Featured Publications
Polo-like Kinase 1 and Chk2 Interact and Co-localize to Centrosomes and the Midbody*
Tsvetkov L, Xu X, Li J, Stern DF. Polo-like Kinase 1 and Chk2 Interact and Co-localize to Centrosomes and the Midbody*. Journal Of Biological Chemistry 2002, 278: 8468-8475. PMID: 12493754, DOI: 10.1074/jbc.m211202200.Peer-Reviewed Original ResearchConceptsPhosphorylation of Chk2Polo-like kinase 1Thr-68DNA damageSimilar subcellular localization patternsDNA damage checkpoint pathwayKinase 1Damage checkpoint pathwaySubcellular localization patternsChromosome segregationMitotic exitLate mitosisNuclear fociMitotic entryIndirect immunofluorescence microscopyMitotic checkpointSer-28Early mitosisCheckpoint pathwayChk2Localization patternsCentrosomesThr-26Immunofluorescence microscopyMidbodyActivation of Neu (ErbB-2) Mediated by Disulfide Bond-Induced Dimerization Reveals a Receptor Tyrosine Kinase Dimer Interface
Burke C, Stern D. Activation of Neu (ErbB-2) Mediated by Disulfide Bond-Induced Dimerization Reveals a Receptor Tyrosine Kinase Dimer Interface. Molecular And Cellular Biology 1998, 18: 5371-5379. PMID: 9710621, PMCID: PMC109122, DOI: 10.1128/mcb.18.9.5371.Peer-Reviewed Original Research3T3 CellsAmino Acid SequenceAmino Acid SubstitutionAnimalsCell LineCell Transformation, NeoplasticCOS CellsCysteineDimerizationDisulfidesDNA PrimersMiceModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPolymerase Chain ReactionProtein Structure, SecondaryRatsReceptor Protein-Tyrosine KinasesReceptor, ErbB-2Recombinant ProteinsSequence Alignment
2002
Chk2 Activation and Phosphorylation-Dependent Oligomerization
Xu X, Tsvetkov LM, Stern DF. Chk2 Activation and Phosphorylation-Dependent Oligomerization. Molecular And Cellular Biology 2002, 22: 4419-4432. PMID: 12024051, PMCID: PMC133858, DOI: 10.1128/mcb.22.12.4419-4432.2002.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAtaxia Telangiectasia Mutated ProteinsBinding SitesCell Cycle ProteinsCell-Free SystemCells, CulturedCheckpoint Kinase 2DNA DamageDNA-Binding ProteinsEnzyme ActivationFibroblastsGenes, Tumor SuppressorHumansMutationPhosphorylationProtein KinasesProtein Serine-Threonine KinasesProtein Structure, TertiaryRabbitsRadiation, IonizingRecombinant ProteinsSignal TransductionTumor Suppressor ProteinsConceptsSQ/TQ cluster domainsChk2 activationDNA damageDNA damage checkpoint pathwaySerine/threonine kinaseAutophosphorylation of Chk2Phosphorylation-dependent oligomerizationDamage checkpoint pathwayKinase catalytic domainForkhead-associated (FHA) domainWortmannin-sensitive kinaseChk2 kinase activityLimited DNA damageAmino acid substitutionsCell-free systemEukaryotic proteinsFHA domainActive Chk2Threonine kinaseCheckpoint functionCatalytic domainOligomeric complexesCheckpoint pathwayKinase activityChk2
1997
Ligands for ErbB-family receptors encoded by a neuregulin-like gene
Chang H, Riese II D, Gilbert W, Stern D, McMahan UJ. Ligands for ErbB-family receptors encoded by a neuregulin-like gene. Nature 1997, 387: 509-512. PMID: 9168114, DOI: 10.1038/387509a0.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsCell LineCerebellumCHO CellsCloning, MolecularCricetinaeErbB ReceptorsGlycoproteinsIn Situ HybridizationLigandsMolecular Sequence DataNeuregulinsPhosphorylationPolymerase Chain ReactionProto-Oncogene ProteinsRatsReceptor, ErbB-2Receptor, ErbB-3Receptor, ErbB-4Recombinant ProteinsTissue DistributionTyrosine
1996
