.
Garcia-Rostan G, Tallini G, Herrero A, D'Aquila TG, Carcangiu ML, Rimm DL. Frequent mutation and nuclear localization of beta-catenin in anaplastic thyroid carcinoma. Cancer Research 1999, 59: 1811-5. PMID: 10213482.Peer-Reviewed Original ResearchConceptsNuclear localizationSingle-strand conformational polymorphismE-cadherin-mediated cell-cell adhesionBeta-catenin actsFrequent nuclear localizationCell-cell adhesionExon 3Conformational polymorphismBeta-catenin genePhosphorylation sitesWingless pathwayTranscriptional activationCytoplasmic proteinsSubcellular localizationMobility shiftMutational analysisNucleotide sequencingDNA sequencingNuclear translocationSomatic alterationsMutationsAnaplastic thyroid carcinomaSequencingProteinFrequent mutations
1998
The expression of p120ctn protein in breast cancer is independent of alpha- and beta-catenin and E-cadherin.
Dillon DA, D'Aquila T, Reynolds AB, Fearon ER, Rimm DL. The expression of p120ctn protein in breast cancer is independent of alpha- and beta-catenin and E-cadherin. American Journal Of Pathology 1998, 152: 75-82. PMID: 9422525, PMCID: PMC1858125.Peer-Reviewed Original Research
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
1994
Molecular Cloning Reveals Alternative Splice Forms of Human α(E)-Catenin
Rimm DL, Kebriaei P, Morrow JS. Molecular Cloning Reveals Alternative Splice Forms of Human α(E)-Catenin. Biochemical And Biophysical Research Communications 1994, 203: 1691-1699. PMID: 7945318, DOI: 10.1006/bbrc.1994.2381.Peer-Reviewed Original ResearchMeSH KeywordsAlpha CateninAlternative SplicingAmino Acid SequenceAnimalsBase SequenceCadherinsCell LineChickensCloning, MolecularConserved SequenceCytoskeletal ProteinsDNA, ComplementaryDrosophilaHominidaeHumansMiceMolecular Sequence DataPhylogenyPolymerase Chain ReactionRNA, MessengerSequence Homology, Amino AcidTranscription, GeneticConceptsCadherin cell-cell adhesion complexCell-cell adhesion complexAmino acid proteinAlternative splice formsSuperfamily of proteinsAmino acid insertionTranscription sitesAdhesion complexesCytoplasmic domainDistinct transcriptsMolecular cloningSingle geneAcid proteinSplice formsAcid insertionSecond transcriptCatenin geneSplice siteNon-epithelial tissuesVinculinTranscriptsCateninHuman alphaSouthern blottingProteinMolecular Cloning of Human E-Cadherin Suggests a Novel Subdivision of the Cadherin Superfamily
Rimm DL, Morrow JS. Molecular Cloning of Human E-Cadherin Suggests a Novel Subdivision of the Cadherin Superfamily. Biochemical And Biophysical Research Communications 1994, 200: 1754-1761. PMID: 8185635, DOI: 10.1006/bbrc.1994.1656.Peer-Reviewed Original ResearchConceptsHuman E-cadherinClassical cadherinsE-cadherinDown-stream signaling cascadesCadherin functionRelated cadherinsHomology domainCytoplasmic domainSequence motifsDomain homologyUnprocessed proteinMolecular cloningCytoplasmic interactionsHuman proteinsCDNA libraryDesmosomal cadherinsSignaling cascadesCadherinMolecular massT-cadherinNovel subdivisionProteinRET oncogeneCloningHomology
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 ResearchConceptsActin-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 chromatographyPolypeptideActinDNANew plasmid vectors for high level synthesis of eukaryotic fusion proteins in Escherichia coli
Rimm D, Pollard T. New plasmid vectors for high level synthesis of eukaryotic fusion proteins in Escherichia coli. Gene 1989, 75: 323-327. PMID: 2653968, DOI: 10.1016/0378-1119(89)90278-3.Peer-Reviewed Original ResearchConceptsFusion proteinBacterial proteinsPlasmid vectorEscherichia coliCloning sitePlasmid vector systemTotal soluble proteinEukaryotic fusion proteinsSoluble recombinant proteinInsertion of sequencesEukaryotic proteinsMultiple cloning sitePlasmid expression vectorTrpE proteinNew plasmid vectorRecombinant proteinsSoluble proteinExpression vectorTail sequencesAmino acidsProteinVector systemSequenceColiCell suspensionsStructure-Function Studies of the Actin Filament System of Acanthamoeba
Pollard T, Magnus K, Doberstein S, Goldschmidt-Clermont P, Kaiser D, Machesky L, Maciver S, Rimm D, Wachsstock D. Structure-Function Studies of the Actin Filament System of Acanthamoeba. Springer Series In Biophysics 1989, 3: 271-279. DOI: 10.1007/978-3-642-73925-5_50.Peer-Reviewed Original ResearchRegulatory proteinsActin polymerizationEssential protein componentsActin filament systemStructure-function studiesMajor functional classesMechanism of actionActin systemAccessory proteinsProtein componentsPrimary structureFilament systemCellular levelProteinCytoplasmic matrixOverall mechanismCellsMechanismFunctional classAssemblyAcanthamoeba
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