2021
Targeting Pyruvate Kinase M2 Phosphorylation Reverses Aggressive Cancer Phenotypes
Apostolidi M, Vathiotis IA, Muthusamy V, Gaule P, Gassaway BM, Rimm DL, Rinehart J. Targeting Pyruvate Kinase M2 Phosphorylation Reverses Aggressive Cancer Phenotypes. Cancer Research 2021, 81: 4346-4359. PMID: 34185676, PMCID: PMC8373815, DOI: 10.1158/0008-5472.can-20-4190.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAnimalsBiomarkers, TumorCarrier ProteinsCell Line, TumorCollagenCyclic N-OxidesDrug CombinationsGenome, HumanHumansIndolizinesLamininMCF-7 CellsMembrane ProteinsMiceNeoplasm InvasivenessNeoplasm TransplantationNeoplasmsOxidation-ReductionPhenotypePhosphorylationProtein IsoformsProteoglycansProteomicsPyridazinesPyridinium CompoundsPyrrolesPyruvate KinaseThyroid HormonesTriple Negative Breast NeoplasmsConceptsTriple-negative breast cancerPyruvate kinase M2TEPP-46Breast cancerAggressive breast cancer cell phenotypesCharacteristic nuclear staining patternAggressive breast cancer subtypeAggressive breast cancer phenotypeBreast cancer cell phenotypeCDK inhibitor dinaciclibCombination of dinaciclibLack of biomarkersEffective therapeutic approachBreast cancer phenotypeBreast cancer subtypesCancer phenotypePhosphorylation of PKM2Cyclin-dependent kinase (CDK) pathwayMouse xenograft modelAggressive cancer phenotypeNuclear staining patternLower survival rateImpaired redox balancePrognostic valueCancer cell phenotype
2014
Identification of proteomic biomarkers predicting prostate cancer aggressiveness and lethality despite biopsy-sampling error
Shipitsin M, Small C, Choudhury S, Giladi E, Friedlander S, Nardone J, Hussain S, Hurley AD, Ernst C, Huang YE, Chang H, Nifong TP, Rimm DL, Dunyak J, Loda M, Berman DM, Blume-Jensen P. Identification of proteomic biomarkers predicting prostate cancer aggressiveness and lethality despite biopsy-sampling error. British Journal Of Cancer 2014, 111: 1201-1212. PMID: 25032733, PMCID: PMC4453845, DOI: 10.1038/bjc.2014.396.Peer-Reviewed Original ResearchMeSH KeywordsActininAgedAlkyl and Aryl TransferasesArea Under CurveBiomarkers, TumorBiopsy, Fine-NeedleCullin ProteinsDNA-Binding ProteinsFollow-Up StudiesHSP70 Heat-Shock ProteinsHumansImage Processing, Computer-AssistedMaleMembrane ProteinsMiddle AgedMitochondrial ProteinsNeoplasm GradingNeoplasm StagingPhosphorylationProstateProstatic NeoplasmsProteomicsRibosomal Protein S6RNA-Binding Protein FUSROC CurveSelection BiasSmad2 ProteinSmad4 ProteinTissue Array AnalysisVoltage-Dependent Anion Channel 1Y-Box-Binding Protein 1ConceptsProstate cancer aggressivenessCancer aggressivenessLarge patient cohortLow Gleason gradePatient cohortTumor microarrayLethal outcomeProstatectomy samplesGleason gradeSignificant overtreatmentBiopsy interpretationProstatectomy tissuePatient samplesBiopsy testsProteomic biomarkersCancer biomarker discoveryExpert pathologistsMarker signaturesTumor heterogeneityBiomarkersAggressivenessProtein biomarkersBiomarker discoveryQuantitative proteomics approachQuantitative measurements of HER2 and phospho-HER2 expression: correlation with pathologic response to neoadjuvant chemotherapy and trastuzumab
Cheng H, Bai Y, Sikov W, Sinclair N, Bossuyt V, Abu-Khalaf MM, Harris LN, Rimm DL. Quantitative measurements of HER2 and phospho-HER2 expression: correlation with pathologic response to neoadjuvant chemotherapy and trastuzumab. BMC Cancer 2014, 14: 326. PMID: 24885187, PMCID: PMC4037428, DOI: 10.1186/1471-2407-14-326.Peer-Reviewed Original ResearchMeSH KeywordsAdenocarcinomaAlbuminsAntibodies, Monoclonal, HumanizedAntineoplastic Combined Chemotherapy ProtocolsBiomarkers, TumorBreast NeoplasmsCarboplatinChemotherapy, AdjuvantConnecticutFemaleFluorescent Antibody