2021
Retrospective cell lineage reconstruction in humans by using short tandem repeats
Tao L, Raz O, Marx Z, Ghosh MS, Huber S, Greindl-Junghans J, Biezuner T, Amir S, Milo L, Adar R, Levy R, Onn A, Chapal-Ilani N, Berman V, Arie A, Rom G, Oron B, Halaban R, Czyz ZT, Werner-Klein M, Klein CA, Shapiro E. Retrospective cell lineage reconstruction in humans by using short tandem repeats. Cell Reports Methods 2021, 1: 100054. PMID: 34341783, PMCID: PMC8313865, DOI: 10.1016/j.crmeth.2021.100054.Peer-Reviewed Original ResearchConceptsLineage reconstructionShort tandem repeatsCell lineagesTandem repeatsCell lineage reconstructionCell lineage analysisSingle cellsLineage tracing methodHuman cell lineagesGenome editingLineage analysisMolecular inversion probesReconstructed lineagesLineagesDU145 cellsSomatic mutationsDiscovery platformCell of originRepeatsHealthy cellsCellsImportant insightsTissue formationOrganismsDevelopmental history
2016
A generic, cost-effective, and scalable cell lineage analysis platform
Biezuner T, Spiro A, Raz O, Amir S, Milo L, Adar R, Chapal-Ilani N, Berman V, Fried Y, Ainbinder E, Cohen G, Barr H, Halaban R, Shapiro E. A generic, cost-effective, and scalable cell lineage analysis platform. Genome Research 2016, 26: 1588-1599. PMID: 27558250, PMCID: PMC5088600, DOI: 10.1101/gr.202903.115.Peer-Reviewed Original ResearchConceptsLineage analysisSingle cell lineage analysisSingle-cell sequencing dataSingle-cell genomicsCurrent sequencing-based methodsIndividual cellsCell lineage analysisSingle-cell sequencingSequencing-based methodsLineage treesSequencing dataLineage relationsCellsTreesGenomicsAnalysis platformInput cellsSequencingBulk analysisVivoDiscoveryLandscapeAMPK promotes tolerance to Ras pathway inhibition by activating autophagy
Sanduja S, Feng Y, Mathis RA, Sokol ES, Reinhardt F, Halaban R, Gupta PB. AMPK promotes tolerance to Ras pathway inhibition by activating autophagy. Oncogene 2016, 35: 5295-5303. PMID: 27041569, PMCID: PMC6086350, DOI: 10.1038/onc.2016.70.Peer-Reviewed Original ResearchConceptsCellular energy sensor AMPEnergy sensor AMPPathway inhibitorTargeted inhibitorsRas-Raf pathwayDrug-tolerant cellsPathway inhibitionOncogenic RasProtein kinaseRaf signalingRas pathway inhibitionReduced growthAMPKAutophagyPathway mutationsCancer cellsResistant cellsKey mechanismPathwayInhibitorsCellsToleranceKinaseSignalingInhibition
2014
Identification of PLX4032‐resistance mechanisms and implications for novel RAF inhibitors
Choi J, Landrette SF, Wang T, Evans P, Bacchiocchi A, Bjornson R, Cheng E, Stiegler AL, Gathiaka S, Acevedo O, Boggon TJ, Krauthammer M, Halaban R, Xu T. Identification of PLX4032‐resistance mechanisms and implications for novel RAF inhibitors. Pigment Cell & Melanoma Research 2014, 27: 253-262. PMID: 24283590, PMCID: PMC4065135, DOI: 10.1111/pcmr.12197.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCell Line, TumorCell ProliferationDNA Transposable ElementsDrug Resistance, NeoplasmHumansIndolesMAP Kinase Signaling SystemMelanomaModels, MolecularMolecular Sequence DataMutagenesis, InsertionalMutant ProteinsMutationProtein Kinase InhibitorsProto-Oncogene Proteins B-rafSulfonamidesVemurafenibConceptsBRAF mutationsNovel BRAF mutationBRAF inhibitorsNext-generation BRAF inhibitorsPLX4032-resistant melanoma cellsMelanoma cellsMelanoma patient survivalHuman prostate cancerBRAF mutant cellsWhole-exome sequencingMelanoma patientsPatient survivalClinical trialsProstate cancerRAF inhibitorsOncogenic mutationsNew screening approachRelevant aberrationsInhibitorsCellsMutationsScreening approachNovel RAF inhibitorsPatientsPLX8394
2010
PLX4032, a selective BRAFV600E kinase inhibitor, activates the ERK pathway and enhances cell migration and proliferation of BRAFWT melanoma cells
