2011
Standardization of Estrogen Receptor Measurement in Breast Cancer Suggests False-Negative Results Are a Function of Threshold Intensity Rather Than Percentage of Positive Cells
Welsh AW, Moeder CB, Kumar S, Gershkovich P, Alarid ET, Harigopal M, Haffty BG, Rimm DL. Standardization of Estrogen Receptor Measurement in Breast Cancer Suggests False-Negative Results Are a Function of Threshold Intensity Rather Than Percentage of Positive Cells. Journal Of Clinical Oncology 2011, 29: 2978-2984. PMID: 21709197, PMCID: PMC3157961, DOI: 10.1200/jco.2010.32.9706.Peer-Reviewed Original ResearchConceptsER-positive patientsEstrogen receptorQuantitative immunofluorescenceBreast cancerTissue microarrayPositive cellsIndependent retrospective cohortsEstrogen receptor measurementsAssessment of survivalTMA cohortFalse-negative resultsRetrospective cohortER immunoreactivityTest discordancePrognostic outcomesIndependent cohortReceptor measurementsLimitations of immunohistochemistryPatientsDiscrepant casesCohortIHC methodPathologists' judgmentsDiscrepant resultsStandardized assays
2009
Phosphatidylinositol-3-Kinase as a Therapeutic Target in Melanoma
Aziz SA, Davies M, Pick E, Zito C, Jilaveanu L, Camp RL, Rimm DL, Kluger Y, Kluger HM. Phosphatidylinositol-3-Kinase as a Therapeutic Target in Melanoma. Clinical Cancer Research 2009, 15: 3029-3036. PMID: 19383818, PMCID: PMC4431617, DOI: 10.1158/1078-0432.ccr-08-2768.Peer-Reviewed Original ResearchMeSH KeywordsBrain NeoplasmsCell ProliferationChromonesEnzyme InhibitorsHumansImmunoblottingImmunoenzyme TechniquesMelanomaMorpholinesNevus, PigmentedPhosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsPhosphorylationProtein Array AnalysisSkin NeoplasmsTissue Array AnalysisTumor Cells, CulturedConceptsPhosphatidylinositol-3 kinasePI3K inhibitorsExpression of p85PI3KP110alpha subunitPathway membersK inhibitorsCell linesPI3K pathway membersReverse phase protein arrayGood drug targetPhase protein arrayPI3K pathwayTargets of drugsCellular processesPhospho-Akt levelsPI3K inhibitionMelanoma cell linesDrug targetsFull activationP85K pathwayLY294002Protein arraysResistant cell lines
2007
Definition of a direct extracellular interaction between Met and E‐cadherin
Reshetnikova G, Troyanovsky S, Rimm DL. Definition of a direct extracellular interaction between Met and E‐cadherin. Cell Biology International 2007, 31: 366-373. PMID: 17336101, DOI: 10.1016/j.cellbi.2007.01.022.Peer-Reviewed Original ResearchConceptsBT-549 cellsE-cadherinCadherin-dependent cell-cell contactsHT-29 cellsE-cadherin interactsHepatocyte growth factorCell-cell adhesionCell-cell contactCross-linking studiesDirect extracellular interactionTyrosine kinase receptor expressionExtracellular interactionsMolecular mechanismsExtracellular domainIntracellular compartmentsPhysical interactionCellular presentationFirst evidenceGrowth factorCellsBT-549HT-29ExpressionReceptor expressionMetS
1998
Dynamic Interaction of PTPμ with Multiple Cadherins In Vivo
Brady-Kalnay S, Mourton T, Nixon J, Pietz G, Kinch M, Chen H, Brackenbury R, Rimm D, Del Vecchio R, Tonks N. Dynamic Interaction of PTPμ with Multiple Cadherins In Vivo. Journal Of Cell Biology 1998, 141: 287-296. PMID: 9531566, PMCID: PMC2132733, DOI: 10.1083/jcb.141.1.287.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, MonoclonalCadherinsCell LineCell Line, TransformedCerebellumCross ReactionsElectrophoresis, Polyacrylamide GelHumansImmunoblottingMiceProtein Tyrosine PhosphatasesRatsReceptor-Like Protein Tyrosine Phosphatases, Class 2Receptor-Like Protein Tyrosine Phosphatases, Class 8Recombinant Fusion ProteinsRecombinant ProteinsSpodopteraTransfectionConceptsReversible tyrosine phosphorylationCadherin-catenin complexTyrosine phosphorylationE-cadherinWC5 cellsTemperature-sensitive mutant formPresence of cadherinCadherin functionV-SrcCytoplasmic segmentMultiple cadherinsCadherin-4PTPmuSf9 cellsMutant formsRegulatory mechanismsAdhesive functionCadherinN-cadherinPhosphorylationDirect interaction
1995
Receptor protein tyrosine phosphatase PTPmu associates with cadherins and catenins in vivo.
Brady-Kalnay SM, Rimm DL, Tonks NK. Receptor protein tyrosine phosphatase PTPmu associates with cadherins and catenins in vivo. Journal Of Cell Biology 1995, 130: 977-986. PMID: 7642713, PMCID: PMC2199947, DOI: 10.1083/jcb.130.4.977.Peer-Reviewed Original ResearchMeSH KeywordsAlpha CateninAnimalsBeta CateninBinding SitesBrainCadherinsCell LineCytoskeletal ProteinsImmunoblottingImmunohistochemistryIntercellular JunctionsLungMembrane ProteinsMinkMyocardiumPhosphorylationPrecipitin TestsProtein BindingProtein Tyrosine PhosphatasesRatsReceptor-Like Protein Tyrosine Phosphatases, Class 2Receptor-Like Protein Tyrosine Phosphatases, Class 8Receptors, Cell SurfaceTissue DistributionTrans-ActivatorsVanadatesConceptsIntracellular segmentIntracellular domainCellular tyrosine phosphatase activityCadherin/catenin complexDynamic tyrosine phosphorylationImmunoglobulin domainFibronectin type III repeatsTyrosine phosphatase activityTyrosine-phosphorylated formType III repeatsCell-cell contactJuxtamembrane segmentPTP domainPervanadate treatmentMAM domainActin cytoskeletonCatenin complexPTPmuTyrosine phosphorylationExtracellular segmentCadherinEndogenous substratesMink lung cellsPhosphatase activityCateninAutoantibodies specific for villin found in patients with colon cancer and other colitides
Rimm D, Holland T, Morrow J, Anderson J. Autoantibodies specific for villin found in patients with colon cancer and other colitides. Digestive Diseases And Sciences 1995, 40: 389-395. PMID: 7851204, DOI: 10.1007/bf02065426.Peer-Reviewed Original ResearchConceptsColon cancerActive autoimmune responseSpecific gastrointestinal diseasesLevels of autoantibodiesColon cancer patients´ seraCancer patient seraIntestinal epithelial cellsCryptic antigensAutoimmune responseGastrointestinal pathologyColonic diseaseGastrointestinal diseasesPatient seraNormal controlsPathological significanceWestern blotDisease statesEpithelial cellsNoninvasive approachUnique noninvasive approachAntibodiesAutoantibodiesBrush borderPatientsCancer
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 Research