TechniqueHumansNeoadjuvant TherapyPaclitaxelPhosphorylationProteomicsReceptor, ErbB-2Rhode IslandTime FactorsTrastuzumabTreatment OutcomeConceptsLikelihood of responsePhospho-HER2Nab-paclitaxelPathologic responseHER2 levelsAdvanced HER2-positive breast cancerHER2-positive breast cancerCarboplatin combination therapyPreoperative clinical trialPre-surgical settingSingle-agent trastuzumabPathologic complete responseInitiation of treatmentWeeks of treatmentBreast cancer patientsTumor core biopsiesCore biopsy samplesMonoclonal antibody trastuzumabEvaluable patientsNeoadjuvant regimenNeoadjuvant chemotherapyNeoadjuvant therapyNeoadjuvant treatmentComplete responsePreoperative setting
2013
Comparison of HER2 and Phospho-HER2 Expression between Biopsy and Resected Breast Cancer Specimens Using a Quantitative Assessment Method
Bai Y, Cheng H, Bordeaux J, Neumeister V, Kumar S, Rimm DL, Stern DF. Comparison of HER2 and Phospho-HER2 Expression between Biopsy and Resected Breast Cancer Specimens Using a Quantitative Assessment Method. PLOS ONE 2013, 8: e79901. PMID: 24278211, PMCID: PMC3836903, DOI: 10.1371/journal.pone.0079901.Peer-Reviewed Original ResearchConceptsCore needle biopsyBreast cancer casesResection specimensCancer casesHER2/neu overexpressionPrediction of responsePre-analytic variablesNeu overexpressionTumor resectionNeedle biopsyBreast cancerHER2 immunoreactivityRetrospective collectionHER2Drug trastuzumabClinical implicationsHER2 proteinQuantitative immunofluorescenceResectionPHER2Good responseFurther studiesBiopsyTrastuzumabImmunoreactivityPin1 modulates ERα levels in breast cancer through inhibition of phosphorylation-dependent ubiquitination and degradation
Rajbhandari P, Schalper KA, Solodin NM, Ellison-Zelski SJ, Ping Lu K, Rimm DL, Alarid ET. Pin1 modulates ERα levels in breast cancer through inhibition of phosphorylation-dependent ubiquitination and degradation. Oncogene 2013, 33: 1438-1447. PMID: 23542176, PMCID: PMC3815749, DOI: 10.1038/onc.2013.78.Peer-Reviewed Original ResearchConceptsERα protein levelsERα proteinBreast cancerERα-positive breast cancerProtein levelsPotential surrogate markerRetrospective cohortSurrogate markerBreast carcinomaTherapy decisionsERα levelsESR1 levelsERα ubiquitinationCertain tumorsHuman tumorsDiscordant levelsESR1Pin1 levelsReceptor interactionUbiquitin-proteasome pathwayReceptor degradationImportant biomarkerTumorsCancerTransactivation functionMolecular profile of head and neck squamous cell carcinomas bearing p16 high phenotype
Rampias T, Pectasides E, Prasad M, Sasaki C, Gouveris P, Dimou A, Kountourakis P, Perisanidis C, Burtness B, Zaramboukas T, Rimm D, Fountzilas G, Psyrri A. Molecular profile of head and neck squamous cell carcinomas bearing p16 high phenotype. Annals Of Oncology 2013, 24: 2124-2131. PMID: 23406730, DOI: 10.1093/annonc/mdt013.Peer-Reviewed Original ResearchMeSH KeywordsBeta CateninBiomarkers, TumorCarcinoma, Squamous CellCell Line, TumorCyclin-Dependent Kinase Inhibitor p16ErbB ReceptorsFemaleHead and Neck NeoplasmsHumansMaleNeoplasm ProteinsOncogene Proteins, ViralOropharyngeal NeoplasmsPapillomavirus E7 ProteinsPapillomavirus InfectionsPhosphorylationPTEN PhosphohydrolaseRepressor ProteinsRNA InterferenceRNA, Small InterferingSquamous Cell Carcinoma of Head and NeckTumor Suppressor Protein p53Wnt Signaling PathwayConceptsE6/E7Β-cateninHNSCC cellsTissue microarrayE6/E7 repressionEpidermal growth factor receptor (EGFR) pathwayNeck squamous cell cancerE6/E7 genesOropharyngeal cancer cellsNeck squamous cell carcinomaShort hairpin RNAGrowth factor receptor pathwayHPV16 E6/E7Squamous cell cancerSquamous cell carcinomaExpression of biomarkersExpression differencesPTEN upregulationAberrant EGFRE7 repressionHairpin RNAMedian OSOverall survivalPhosphorylated EGFRCell cancer
