1990
Murine and human b locus pigmentation genes encode a glycoprotein (gp75) with catalase activity.
Halaban R, Moellmann G. Murine and human b locus pigmentation genes encode a glycoprotein (gp75) with catalase activity. Proceedings Of The National Academy Of Sciences Of The United States Of America 1990, 87: 4809-4813. PMID: 1693779, PMCID: PMC54207, DOI: 10.1073/pnas.87.12.4809.Peer-Reviewed Original ResearchConceptsPigmentation genesRapid proteolytic degradationMelanosomal glycoproteinLocus proteinBrown locusCatalase BB mutationsProteolytic degradationB locusMelanogenic activityGenesMelanin precursorsLociProteinMutationsGlycoproteinCatalase activityTyrosinaseHydrogen peroxideHydroperoxidaseMelanogenesisGp75ActivityMurinePigmentation
1989
Isolation, Chromosomal Mapping, and Expression of the Mouse Tyrosinase Gene
Kwon B, Haq A, Wakulchik M, Kestler D, Barton D, Francke U, Lamoreux M, Whitney J, Halaban R. Isolation, Chromosomal Mapping, and Expression of the Mouse Tyrosinase Gene. Journal Of Investigative Dermatology 1989, 93: 589-594. PMID: 2507645, DOI: 10.1111/1523-1747.ep12319693.Peer-Reviewed Original ResearchConceptsMouse tyrosinaseTyrosinase geneMouse chromosome 7Mouse tyrosinase geneSomatic cell hybridsSouthern blot analysisChromosomal mappingGenomic clonesCell hybridsPromoter sequencesTATA elementAlbino locusChromosome 7Melanoma cell linesCDNA probeNormal melanocytesTyrosinase mRNABackcross miceBlot analysisFarthest upstreamCell linesDeletion miceGenesLociCloudman SMolecular basis of mouse Himalayan mutation
Kwon B, Halaban R, Chintamaneni C. Molecular basis of mouse Himalayan mutation. Biochemical And Biophysical Research Communications 1989, 161: 252-260. PMID: 2567165, DOI: 10.1016/0006-291x(89)91588-x.Peer-Reviewed Original ResearchConceptsAmino acid 420Histidine residuesAmino acidsTemperature-sensitive tyrosinaseCDNA libraryHimalayan miceMouse tyrosinaseInteresting mutantsNucleotide sequenceB proteinMolecular basisTyrosinase geneTyrosinase cDNAArginine residuesTyrosinase moleculesHuman tyrosinaseG changeResiduesMutationsTyrosinaseMutantsCDNAGenesMiceTyrosinase inhibitors
1988
Tyrosinases of murine melanocytes with mutations at the albino locus.
Halaban R, Moellmann G, Tamura A, Kwon BS, Kuklinska E, Pomerantz SH, Lerner AB. Tyrosinases of murine melanocytes with mutations at the albino locus. Proceedings Of The National Academy Of Sciences Of The United States Of America 1988, 85: 7241-7245. PMID: 3140237, PMCID: PMC282161, DOI: 10.1073/pnas.85.19.7241.Peer-Reviewed Original ResearchConceptsAlbino locusTrans-Golgi networkWild-type melanocytesWild-type strainAbnormal posttranslational modificationsSynthesis of melaninDiminished pigmentationStructural genePosttranslational modificationsMurine melanocytesLocus mutantsKey enzymeLevels of mRNAMutantsKinetics of activationProteolytic cleavageUnstable enzymeEnzymeLociMelanocytesReduced levelsMutationsConfer susceptibilityTyrosinaseLittle enzymeSequence analysis of mouse tyrosinase cDNA and the effect of melanotropin on its gene expression
Kwon B, Wakulchik M, Haq A, Halaban R, Kestler D. Sequence analysis of mouse tyrosinase cDNA and the effect of melanotropin on its gene expression. Biochemical And Biophysical Research Communications 1988, 153: 1301-1309. PMID: 3134020, DOI: 10.1016/s0006-291x(88)81370-6.Peer-Reviewed Original ResearchConceptsAmino acid sequenceAcid sequenceTyrosinase cDNAPotential N-glycosylation sitesMouse genomic cloneHistidine-rich regionMouse tyrosinase geneN-glycosylation sitesLevels of transcriptsCopper-binding siteMouse tyrosinase cDNADeduced proteinGenomic clonesTransmembrane sequenceHuman tyrosinase cDNACDNA clonesMouse tyrosinaseTyrosinase geneGene expressionSequence analysisAmino acidsHuman tyrosinaseClonesCDNAMelanoma cellsCloning and characterization of a human tyrosinase cDNA.
