1998
A Mutation in α-Catenin Disrupts Adhesion in Clone A Cells Without Perturbing its Actin and β-Catenin Binding Activity
Roe S, Koslov E, Rimm D. A Mutation in α-Catenin Disrupts Adhesion in Clone A Cells Without Perturbing its Actin and β-Catenin Binding Activity. Cell Communication & Adhesion 1998, 5: 283-296. PMID: 9762469, DOI: 10.3109/15419069809040298.Peer-Reviewed Original ResearchMeSH KeywordsActinsAlpha CateninBeta CateninCadherinsCell AdhesionCloning, MolecularColonic NeoplasmsCytoskeletal ProteinsCytoskeletonDesmoplakinsExonsGamma CateninHeLa CellsHumansIntercellular JunctionsMutationOctoxynolPrecipitin TestsProtein BindingRecombinant Fusion ProteinsReverse Transcriptase Polymerase Chain ReactionRNA, MessengerSequence Analysis, DNASolubilityTrans-ActivatorsTransfectionTumor Cells, CulturedConceptsN-terminusE-cadherin-catenin complexBundles F-actinCo-sedimentation assaysCell-cell adhesionFull-length proteinClone A cellsCo-precipitation experimentsInternal deletion mutationsWhole cell lysatesAdhesive complexesMutant proteinsA mutantsMutant bindsHuman colon carcinoma cell lineColon carcinoma cell lineMutant formsLength proteinWild typeCytoplasmic connectionsF-actinAdhesive phenotypeDeletion mutationsCell lysatesCarcinoma cell lines
1997
Transcriptional defects underlie loss of E-cadherin expression in breast cancer.
Ji X, Woodard AS, Rimm DL, Fearon ER. Transcriptional defects underlie loss of E-cadherin expression in breast cancer. Molecular Cancer Research 1997, 8: 773-8. PMID: 9218871.Peer-Reviewed Original ResearchMeSH KeywordsAntimetabolites, AntineoplasticAzacitidineBreast NeoplasmsCadherinsCloning, MolecularDecitabineDNA MethylationDNA-Binding ProteinsGene Expression Regulation, NeoplasticHumansPromoter Regions, GeneticTrans-ActivatorsTranscription Factor AP-2Transcription FactorsTranscription, GeneticTumor Cells, CulturedConceptsE-cad expressionBreast cancerEpithelial cancersHuman breast cancer cell linesMost breast cancersDifferent epithelial cancersBreast cancer cell linesMajority of cancersE-cadherin expressionCancer cell linesCell adhesion moleculeProgression eventsCancerAdhesion moleculesTumor heterogeneityE-cadherinFunctional assaysCell linesSomatic mutationsE-cad geneGene expression differencesExpressionPromoter activityGene expressionReporter gene constructs
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. 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 ResearchConceptsMyosin IIHeptad repeatAcanthamoeba myosin IIHead-tail junctionCoiled-coil structureHydrophobic amino acidsNative myosin IIIdentical polypeptidesNH2 terminusMyosin-II tailNonmuscle myosinProteolytic separationLines of evidenceShort tailAmino acidsPosition 847RepeatsMyosinResiduesTailMyosin moleculesHeptadTerminusMonoclonal antibodiesPolypeptideNew 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 suspensions
1984
Structural analysis of the murine IgG3 constant region gene.
Wels J, Word C, Rimm D, Der-Balan G, Martinez H, Tucker P, Blattner F. Structural analysis of the murine IgG3 constant region gene. The EMBO Journal 1984, 3: 2041-2046. PMID: 6092053, PMCID: PMC557641, DOI: 10.1002/j.1460-2075.1984.tb02089.x.Peer-Reviewed Original ResearchConceptsConstant region genesMembrane exonsMRNA precursorsHeavy chain constant region genesAmino acid sequenceRegion genesSwitch recombination regionC gamma 3 geneGamma 3 chainCarbohydrate addition sitesProtein domainsC deltaCarboxyl terminusComplete sequenceAcid sequenceRemarkable homologyGamma 3 geneAddition siteSwitch sitesSecondary structureMembrane formClass switch mechanismExonsGenesC mu