2012
Low levels of Stat5a protein in breast cancer are associated with tumor progression and unfavorable clinical outcomes
Peck AR, Witkiewicz AK, Liu C, Klimowicz AC, Stringer GA, Pequignot E, Freydin B, Yang N, Ertel A, Tran TH, Girondo MA, Rosenberg AL, Hooke JA, Kovatich AJ, Shriver CD, Rimm DL, Magliocco AM, Hyslop T, Rui H. Low levels of Stat5a protein in breast cancer are associated with tumor progression and unfavorable clinical outcomes. Breast Cancer Research 2012, 14: r130. PMID: 23036105, PMCID: PMC4053108, DOI: 10.1186/bcr3328.Peer-Reviewed Original ResearchConceptsPoor prognosisBreast cancerClinical outcomesIndependent markerNode-negative breast cancer patientsNode-negative breast cancerLower tumor levelsPrimary breast cancerUnfavorable clinical outcomeBreast cancer patientsClinical outcome dataProtein levelsRandomized clinical trialsPredictors of responseNew independent markerBreast cancer progressionTherapy-naïveFourfold riskCancer patientsTherapy failureTumor levelsArchival cohortUnfavorable outcomeClinical trialsStat5a/b
2011
β-Catenin Signaling Controls Metastasis in Braf-Activated Pten-Deficient Melanomas
Damsky WE, Curley DP, Santhanakrishnan M, Rosenbaum LE, Platt JT, Rothberg BE, Taketo MM, Dankort D, Rimm DL, McMahon M, Bosenberg M. β-Catenin Signaling Controls Metastasis in Braf-Activated Pten-Deficient Melanomas. Cancer Cell 2011, 20: 741-754. PMID: 22172720, PMCID: PMC3241928, DOI: 10.1016/j.ccr.2011.10.030.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, DifferentiationBenzamidesBeta CateninCell Transformation, NeoplasticColorectal NeoplasmsEnzyme ActivationGene Knockdown TechniquesHumansImatinib MesylateKaplan-Meier EstimateLung NeoplasmsLymphatic MetastasisMelanocytesMelanoma, ExperimentalMiceMice, 129 StrainMice, Inbred C57BLMice, TransgenicPhosphorylationPiperazinesProtein StabilityProto-Oncogene Proteins B-rafProto-Oncogene Proteins c-aktPTEN PhosphohydrolasePyrimidinesSignal TransductionSkin NeoplasmsSplenic NeoplasmsTranscription, GeneticTumor Cells, CulturedConceptsΒ-catenin levelsPI3K/AktLymph nodesMetastatic tumorsFrequent metastasisTumor differentiationMalignant melanomaMAPK/ERKMelanoma metastasesMouse modelControl metastasisHuman melanomaMelanomaMetastasisΒ-catenin stabilizationPTEN lossCentral mediatorMetastasis regulatorsΒ-cateninSpecific changesFunctional implicationsWntLungProinvasion Metastasis Drivers in Early-Stage Melanoma Are Oncogenes
Scott KL, Nogueira C, Heffernan TP, van Doorn R, Dhakal S, Hanna JA, Min C, Jaskelioff M, Xiao Y, Wu CJ, Cameron LA, Perry SR, Zeid R, Feinberg T, Kim M, Woude G, Granter SR, Bosenberg M, Chu GC, DePinho RA, Rimm DL, Chin L. Proinvasion Metastasis Drivers in Early-Stage Melanoma Are Oncogenes. Cancer Cell 2011, 20: 92-103. PMID: 21741599, PMCID: PMC3176328, DOI: 10.1016/j.ccr.2011.05.025.Peer-Reviewed Original ResearchMeSH KeywordsAcid PhosphataseAnimalsCell LineageConserved SequenceEvolution, MolecularGene Expression ProfilingGene Expression Regulation, NeoplasticGenomeHumansIsoenzymesKaplan-Meier EstimateMelanomaMiceNeoplasm InvasivenessNeoplasm MetastasisNeoplasm StagingOncogenesPhosphorylationReproducibility of ResultsSkin NeoplasmsTartrate-Resistant Acid PhosphataseTissue Array AnalysisConceptsFunctional genetic screensGenetic screenGlobal transcriptomeMetastatic potentialSuch genesGenomic evidenceExpression selectionTranscriptomic profilesHuman melanoma tissuesMetastasis driverCell invasionKey pathwaysOncogenic capabilitiesMelanoma tissuesGenesHuman melanomaHuman primary melanomasTranscriptomeMouse modelSpontaneous metastasisOncogeneEnhancerACP5PathwayInvasionLoss of Nuclear Localized and Tyrosine Phosphorylated Stat5 in Breast Cancer Predicts Poor Clinical Outcome and Increased Risk of Antiestrogen Therapy Failure
