2016
GNA14 Somatic Mutation Causes Congenital and Sporadic Vascular Tumors by MAPK Activation
Lim YH, Bacchiocchi A, Qiu J, Straub R, Bruckner A, Bercovitch L, Narayan D, Genomics Y, McNiff J, Ko C, Robinson-Bostom L, Antaya R, Halaban R, Choate KA. GNA14 Somatic Mutation Causes Congenital and Sporadic Vascular Tumors by MAPK Activation. American Journal Of Human Genetics 2016, 99: 443-450. PMID: 27476652, PMCID: PMC4974082, DOI: 10.1016/j.ajhg.2016.06.010.Peer-Reviewed Original ResearchMeSH KeywordsCells, CulturedChild, PreschoolEnzyme ActivationGTP-Binding Protein alpha SubunitsGTP-Binding Protein alpha Subunits, Gq-G11Human Umbilical Vein Endothelial CellsHumansInfantInfant, NewbornIntercellular Signaling Peptides and ProteinsMaleMAP Kinase Signaling SystemMelanocytesMitogen-Activated Protein KinasesMutationProto-Oncogene Proteins c-aktVascular NeoplasmsConceptsLobular capillary hemangiomaVascular tumorsKaposiform hemangioendotheliomaMonths of lifeYears of ageSomatic activating mutationsGNA14 mutationsHuman endothelial cellsPharmacologic interventionsSignificant complicationsCommon neoplasmCapillary hemangiomaInfantile hemangiomasLCH lesionsPrimary human endothelial cellsTherapeutic interventionsActivating mutationsGNA11 mutationsTumorsEndothelial cellsLesionsPotential targetHemangiomaGNA14Somatic mutations
2011
Phosphoproteomic Screen Identifies Potential Therapeutic Targets in Melanoma
Tworkoski K, Singhal G, Szpakowski S, Zito CI, Bacchiocchi A, Muthusamy V, Bosenberg M, Krauthammer M, Halaban R, Stern DF. Phosphoproteomic Screen Identifies Potential Therapeutic Targets in Melanoma. Molecular Cancer Research 2011, 9: 801-812. PMID: 21521745, PMCID: PMC3117976, DOI: 10.1158/1541-7786.mcr-10-0512.Peer-Reviewed Original ResearchMeSH KeywordsApoptosisCell Line, TumorCell MovementCell ProliferationErbB ReceptorsGene Expression Regulation, NeoplasticGene Knockdown TechniquesHEK293 CellsHumansInfant, NewbornMelanocytesMelanomaPhosphoproteinsPhosphorylationProteomicsReceptor Protein-Tyrosine KinasesReceptor, IGF Type 2RNA, Small InterferingSignal TransductionSkin NeoplasmsSTAT3 Transcription FactorConceptsTherapeutic targetReceptor tyrosine kinasesMelanoma cellsPotential therapeutic targetIdentifies potential therapeutic targetsActive receptor tyrosine kinasesTyrosine kinaseMelanoma cell migrationReceptor expressionBreast cancerAxl knockdownAutocrine circuitTherapeutic interventionsCancer subtypesReceptor tyrosine kinase activationTyrosine kinase activationNovel targetActivated receptorsAxlRNA knockdownMelanomaCell migrationHER3KnockdownIGF1R
2009
Genome-wide screen of promoter methylation identifies novel markers in melanoma
Koga Y, Pelizzola M, Cheng E, Krauthammer M, Sznol M, Ariyan S, Narayan D, Molinaro AM, Halaban R, Weissman SM. Genome-wide screen of promoter methylation identifies novel markers in melanoma. Genome Research 2009, 19: 1462-1470. PMID: 19491193, PMCID: PMC2720187, DOI: 10.1101/gr.091447.109.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAdultAgedBiomarkers, TumorCells, CulturedCluster AnalysisCollagenCollagen Type IDNA MethylationFemaleGene Expression ProfilingGenome, HumanGenome-Wide Association StudyHSP20 Heat-Shock ProteinsHumansInfant, NewbornMaleMelanomaMetallothioneinMiddle AgedMolecular ChaperonesNuclear ProteinsNucleoplasminsOligonucleotide Array Sequence AnalysisPhosphoproteinsPromoter Regions, GeneticProteinsReproducibility of ResultsReverse Transcriptase Polymerase Chain ReactionSequence Analysis, DNATumor Cells, CulturedConceptsDifferential gene expressionGene expressionPromoter methylationGenome-wide promoter methylationGenome-wide integrative analysisPromoter CpG contentMethylation markersGenome-wide screenSequencing of bisulfiteTranscription start siteMelanoma cell strainsCell strainsTranscriptional machineryNovel genesEpigenetic modificationsDNA methylationIdentifies novel markersStart siteSnap-frozen tissuesCpG contentAdult melanocytesIntegrative analysisReal-time reverse transcriptase PCRHuman diseasesMethylation
2008
MEDME: An experimental and analytical methodology for the estimation of DNA methylation levels based on microarray derived MeDIP-enrichment
Pelizzola M, Koga Y, Urban AE, Krauthammer M, Weissman S, Halaban R, Molinaro AM. MEDME: An experimental and analytical methodology for the estimation of DNA methylation levels based on microarray derived MeDIP-enrichment. Genome Research 2008, 18: 1652-1659. PMID: 18765822, PMCID: PMC2556264, DOI: 10.1101/gr.080721.108.Peer-Reviewed Original ResearchConceptsDNA methylation levelsDNA methylationMethylation levelsRelative DNA methylation levelsChromosome-wide levelBisulfite genomic DNA sequencingGenome-wide studiesMelanoma cell strainsDNA methylation statusGenomic DNA sequencingTranscriptional machineryNormal human melanocytesMethylated CpGsMethylated fragmentsEpigenetic modificationsMethylation estimatesHigh-throughput settingHuman diseasesHuman melanocytesMethylationMethylation statusDNA sequencingAntibody enrichmentGenomeCell strains
1997
Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells
Halaban R, Cheng E, Zhang Y, Moellmann G, Hanlon D, Michalak M, Setaluri V, Hebert D. Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 6210-6215. PMID: 9177196, PMCID: PMC21028, DOI: 10.1073/pnas.94.12.6210.Peer-Reviewed Original ResearchMeSH KeywordsAdultCalcium-Binding ProteinsCalnexinCalreticulinCell DifferentiationCells, CulturedCoculture TechniquesEndoplasmic ReticulumEnzyme PrecursorsHumansInfant, NewbornKineticsMelanocytesMelanomaMolecular ChaperonesMolecular WeightMonophenol MonooxygenasePhenotypeRibonucleoproteinsSkin NeoplasmsTime FactorsTumor Cells, CulturedConceptsEndoplasmic reticulumNormal melanocytesER chaperone calnexinMelanin synthesisMalignant melanocytesMelanoma cellsChaperone bindingAberrant retentionChaperone calnexinGolgi compartmentSubcellular localizationAmelanotic melanoma cell lineKey enzymeMelanoma cell linesMaturation of tyrosinaseAmelanotic melanoma cellsKinetics of synthesisInhibitor sensitivityDedifferentiated phenotypeProteolytic degradationCell linesProteasome inhibitorsEnzymeProteasomeImmature forms
1995
Identification of p90RSK as the probable CREB-Ser133 kinase in human melanocytes.
