2008
Nuclear to non-nuclear Pmel17/gp100 expression (HMB45 staining) as a discriminator between benign and malignant melanocytic lesions
Rothberg BE, Moeder CB, Kluger H, Halaban R, Elder DE, Murphy GF, Lazar A, Prieto V, Duncan LM, Rimm DL. Nuclear to non-nuclear Pmel17/gp100 expression (HMB45 staining) as a discriminator between benign and malignant melanocytic lesions. Modern Pathology 2008, 21: 1121-1129. PMID: 18552823, PMCID: PMC2570478, DOI: 10.1038/modpathol.2008.100.Peer-Reviewed Original ResearchAntigens, NeoplasmBiomarkers, TumorCell NucleusDiagnosis, DifferentialFluorescent Antibody Technique, IndirectGp100 Melanoma AntigenHumansImage Processing, Computer-AssistedImmunoenzyme TechniquesMelanomaMelanoma-Specific AntigensMembrane GlycoproteinsNeoplasm ProteinsNevus, PigmentedSkin NeoplasmsTissue Array Analysis
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
Translation Rate of Human Tyrosinase Determines ItsN-Linked Glycosylation Level*
Újvári A, Aron R, Eisenhaure T, Cheng E, Parag H, Smicun Y, Halaban R, Hebert D. Translation Rate of Human Tyrosinase Determines ItsN-Linked Glycosylation Level*. Journal Of Biological Chemistry 2000, 276: 5924-5931. PMID: 11069924, DOI: 10.1074/jbc.m009203200.Peer-Reviewed Original ResearchConceptsTranslation rateCell-free systemProtein translation ratesType I membrane glycoproteinsNormal melanocytesHuman tyrosinaseSemi-permeabilized cellsMelanoma cellsUbiquitin-proteasomal pathwayRate of translationSite-directed mutagenesisWild-type tyrosinaseProtein synthesis inhibitor cycloheximideInefficient glycosylationGlycosylation efficiencyAberrant retentionProtein translationCotranslational eventsConsensus sitesCore glycanDegradative fateProtein doubletEndoplasmic reticulumMaturation eventsAmelanotic melanoma cells
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 ResearchMeSH KeywordsAnimalsGp100 Melanoma AntigenHumansIndolesMelaninsMelanocytesMembrane GlycoproteinsMolecular WeightMutationOxidoreductasesPigmentationProteinsRabbitsConceptsPmel 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
1995
Mouse silver. mutation is caused by a single base insertion in the putative cytoplasmic domain of Pmel 17
Kwon B, Halaban R, Ponnazhagan S, Kim K, Chintamaneni C, Bennett D, Pickard R. Mouse silver. mutation is caused by a single base insertion in the putative cytoplasmic domain of Pmel 17. Nucleic Acids Research 1995, 23: 154-158. PMID: 7870580, PMCID: PMC306643, DOI: 10.1093/nar/23.1.154.Peer-Reviewed Original ResearchConceptsPmel 17CDNA clonesMelanocyte cDNA libraryPutative cytoplasmic tailPutative cytoplasmic domainAmino acidsMouse chromosome 10Coat color locusSingle nucleotide insertionSilver locusSingle base insertionChromosomal locationGenomic regionsCytoplasmic domainTermination signalCytoplasmic tailCDNA libraryReading frameSI allelesColor locusCarboxyl terminusC-terminusChromosome 10Nucleotide insertionBase insertion
1994
Characterization of Mouse Pmel 17 Gene and Silver Locus
KWON B, KIM K, HALABAN R, PICKARD R. Characterization of Mouse Pmel 17 Gene and Silver Locus. Pigment Cell & Melanoma Research 1994, 7: 394-397. PMID: 7761347, DOI: 10.1111/j.1600-0749.1994.tb00067.x.Peer-Reviewed Original ResearchConceptsCDNA clonesPutative cytoplasmic tailPmel 17Amino acidsC-terminal amino acidsSingle nucleotide insertionSilver locusGenomic regionsCytoplasmic tailCarboxyl terminusC-terminusMurine melanocytesNucleotide insertionMutation sitesProteinClonesGenesTerminusLociMajor defectsMutationsResiduesAcidMelanocytesInsertion