Featured Publications
Activation 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
1999
Expression of dominant-negative ErbB2 in the mammary gland of transgenic mice reveals a role in lobuloalveolar development and lactation
Jones F, Stern D. Expression of dominant-negative ErbB2 in the mammary gland of transgenic mice reveals a role in lobuloalveolar development and lactation. Oncogene 1999, 18: 3481-3490. PMID: 10376526, DOI: 10.1038/sj.onc.1202698.Peer-Reviewed Original ResearchConceptsNormal mouse mammary gland developmentDominant-negative alleleMouse mammary gland developmentMammary glandErbB2/HER2/NeuMammary gland developmentMouse mammary glandNegative allelesFunctions of ErbB2ErbB2 signalingGland developmentLobuloalveolar developmentMammary developmentProtein expressionHuman breast cancerErbB2Transgenic miceExpressionPhenotypeLobuloalveoliSignalingOverexpression
1997
Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation
Burke C, Lemmon M, Coren B, Engelman D, Stern D. Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation. Oncogene 1997, 14: 687-696. PMID: 9038376, DOI: 10.1038/sj.onc.1200873.Peer-Reviewed Original ResearchConceptsReceptor tyrosine kinasesTransmembrane domainEpidermal growth factor receptorSignal transductionWild-type domainSecond-site mutationsPosition 664Dimerization domainGrowth factor receptorTyrosine kinaseGlycophorin AFactor receptorValine substitutionDimerizationMutationsTransductionGlutamic acidDomainWeak dimerizationMutantsKinaseSignalingProteinEGFChimeras
1992
An extra cysteine proximal to the transmembrane domain induces differential cross-linking of p185neu and p185neu.
Cao H, Bangalore L, Dompé C, Bormann BJ, Stern DF. An extra cysteine proximal to the transmembrane domain induces differential cross-linking of p185neu and p185neu. Journal Of Biological Chemistry 1992, 267: 20489-20492. PMID: 1356980, DOI: 10.1016/s0021-9258(19)88728-8.Peer-Reviewed Original ResearchA subdomain in the transmembrane domain is necessary for p185neu* activation.
Cao H, Bangalore L, Bormann BJ, Stern DF. A subdomain in the transmembrane domain is necessary for p185neu* activation. The EMBO Journal 1992, 11: 923-932. PMID: 1347745, PMCID: PMC556533, DOI: 10.1002/j.1460-2075.1992.tb05131.x.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAmino Acid SequenceAnimalsBase SequenceBlotting, WesternCell MembraneElectrophoresis, Polyacrylamide GelErbB ReceptorsGliomaGlutamatesGlutamic AcidMiceMolecular Sequence DataMutagenesis, Site-DirectedNeuroblastomaPrecipitin TestsProtein-Tyrosine KinasesProto-Oncogene ProteinsRatsReceptor, ErbB-2Signal TransductionValineConceptsTransmembrane domainTyrosine kinase activityKinase activityElevated tyrosine kinase activitySite-directed mutagenesisSpecific amino acidsEpidermal growth factor receptorGlutamic acidGrowth factor receptorEGF receptorPrimary structureAmino acidsFactor receptorProteinSpecific interactionsActivationDomainMutagenesisReceptorsMolecular weightAcidNeu proteinP185neuHigh propensityRole