Peck AR, Witkiewicz AK, Liu C, Stringer GA, Klimowicz AC, Pequignot E, Freydin B, Tran TH, Yang N, Rosenberg AL, Hooke JA, Kovatich AJ, Nevalainen MT, Shriver CD, Hyslop T, Sauter G, Rimm DL, Magliocco AM, Rui H. Loss of Nuclear Localized and Tyrosine Phosphorylated Stat5 in Breast Cancer Predicts Poor Clinical Outcome and Increased Risk of Antiestrogen Therapy Failure. Journal Of Clinical Oncology 2011, 29: 2448-2458. PMID: 21576635, PMCID: PMC3675698, DOI: 10.1200/jco.2010.30.3552.Peer-Reviewed Original ResearchMeSH KeywordsAdultAgedAged, 80 and overAntineoplastic Agents, HormonalBreast NeoplasmsCarcinoma, Ductal, BreastCarcinoma, Intraductal, NoninfiltratingCohort StudiesDisease ProgressionDisease-Free SurvivalDrug Resistance, NeoplasmEstrogen Receptor ModulatorsFemaleHumansLymphatic MetastasisMiddle AgedNeoplasm ProteinsNuclear ProteinsPhosphorylationPhosphotyrosinePrognosisProtein Processing, Post-TranslationalSTAT5 Transcription FactorSurvival AnalysisTreatment FailureTumor Suppressor ProteinsYoung AdultConceptsNode-negative breast cancerCancer-specific survivalIndependent prognostic markerBreast cancerWhole tissue sectionsTherapy failurePrognostic markerTissue microarrayPathologist scoringMultivariate analysis patientsSystemic adjuvant therapyAdjuvant hormone therapyMarker of prognosisPoor clinical outcomeUseful predictive markerPredictors of responseNormal breast epitheliumTissue sectionsCohort IVAdjuvant therapyHormone therapyAnalysis patientsClinical outcomesDuctal carcinomaProspective study
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 linesAnalysis of Drosophila Segmentation Network Identifies a JNK Pathway Factor Overexpressed in Kidney Cancer
Liu J, Ghanim M, Xue L, Brown CD, Iossifov I, Angeletti C, Hua S, Nègre N, Ludwig M, Stricker T, Al-Ahmadie HA, Tretiakova M, Camp RL, Perera-Alberto M, Rimm DL, Xu T, Rzhetsky A, White KP. Analysis of Drosophila Segmentation Network Identifies a JNK Pathway Factor Overexpressed in Kidney Cancer. Science 2009, 323: 1218-1222. PMID: 19164706, PMCID: PMC2756524, DOI: 10.1126/science.1157669.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsApoptosisCarcinoma, Renal CellCell LineCompound Eye, ArthropodDrosophila melanogasterDrosophila ProteinsEmbryo, NonmammalianFushi Tarazu Transcription FactorsGene Expression ProfilingGene Regulatory NetworksHomeodomain ProteinsHumansJanus KinasesKidneyKidney NeoplasmsMolecular Sequence DataNervous SystemNuclear ProteinsPhosphoprotein PhosphatasesPhosphorylationRepressor ProteinsSignal TransductionTranscription FactorsTranscription, GeneticConceptsTranscription factorsClear cell renal cell carcinomaCell renal cell carcinomaKey transcription factorDrosophila segmentation networkConserved roleEmbryonic segmentationDrosophila melanogasterUbiquitin E3JNK signalingDependent apoptosisSPOPRenal cell carcinomaSPOP expressionKidney cancerTumor necrosis factorNew roleDrosophilaMelanogasterPuckeredGenesSignalingOverexpressedIdentificationApoptosis
2007
Phosphorylation of Akt (Ser473) Predicts Poor Clinical Outcome in Oropharyngeal Squamous Cell Cancer