Halaban R, Zhang W, Bacchiocchi A, Cheng E, Parisi F, Ariyan S, Krauthammer M, McCusker JP, Kluger Y, Sznol M. PLX4032, a selective BRAFV600E kinase inhibitor, activates the ERK pathway and enhances cell migration and proliferation of BRAFWT melanoma cells. Pigment Cell & Melanoma Research 2010, 23: 190-200. PMID: 20149136, PMCID: PMC2848976, DOI: 10.1111/j.1755-148x.2010.00685.x.Peer-Reviewed Original ResearchConceptsMelanoma cellsTumor cellsMelanoma tumor cellsPrimary melanoma cellsMetastatic tumor cellsStatus of mutationsClinical responseRate of proliferationAdvanced lesionsInhibitor PLX4032Kinase inhibitorsPLX4032ERK pathwayCell migrationNRASDownstream effectorsCell adherenceERK1/2CellsProliferationCell cycle controlMobility of cellsActive ERK1/2Therapy
2003
Tyrosinase Maturation and Oligomerization in the Endoplasmic Reticulum Require a Melanocyte-specific Factor*
Francis E, Wang N, Parag H, Halaban R, Hebert DN. Tyrosinase Maturation and Oligomerization in the Endoplasmic Reticulum Require a Melanocyte-specific Factor*. Journal Of Biological Chemistry 2003, 278: 25607-25617. PMID: 12724309, DOI: 10.1074/jbc.m303411200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalnexinCalreticulinCells, CulturedCentrifugation, Density GradientCHO CellsCricetinaeCross-Linking ReagentsDimerizationDogsElectrophoresis, Polyacrylamide GelEndoplasmic ReticulumLectinsMelanocytesMembrane GlycoproteinsMiceMicrosomesMonophenol MonooxygenaseMutationOxidoreductasesPancreasPlasmidsPolysaccharidesProtein BindingProtein BiosynthesisProtein FoldingProtein TransportProteinsRabbitsSucroseTime FactorsTranscription, GeneticTrypsinConceptsMelanocyte-specific factorsSemipermeabilized cellsEndoplasmic reticulum retentionLectin chaperones calnexinMelanocyte-specific proteinsTyrosinase-related protein 1Wild-type tyrosinaseSynthesis of melaninChaperone interactionsChaperone calnexinTyrosinase maturationMouse melanocytesTrypsin-resistant stateProtein 1Human tyrosinaseTranslation systemOligomerizationPersistent interactionsMaturationMelanocytesTyrosinaseCellsCalnexinMisfoldingER
2000
Proper Folding and Endoplasmic Reticulum to Golgi Transport of Tyrosinase Are Induced by Its Substrates, DOPA and Tyrosine*
Halaban R, Cheng E, Svedine S, Aron R, Hebert D. Proper Folding and Endoplasmic Reticulum to Golgi Transport of Tyrosinase Are Induced by Its Substrates, DOPA and Tyrosine*. Journal Of Biological Chemistry 2000, 276: 11933-11938. PMID: 11124258, DOI: 10.1074/jbc.m008703200.Peer-Reviewed Original ResearchConceptsWild-type tyrosinaseEndoplasmic reticulumProper foldingWild-type proteinMelanoma cellsLoss of pigmentationTyrosinase-positive melanoma cellsGolgi transportType proteinAlbino mutantS proteasomeSubsequent retranslocationMutant formsCatalytic stateEnzymatic activityProteolytic degradationNative formReticulumFoldingProteinTumor-derived antigenic peptidesTyrosinase activitySuppress tyrosinase activityCellsMetabolic changes
1996
Characterization and Subcellular Localization of Human Pmel 17/silver, a 100-kDa (Pre)Melanosomal Membrane Protein Associated With 5,6,-Dihydroxyindole-2-Carboxylic Acid (DHICA) Converting Activity
Lee Z, Hou L, Moellmann G, Kuklinska E, Antol K, Fraser M, Halaban R, Kwon B. Characterization and Subcellular Localization of Human Pmel 17/silver, a 100-kDa (Pre)Melanosomal Membrane Protein Associated With 5,6,-Dihydroxyindole-2-Carboxylic Acid (DHICA) Converting Activity. Journal Of Investigative Dermatology 1996, 106: 605-610. PMID: 8617992, DOI: 10.1111/1523-1747.ep12345163.Peer-Reviewed Original ResearchConceptsPmel 17Baculovirus expression vectorCo-precipitated proteinsElectron transfer chainPigmentation lociCytosolic vesiclesInsect cellsComplexed proteinsSubcellular localizationPolyclonal antibodiesProtein AssociatedMelanin biosynthesisPigment cellsExpression vectorPrimary structureTransfer chainApproximate molecular sizeHuman melanoma cellsProteinNatural proteinsOxidoreductive enzymesMelanoma cellsUltrastructural locationElectron microscopic cytochemistryCells
1993
KIT ligand (mast cell growth factor) inhibits the growth of KIT-expressing melanoma cells.