Böhm M, Moellmann G, Cheng E, Alvarez-Franco M, Wagner S, Sassone-Corsi P, Halaban R. Identification of p90RSK as the probable CREB-Ser133 kinase in human melanocytes. Molecular Cancer Research 1995, 6: 291-302. PMID: 7540859.Peer-Reviewed Original ResearchMeSH KeywordsCell CountCell DivisionCells, CulturedCyclic AMPCyclic AMP Response Element-Binding ProteinDrug SynergismEndothelinsFibroblast Growth Factor 2Growth SubstancesHematopoietic Cell Growth FactorsHepatocyte Growth FactorHumansInfant, NewbornMelanocytesPhosphorylationProtein Serine-Threonine KinasesRecombinant Fusion ProteinsRibosomal Protein S6 KinasesSerineStem Cell FactorTime FactorsTranscription FactorsConceptsSynergistic growth factorsMast/stem cell growth factorHuman melanocytesGrowth factorHepatocyte growth factor/scatter factorActivation of p90RSKGrowth factor/scatter factorStem cell growth factorCAMP-responsive element binding proteinKID domainElement-binding proteinNormal human melanocytesTranscription factor 1Peptide growth factorsSer133 phosphorylationTranscriptional activationCell divisionPhosphorylated stateTranscription factorsInduces phosphorylationRegulatory proteinsSignal transducerFibroblast growth factorBasic fibroblast growth factorBinding protein
1993
Altered Metabolism of Mast-Cell Growth Factor (c-kit Ligand) in Cutaneous Mastocytosis
Longley B, Morganroth G, Tyrrell L, Ding T, Anderson D, Williams D, Halaban R. Altered Metabolism of Mast-Cell Growth Factor (c-kit Ligand) in Cutaneous Mastocytosis. New England Journal Of Medicine 1993, 328: 1302-1307. PMID: 7682288, DOI: 10.1056/nejm199305063281803.Peer-Reviewed Original ResearchConceptsMast cell growth factorMessenger RNAGrowth factorC-kit proto-oncogeneProduction of melaninSoluble formGrowth factor geneFactor genesProteolytic processingProto-oncogeneSequence abnormalitiesExtracellular spaceAltered metabolismAltered distributionGrowth factor messenger RNASkin of patientsDermal cellsCellsPolymerase chain reactionCutaneous mastocytosisMast cellsPigmentation and Proliferation of Human Melanocytes and the Effects of Melanocyte‐Stimulating Hormone and Ultraviolet B Lighta
HALABAN R, TYRRELL L, LONGLEY J, YARDEN Y, RUBIN J. Pigmentation and Proliferation of Human Melanocytes and the Effects of Melanocyte‐Stimulating Hormone and Ultraviolet B Lighta. Annals Of The New York Academy Of Sciences 1993, 680: 290-301. PMID: 7685575, DOI: 10.1111/j.1749-6632.1993.tb19691.x.Peer-Reviewed Original Research
1987
bFGF is the putative natural growth factor for human melanocytes
Halaban R, Ghosh S, Baird A. bFGF is the putative natural growth factor for human melanocytes. In Vitro Cellular & Developmental Biology 1987, 23: 47-52. PMID: 3027025, DOI: 10.1007/bf02623492.Peer-Reviewed Original Research
1986
Human Melanocytes Cultured from Nevi and Melanomas
Halaban R, Ghosh S, Duray P, Kirkwood J, Lerner A. Human Melanocytes Cultured from Nevi and Melanomas. Journal Of Investigative Dermatology 1986, 87: 95-101. PMID: 2425008, DOI: 10.1111/1523-1747.ep12523594.Peer-Reviewed Original ResearchConceptsPresence of mitogensHuman melanocytesNeonatal melanocytesRate of proliferationPrimary melanomaCongenital neviMalignant transformationTransformation of melanocytesCholera toxinIsobutylmethyl xanthineHuman placentaGrowth factorProliferative rateMelanomaNewborn foreskinUnidentified factorsCell linesMelanocytesMitogenNeviHuman neonatal melanocytesPopulation doublingsMonthsLate eventProliferation