Yu Z, Weinberger PM, Sasaki C, Egleston BL, Speier WF, Haffty B, Kowalski D, Camp R, Rimm D, Vairaktaris E, Burtness B, Psyrri A. Phosphorylation of Akt (Ser473) Predicts Poor Clinical Outcome in Oropharyngeal Squamous Cell Cancer. Cancer Epidemiology Biomarkers & Prevention 2007, 16: 553-558. PMID: 17372251, DOI: 10.1158/1055-9965.epi-06-0121.Peer-Reviewed Original ResearchMeSH KeywordsAdultAgedBiomarkers, TumorCarcinoma, Squamous CellChi-Square DistributionFemaleHumansImmunoenzyme TechniquesMaleMiddle AgedNeoplasm Recurrence, LocalOropharyngeal NeoplasmsPhosphorylationPredictive Value of TestsPrognosisProportional Hazards ModelsProtein Array AnalysisProto-Oncogene Proteins c-aktPTEN PhosphohydrolaseSurvival AnalysisConceptsNuclear p-AktAkt activationP-AktOropharyngeal squamous cell cancerSquamous cell carcinoma progressionPhosphorylated AktCohort of patientsLocal recurrence rateOverall survival rateSquamous cell cancerPoor clinical outcomeAdverse patient outcomesP-AKT levelsPromising molecular targetP-AKT expressionProtein expression levelsPhosphorylation of AktDisease recurrenceLocal recurrenceCell cancerClinical outcomesAdjusted analysisPrognostic significanceRecurrence ratePatient outcomes
2004
Functional correlates of mutation of the Asp32 and Gly34 residues of beta-catenin
Provost E, McCabe A, Stern J, Lizardi I, D'Aquila TG, Rimm DL. Functional correlates of mutation of the Asp32 and Gly34 residues of beta-catenin. Oncogene 2004, 24: 2667-2676. PMID: 15829978, DOI: 10.1038/sj.onc.1208346.Peer-Reviewed Original ResearchConceptsThreonine residuesΒ-cateninStable MDCK cell linesCell linesCadherin-mediated adhesionMutant β-cateninMutant cell linesExon 3Stable cell linesDestruction motifKinase substrateTranscriptional activationUbiquitination statusMultifunctional proteinMDCK cell lineCellular transformationTarget genesKey serineFunctional implicationsTransforming propertiesMutationsResiduesMotifG34Ubiquitination
2003
Functional Correlates of Mutations in β-Catenin Exon 3 Phosphorylation Sites*
Provost E, Yamamoto Y, Lizardi I, Stern J, D'Aquila TG, Gaynor RB, Rimm DL. Functional Correlates of Mutations in β-Catenin Exon 3 Phosphorylation Sites*. Journal Of Biological Chemistry 2003, 278: 31781-31789. PMID: 12799363, DOI: 10.1074/jbc.m304953200.Peer-Reviewed Original ResearchConceptsCasein kinase 1Mutation of serineGlycogen synthase kinase 3 betaSynthase kinase 3 betaMadin-Darby canine kidney cellsTarget genes cyclin D1Canine kidney cellsGene cyclin D1Threonine residuesPhosphorylation sitesDownstream genesStable transformationKinase activityWounding assayKinase 1Ser45Functional assaysThr41Functional differencesMutationsSoft agarExon 3Kidney cellsCyclin D1Ser33Tissue microarray analysis of signal transducers and activators of transcription 3 (Stat3) and phospho-Stat3 (Tyr705) in node-negative breast cancer shows nuclear localization is associated with a better prognosis.
Dolled-Filhart M, Camp RL, Kowalski DP, Smith BL, Rimm DL. Tissue microarray analysis of signal transducers and activators of transcription 3 (Stat3) and phospho-Stat3 (Tyr705) in node-negative breast cancer shows nuclear localization is associated with a better prognosis. Clinical Cancer Research 2003, 9: 594-600. PMID: 12576423.Peer-Reviewed Original ResearchMeSH KeywordsAcute-Phase ProteinsBiomarkersBreast NeoplasmsCell NucleusDNA-Binding ProteinsFemaleHumansImmunohistochemistryLymphatic MetastasisMultivariate AnalysisPhosphorylationPhosphotyrosinePrognosisProportional Hazards ModelsSTAT3 Transcription FactorSurvival AnalysisTime FactorsTrans-ActivatorsConceptsNode-negative breast cancerBreast cancerCytoplasmic expressionNuclear expressionOverall survivalReceptor stainingPrognostic markerPhospho-STAT3Breast cancer tissue microarrayEstrogen receptor stainingProgesterone receptor stainingNode-negative tumorsLarge retrospective studyIndependent prognostic markerBreast cancer specimensTissue microarray analysisCancer tissue microarrayShort-term survivalTranscription 3Breast cancer tumorsHER2 stainingBetter prognosisRetrospective studyRole of STAT3Signal transducer
2002
Alterations of Smad signaling in human breast carcinoma are associated with poor outcome: a tissue microarray study.
