2016
Non-malignant respiratory epithelial cells preferentially proliferate from resected non-small cell lung cancer specimens cultured under conditionally reprogrammed conditions
Gao B, Huang C, Kernstine K, Pelekanou V, Kluger Y, Jiang T, Peters-Hall JR, Coquelin M, Girard L, Zhang W, Huffman K, Oliver D, Kinose F, Haura E, Teer JK, Rix U, Le AT, Aisner DL, Varella-Garcia M, Doebele RC, Covington KR, Hampton OA, Doddapaneni HV, Jayaseelan JC, Hu J, Wheeler DA, Shay JW, Rimm DL, Gazdar A, Minna JD. Non-malignant respiratory epithelial cells preferentially proliferate from resected non-small cell lung cancer specimens cultured under conditionally reprogrammed conditions. Oncotarget 2016, 5: 11114-11126. PMID: 28052041, PMCID: PMC5355251, DOI: 10.18632/oncotarget.14366.Peer-Reviewed Original ResearchMeSH KeywordsA549 CellsAdultAgedAged, 80 and overBase SequenceCarcinoma, Non-Small-Cell LungCell Line, TumorCell ProliferationCells, CulturedCoculture TechniquesDNA Copy Number VariationsDNA Mutational AnalysisEpithelial CellsFemaleGene Expression ProfilingGenetic Predisposition to DiseaseHumansLung NeoplasmsMaleMiddle AgedMutationRespiratory MucosaTumor Cells, CulturedConceptsNon-small cell lung cancerRespiratory epithelial cellsNon-malignant lungCell lung cancerCRC culturesLung cancerEpithelial cellsResected non-small cell lung cancerPrimary lung cancerNon-malignant samplesLung epithelial cellsRho-kinase inhibitorNon-malignant cellsPrimary NSCLCPrimary tumorDiploid patternOriginal tumorTumor specimensTumor tissueTumorsKinase inhibitorsCancerCancer cellsMRNA expression profilesSmall subpopulation
1995
Frequent alterations in E-cadherin and alpha- and beta-catenin expression in human breast cancer cell lines.
Pierceall W, Woodard A, Morrow J, Rimm D, Fearon E. Frequent alterations in E-cadherin and alpha- and beta-catenin expression in human breast cancer cell lines. Oncogene 1995, 11: 1319-26. PMID: 7478552.Peer-Reviewed Original ResearchMeSH KeywordsAlpha CateninBase SequenceBeta CateninBlotting, SouthernBlotting, WesternBreast NeoplasmsCadherinsCytoskeletal ProteinsFemaleGene DeletionGene ExpressionHumansMolecular Sequence DataMutationOligodeoxyribonucleotidesPolymerase Chain ReactionPolymorphism, Single-Stranded ConformationalReceptor, ErbB-2RibonucleasesTrans-ActivatorsTumor Cells, CulturedConceptsAlpha-catenin proteinE-cadherin transcriptE-cadherinE-cadherin expressionBeta-catenin expressionCell linesBreast cancer cell linesEpithelial cell-cell interactionsCancer cell linesBeta-catenin proteinCancer-derived cell linesMembrane cytoskeletal proteinsCell-cell interactionsBreast cancer-derived cell linesE-cadherin geneHuman breast cancer-derived cell linesLoss of functionTransmembrane proteinAdherens junctionsCytoskeletal matrixCadherin proteinCytoskeletal proteinsTranscript levelsFrequent alterationsSequence alterations
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
1991
Analysis of cDNA clones for Acanthamoeba profilin‐I and profilin‐II shows end to end homology with vertebrate profilins and a small family of profilin genes
Pollard T, Rimm D. Analysis of cDNA clones for Acanthamoeba profilin‐I and profilin‐II shows end to end homology with vertebrate profilins and a small family of profilin genes. Cytoskeleton 1991, 20: 169-177. PMID: 1751969, DOI: 10.1002/cm.970200209.Peer-Reviewed Original ResearchConceptsProfilin IIDNA sequencesProtein sequencesAcanthamoeba profilinGenomic DNA fragmentsFull-length cDNAFamily of proteinsProfilin geneAncestral precursorDifferent phylaInvariant residuesAdditional genesCDNA clonesLength cDNAConservative substitutionsPairwise identityDNA fragmentsSouthern blotNorthern blotGenesProfilinAmino acidsSmall familyCDNAConsiderable divergence
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
New 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: 2041-6. 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