2013
RAC1P29S is a spontaneously activating cancer-associated GTPase
Davis MJ, Ha BH, Holman EC, Halaban R, Schlessinger J, Boggon TJ. RAC1P29S is a spontaneously activating cancer-associated GTPase. Proceedings Of The National Academy Of Sciences Of The United States Of America 2013, 110: 912-917. PMID: 23284172, PMCID: PMC3549122, DOI: 10.1073/pnas.1220895110.Peer-Reviewed Original ResearchAmino Acid SubstitutionAnimalsCell Surface ExtensionsChlorocebus aethiopsCOS CellsCrystallography, X-RayEnzyme ActivationGenetic Association StudiesGuanosine TriphosphateHumansHydrolysisKineticsMelanomaMiceMicroscopy, FluorescenceModels, MolecularMutation, MissenseNIH 3T3 CellsOncogenesRac1 GTP-Binding ProteinRecombinant Fusion ProteinsSignal TransductionStatic Electricity
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
VEGF121, a Vascular Endothelial Growth Factor (VEGF) Isoform Lacking Heparin Binding Ability, Requires Cell-surface Heparan Sulfates for Efficient Binding to the VEGF Receptors of Human Melanoma Cells*
Cohen T, Gitay-Goren H, Sharon R, Shibuya M, Halaban R, Levi B, Neufeld G. VEGF121, a Vascular Endothelial Growth Factor (VEGF) Isoform Lacking Heparin Binding Ability, Requires Cell-surface Heparan Sulfates for Efficient Binding to the VEGF Receptors of Human Melanoma Cells*. Journal Of Biological Chemistry 1995, 270: 11322-11326. PMID: 7744769, DOI: 10.1074/jbc.270.19.11322.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingBinding SitesCell DivisionCell LineCell MembraneCross-Linking ReagentsEndothelial Growth FactorsGene ExpressionGenetic VariationHeparinHeparitin SulfateHumansKineticsLymphokinesMelanomaReceptor Protein-Tyrosine KinasesReceptors, Growth FactorReceptors, MitogenReceptors, Vascular Endothelial Growth FactorRNA, MessengerTumor Cells, CulturedVascular Endothelial Growth Factor AVascular Endothelial Growth FactorsConceptsHuman melanoma cellsVEGF receptorsMelanoma cellsCell surface heparan sulfateVEGF receptor Flt-1VEGF receptor KDR/flkVascular endothelial growth factor isoformsHeparan sulfateReceptor KDR/flkReceptor Flt-1Growth factor isoformsCell surface heparin-like moleculesKDR/FlkVascular endothelial growth factor (VEGF) splice variantsHeparin-like moleculesAddition of heparin
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
1987
Normal murine melanocytes in culture
Tamura A, Halaban R, Moellmann G, Cowan J, Lerner M, Lerner A. Normal murine melanocytes in culture. In Vitro Cellular & Developmental Biology 1987, 23: 519-522. PMID: 3610949, DOI: 10.1007/bf02628423.Peer-Reviewed Original Research
1984
Selective elimination of fibroblasts from cultures of normal human melanocytes
Halaban R, Alfano F. Selective elimination of fibroblasts from cultures of normal human melanocytes. In Vitro Cellular & Developmental Biology 1984, 20: 447-450. PMID: 6724622, DOI: 10.1007/bf02619590.Peer-Reviewed Original Research