Zakut R, Perlis R, Eliyahu S, Yarden Y, Givol D, Lyman S, Halaban R. KIT ligand (mast cell growth factor) inhibits the growth of KIT-expressing melanoma cells. Oncogene 1993, 8: 2221-9. PMID: 7687762.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCell DivisionHematopoietic Cell Growth FactorsHumansMelanomaMolecular Sequence DataNeoplasm ProteinsPhosphorylationProtein-Tyrosine KinasesProto-Oncogene MasProto-Oncogene ProteinsProto-Oncogene Proteins c-kitRNA, MessengerRNA, NeoplasmStem Cell FactorTumor Cells, CulturedConceptsMast cell growth factorMelanoma cell linesNormal melanocyte developmentMelanoma cellsAberrant signal transductionMetastatic melanoma cell linesCell linesActivation of KITMelanocyte developmentSignal transductionKIT proto-oncogeneKinase activationKIT mRNAKit ligandNormal melanocytesProto-oncogeneKIT kinaseCell growth factorBiological responsesGrowth factorHuman melanomaMelanocytesCellsKIT expressionNeoplastic melanocytesA transcriptional inhibitor induced in human melanoma cells upon ultraviolet irradiation.
Yang Y, Rutberg S, Luo F, Spratt T, Halaban R, Ferrone S, Ronai Z. A transcriptional inhibitor induced in human melanoma cells upon ultraviolet irradiation. Molecular Cancer Research 1993, 4: 595-602. PMID: 8398900.Peer-Reviewed Original ResearchAltered 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 cellsGrowth Regulation in Normal and Malignant Melanocytes
Halaban R. Growth Regulation in Normal and Malignant Melanocytes. Recent Results In Cancer Research 1993, 128: 133-150. PMID: 8356315, DOI: 10.1007/978-3-642-84881-0_10.Peer-Reviewed Original ResearchConceptsNormal human melanocytesHuman melanocytesSignal transduction pathwaysGrowth factorMalignant melanocytesGrowth factors/receptorsTransduction pathwaysGrowth regulationConstitutive activationBiochemical basisBiochemical eventsNormal melanocytesGrowth phaseRadial growth phaseMalignant stateMelanocytesMelanoma cellsNormal counterpartsPreneoplastic cellsReceptor activityInappropriate productionCellsMetastatic melanoma lesionsActivationReceptorsmet and HGF-SF in normal melanocytes and melanoma cells.
Halaban R, Rubin J, White W. met and HGF-SF in normal melanocytes and melanoma cells. 1993, 65: 329-39. PMID: 8380740.Peer-Reviewed Original ResearchConceptsHGF-SFFactor-dependent cellsMelanoma cellsNormal human melanocytesSignal transductionMouse melanocytesTumorigenic phenotypeHuman melanocytesHuman melanoma cellsNormal melanocytesAutocrine loopMelanocytesHuman melanomaMalignant conversionMelanin contentTyrosinase activityEctopic sitesCellsSynergistic factorExpressionBFGFERK2TransductionPhosphorylationProtein
1988
Basic fibroblast growth factor from human keratinocytes is a natural mitogen for melanocytes.