Xie W, Mertens JC, Reiss DJ, Rimm DL, Camp RL, Haffty BG, Reiss M. Alterations of Smad signaling in human breast carcinoma are associated with poor outcome: a tissue microarray study. Cancer Research 2002, 62: 497-505. PMID: 11809701.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBreast NeoplasmsCell DivisionCell LineDNA-Binding ProteinsFemaleGenes, BRCA1Genes, BRCA2Germ-Line MutationHeterozygoteHumansImmunohistochemistryKeratinocytesMammary Glands, AnimalMiceMice, Inbred BALB CPhosphorylationPregnancyPrognosisSignal TransductionSmad2 ProteinSmad3 ProteinSmad4 ProteinTrans-ActivatorsTransforming Growth Factor betaTumor Cells, CulturedConceptsHuman breast cancer cell linesBreast cancer cell linesHuman breast carcinomaBreast cancerCancer cell linesBreast carcinomaCell linesStage II breast cancerAxillary lymph node metastasisHuman breast cancer developmentHER2/neu expressionSmad signalingParticular histological subtypeProgesterone receptor expressionLymph node metastasisShorter overall survivalTGF-beta type II receptorTissue microarray studyBreast carcinoma specimensBreast cancer developmentTransgenic mouse modelHuman breast cancerHereditary breast cancerTGF-beta receptor signalingGrowth factor-beta signaling
1999
Controversies at the cytoplasmic face of the cadherin-based adhesion complex
Provost E, Rimm D. Controversies at the cytoplasmic face of the cadherin-based adhesion complex. Current Opinion In Cell Biology 1999, 11: 567-572. PMID: 10508647, DOI: 10.1016/s0955-0674(99)00015-0.Peer-Reviewed Original ResearchMeSH KeywordsAlpha CateninAnimalsArmadillo Domain ProteinsBeta CateninCadherinsCalciumCateninsCell AdhesionCell Adhesion MoleculesCytoplasmCytoskeletal ProteinsDelta CateninDimerizationDrosophila ProteinsHumansInsect ProteinsMacromolecular SubstancesMultigene FamilyPhosphoproteinsPhosphorylationProtein BindingProtein Processing, Post-TranslationalProtein Structure, TertiarySpectrinTrans-ActivatorsVinculinPECAM-1 (CD31) functions as a reservoir for and a modulator of tyrosine-phosphorylated β-catenin
Ilan N, Mahooti S, Rimm D, Madri J. PECAM-1 (CD31) functions as a reservoir for and a modulator of tyrosine-phosphorylated β-catenin. Journal Of Cell Science 1999, 112: 3005-3014. PMID: 10462517, DOI: 10.1242/jcs.112.18.3005.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBeta CateninCattleCells, CulturedCytoskeletal ProteinsEndothelial Growth FactorsEndothelium, VascularGene ExpressionHumansIn Vitro TechniquesLymphokinesModels, BiologicalNeovascularization, PhysiologicPhosphorylationPlatelet Endothelial Cell Adhesion Molecule-1Protein-Tyrosine KinasesTrans-ActivatorsTransfectionTyrosineVascular Endothelial Growth Factor AVascular Endothelial Growth FactorsConceptsTyrosine phosphorylationBeta-catenin tyrosine phosphorylationBeta-catenin nuclear translocationAdherens junction formationProtein tyrosine kinasesPECAM-1 functionsTyrosine phosphorylation levelsCell-cell contactSW480 colon carcinoma cellsEndothelial cell-cell contactsCatenin functionVascular endothelial growth factorCell adhesion moleculeTranscriptional factorsPECAM-1Colon carcinoma cellsTyrosine kinaseGamma cateninMajor substrateJunctional proteinsCytoplasmic levelsPhosphorylation levelsNuclear translocationΒ-cateninCateninFrequent 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