The Epidermal Growth Factor Receptor Couples Transforming Growth Factor-α, Heparin-binding Epidermal Growth Factor-like Factor, and Amphiregulin to Neu, ErbB-3, and ErbB-4*
Riese D, Kim E, Elenius K, Buckley S, Klagsbrun M, Plowman G, Stern D. The Epidermal Growth Factor Receptor Couples Transforming Growth Factor-α, Heparin-binding Epidermal Growth Factor-like Factor, and Amphiregulin to Neu, ErbB-3, and ErbB-4*. Journal Of Biological Chemistry 1996, 271: 20047-20052. PMID: 8702723, DOI: 10.1074/jbc.271.33.20047.Peer-Reviewed Original ResearchMeSH KeywordsAmphiregulinAnimalsCell DivisionCell LineCell SurvivalEGF Family of ProteinsEpidermal Growth FactorErbB ReceptorsGlycoproteinsGrowth SubstancesHeparin-binding EGF-like Growth FactorIntercellular Signaling Peptides and ProteinsInterleukin-3MicePhosphorylationPhosphotyrosineProto-Oncogene ProteinsReceptor Protein-Tyrosine KinasesReceptor, ErbB-2Receptor, ErbB-3Receptor, ErbB-4Recombinant ProteinsSignal TransductionTransforming Growth Factor alphaConceptsHeparin-binding EGF-like growth factorErbB family receptorsPhysiologic responsesReceptor tyrosine phosphorylationFamily receptorsGrowth factorEpidermal growth factor (EGF) familyBa/F3 cell lineEpidermal growth factor-like factorsCell linesEGF-like growth factorGrowth factor familyTGF-alphaReceptor couplingReceptors coupleHuman malignanciesAmphiregulinTyrosine phosphorylationEGF familyErbB-3ErbB-4ReceptorsStimulationEGFSimilar pattern
1991
Spk1, a new kinase from Saccharomyces cerevisiae, phosphorylates proteins on serine, threonine, and tyrosine.
Stern DF, Zheng P, Beidler DR, Zerillo C. Spk1, a new kinase from Saccharomyces cerevisiae, phosphorylates proteins on serine, threonine, and tyrosine. Molecular And Cellular Biology 1991, 11: 987-1001. PMID: 1899289, PMCID: PMC359764, DOI: 10.1128/mcb.11.2.987.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBinding SitesCell Cycle ProteinsCheckpoint Kinase 2Cloning, MolecularEscherichia coliFungal ProteinsGene LibraryGenes, FungalImmunoblottingMolecular Sequence DataProtein KinasesProtein Serine-Threonine KinasesProtein-Tyrosine KinasesRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Nucleic AcidSerineSubstrate SpecificityThreonineTyrosineConceptsSerine/threonine kinaseProtein kinaseFusion proteinThreonine kinaseTyrosine phosphorylationGlutathione S-transferase fusion proteinCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseSerine protein kinaseSerine/threonineCalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IITyrosine protein kinaseOpen reading frameProtein kinase IILambda gt11 libraryPutative kinaseNew kinasesThreonine phosphorylationCatalytic subunitSaccharomyces cerevisiaeBacterial proteinsReading frameAntiphosphotyrosine antibodyKinase IIConstruction and expression of transforming gene resulting from fusion of basic fibroblast growth factor gene with signal peptide sequence
Rogelj S, Stern D, Klagsbrun M. Construction and expression of transforming gene resulting from fusion of basic fibroblast growth factor gene with signal peptide sequence. Methods In Enzymology 1991, 198: 117-124. PMID: 1906971, DOI: 10.1016/0076-6879(91)98013-v.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrainCattleCell LineCell Transformation, NeoplasticChimeraCloning, MolecularFibroblast Growth Factor 2Genes, SyntheticGenetic VectorsImmunoglobulin Heavy ChainsMiceMolecular Sequence DataProtein Sorting SignalsRecombinant Fusion ProteinsRecombinant ProteinsRestriction MappingTransfection