Halaban R, Langdon R, Birchall N, Cuono C, Baird A, Scott G, Moellmann G, McGuire J. Basic fibroblast growth factor from human keratinocytes is a natural mitogen for melanocytes. Journal Of Cell Biology 1988, 107: 1611-1619. PMID: 2459134, PMCID: PMC2115244, DOI: 10.1083/jcb.107.4.1611.Peer-Reviewed Original ResearchConceptsBasic fibroblast growth factorFibroblast growth factorBFGF gene transcriptsHuman melanocytesGrowth factorNormal human melanocytesNatural mitogenHuman keratinocytesGene transcriptsNatural growth factorsNorthern blotMelanocyte mitogensMelanocyte growthMelanocytesPure culturePresence of serumMitogenSynthetic peptidesKeratinocytesCellsCAMPTranscriptsPresence of keratinocytesBindingBlotCytogenetic Analysis of Melanocytes From Premalignant Nevi and Melanomas2
Cowan J, Halaban R, Francka U. Cytogenetic Analysis of Melanocytes From Premalignant Nevi and Melanomas2. Journal Of The National Cancer Institute 1988, 80: 1159-1164. PMID: 3166071, DOI: 10.1093/jnci/80.14.1159.Peer-Reviewed Original ResearchbFGF as an autocrine growth factor for human melanomas.
Halaban R, Kwon BS, Ghosh S, Delli Bovi P, Baird A. bFGF as an autocrine growth factor for human melanomas. Oncogene Research 1988, 3: 177-86. PMID: 3226725.Peer-Reviewed Original ResearchConceptsBasic fibroblast growth factorNormal human melanocytesBFGF gene transcriptsHuman melanocytesGrowth factorAutocrine growth factorGene transcriptsHuman metastatic melanomaMolecular mechanismsFibroblast growth factorNormal melanocytesCyclic adenosine monophosphateSerum-containing mediumAnti-bFGF antibodyMelanoma cellsAbnormal expressionAdenosine monophosphateHuman melanomaMelanocytesRegular culture mediumDibutyryl cyclic adenosine monophosphateMitogenic activityCulture mediumCellsTranscripts
1987
Transplantation of Human Melanocytes
Lerner A, Halaban R, Klaus S, Moellmann G. Transplantation of Human Melanocytes. Journal Of Investigative Dermatology 1987, 89: 219-224. PMID: 3624895, DOI: 10.1111/1523-1747.ep12470973.Peer-Reviewed Original Research
1986
Phorbol Ester Serves As a Coepibolin in the Spreading of Primary Guinea Pig Epidermal Cells
Stenn K, Core N, Halaban R. Phorbol Ester Serves As a Coepibolin in the Spreading of Primary Guinea Pig Epidermal Cells. Journal Of Investigative Dermatology 1986, 87: 754-757. PMID: 2431072, DOI: 10.1111/1523-1747.ep12456946.Peer-Reviewed Original Research
1980
Pigmentation and tumorigenicity of reconstituted, cybrid and hybrid mouse cells
Halaban R, Moellmann G, Godawska E, Eisenstadt J. Pigmentation and tumorigenicity of reconstituted, cybrid and hybrid mouse cells. Experimental Cell Research 1980, 130: 427-435. PMID: 7449860, DOI: 10.1016/0014-4827(80)90021-x.Peer-Reviewed Original ResearchConceptsWhole cellsHybrid cellsSuppression of tumorigenicityMelanoma genomeMelanocytic functionNon-tumorigenic fibroblastsDonor parentMouse cellsCybridsStable expressionCytoplasmic transferCellular fragmentsTumorigenicityExpressionCytoplastsCellsViral particlesMurine melanomaGenomeChromosomesNucleoplastsPhenotypeExtinctionComparable numberPigmentation
1978
Phenylalanine hydroxylase in melanoma cells
Breakefield X, Castiglione C, Halaban R, Pawelek J, Shiman R. Phenylalanine hydroxylase in melanoma cells. Journal Of Cellular Physiology 1978, 94: 307-314. PMID: 23386, DOI: 10.1002/jcp.1040940308.Peer-Reviewed Original ResearchConceptsPhenylalanine hydroxylase activityHydroxylase activityMelanoma cellsMelanoma cell extractsS91 melanoma cellsCloudman S91 melanoma cellsP-chlorophenylalanineTyrosine hydroxylasePhenylalanine hydroxylaseTryptophan hydroxylaseHydroxylaseConversion of phenylalanineSensitive assayTyrosinase activityCellsLiver phenylalanine hydroxylaseCell extractsSodium dodecyl sulfate-polyacrylamide gel electrophoresisDodecyl sulfate-polyacrylamide gel electrophoresisSulfate-polyacrylamide gel electrophoresisLatter activityActivity