Kwon B, Haq A, Kim G, Pomerantz S, Halaban R. Cloning and characterization of a human tyrosinase cDNA. Progress In Clinical And Biological Research 1988, 256: 273-82. PMID: 2835779.Peer-Reviewed Original Research
1987
A melanocyte-specific complementary DNA clone whose expression is inducible by melanotropin and isobutylmethyl xanthine.
Kwon B, Halaban R, Kim G, Usack L, Pomerantz S, Haq A. A melanocyte-specific complementary DNA clone whose expression is inducible by melanotropin and isobutylmethyl xanthine. Molecular Biology & Medicine 1987, 4: 339-55. PMID: 2449595.Peer-Reviewed Original ResearchMeSH Keywords1-Methyl-3-isobutylxanthineAnimalsAntibodies, MonoclonalCatechol OxidaseDNAGene Expression RegulationGlycoproteinsHumansMelaninsMelanocyte-Stimulating HormonesMelanocytesMelanomaMelanoma, ExperimentalMiceMonophenol MonooxygenaseNeoplasm ProteinsPigmentationSpecies SpecificityTheophyllineTumor Cells, CulturedConceptsPmel 17CDNA clonesLambda gt11 cDNA libraryComplementary DNA cloneHuman tyrosinase geneNormal human melanocytesSingle geneDNA clonesCDNA libraryStimulation of humanMRNA speciesTyrosinase geneMurine melanocytesMurine DNAMurine melanoma cellsRestriction fragmentsHuman melanocytesRepresentative clonesGenesClonesImmunological homologyCDNAMelanoma cellsMelanocytesSpeciesIsolation and sequence of a cDNA clone for human tyrosinase that maps at the mouse c-albino locus.
Kwon BS, Haq AK, Pomerantz SH, Halaban R. Isolation and sequence of a cDNA clone for human tyrosinase that maps at the mouse c-albino locus. Proceedings Of The National Academy Of Sciences Of The United States Of America 1987, 84: 7473-7477. PMID: 2823263, PMCID: PMC299318, DOI: 10.1073/pnas.84.21.7473.Peer-Reviewed Original ResearchConceptsCDNA clonesMelanocyte cDNA libraryRelated mRNA speciesHuman tyrosinaseAmino acid sequenceSouthern blot analysisStructural geneCDNA libraryNucleotide sequenceMRNA speciesAcid sequenceGlycosylation sitesCDNA insertDeletion mutationsCell typesAmino acidsCopper bindingBlot analysisClonesMalignant melanocytesLociSequenceTyrosinaseApproximate lengthKilobasesTyrosinase and Acid Phosphatase Activities in Melanocytes from Avian Albinos
Boissy R, Moellmann G, Halaban R. Tyrosinase and Acid Phosphatase Activities in Melanocytes from Avian Albinos. Journal Of Investigative Dermatology 1987, 88: 292-300. PMID: 3102623, DOI: 10.1111/1523-1747.ep12466164.Peer-Reviewed Original Research
1984
Tyrosinase activity and abundance in Cloudman melanoma cells
Halaban R, Pomerantz S, Marshall S, Lerner A. Tyrosinase activity and abundance in Cloudman melanoma cells. Archives Of Biochemistry And Biophysics 1984, 230: 383-387. PMID: 6201140, DOI: 10.1016/0003-9861(84)90121-8.Peer-Reviewed Original Research
1983
Regulation of tyrosinase in human melanocytes grown in culture.
Halaban R, Pomerantz S, Marshall S, Lambert D, Lerner A. Regulation of tyrosinase in human melanocytes grown in culture. Journal Of Cell Biology 1983, 97: 480-488. PMID: 6411733, PMCID: PMC2112541, DOI: 10.1083/jcb.97.2.480.Peer-Reviewed Original ResearchConceptsHuman melanocytesApparent molecular weightMalignant human melanocytesTyrosinase activityMajor biochemical eventsExpression of tyrosinaseSynthesis of melaninRegulation of tyrosinasePosttranslational modificationsImmunoprecipitation experimentsO-glycosylationBiochemical eventsNormal melanocytesMelanocytesMolecular weightProteinEnzymeTyrosinaseTunicamycinAbundanceActivityRegulationHigh levelsLow levelsCulture
1975
Melanoma cells resistant to inhibition of growth by melanocyte stimulating hormone.
Pawelek J, Sansone M, Koch N, Christie G, Halaban R, Hendee J, Lerner A, Varga J. Melanoma cells resistant to inhibition of growth by melanocyte stimulating hormone. Proceedings Of The National Academy Of Sciences Of The United States Of America 1975, 72: 951-955. PMID: 165495, PMCID: PMC432441, DOI: 10.1073/pnas.72.3.951.Peer-Reviewed Original Research