2005
Activation of the Checkpoint Kinase Rad53 by the Phosphatidyl Inositol Kinase-like Kinase Mec1*
Ma JL, Lee SJ, Duong JK, Stern DF. Activation of the Checkpoint Kinase Rad53 by the Phosphatidyl Inositol Kinase-like Kinase Mec1*. Journal Of Biological Chemistry 2005, 281: 3954-3963. PMID: 16365046, DOI: 10.1074/jbc.m507508200.Peer-Reviewed Original ResearchConceptsPhosphorylation-dependent mechanismDNA damageKinase activityDNA replication checkpoint pathwayRad53 kinase activityCheckpoint kinase Rad53Essential protein kinaseReplication checkpoint pathwayActivation of Rad53Protein kinase activityMammalian Chk2Rad53 phosphorylationRad53 activationRad53Protein kinaseDownstream responsesCheckpoint pathwayOrthologsAutophosphorylationKinasePhosphorylationIntermolecular mechanismActivationPIKKsComplexes
2004
A Ddc2-Rad53 Fusion Protein Can Bypass the Requirements for RAD9 and MRC1 in Rad53 Activation
Lee SJ, Duong JK, Stern DF. A Ddc2-Rad53 Fusion Protein Can Bypass the Requirements for RAD9 and MRC1 in Rad53 Activation. Molecular Biology Of The Cell 2004, 15: 5443-5455. PMID: 15456903, PMCID: PMC532024, DOI: 10.1091/mbc.e04-07-0608.Peer-Reviewed Original ResearchConceptsDNA damageDNA damage checkpoint pathwayFusion proteinDamage checkpoint pathwayRad53p activationRad53 activationMethyl methaneCheckpoint pathwaySignaling systemCell survivalMediator requirementMec1pEssential roleProteinCellsActivationExpressionRad53pRad9pDdc2Rad9Mrc1pMinimal requirementsMrc1OligomerizationEstablishment of a Cell-Free System to Study the Activation of Chk2
Xu X, Stern DF. Establishment of a Cell-Free System to Study the Activation of Chk2. Methods In Molecular Biology 2004, 280: 165-174. PMID: 15187252, DOI: 10.1385/1-59259-788-2:165.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAtaxia Telangiectasia Mutated ProteinsCell Cycle ProteinsCell-Free SystemCheckpoint Kinase 2DNA DamageDNA-Binding ProteinsGenetic VectorsHumansImmunoblottingPlasmidsPrecipitin TestsProtein BiosynthesisProtein Serine-Threonine KinasesRabbitsReticulocytesTranscription, GeneticTriticumTumor Suppressor ProteinsConceptsActivation of Chk2Cell-free systemVitro transcription/translation systemTranscription/translation systemCheckpoint kinase Chk2Rabbit reticulocyte lysateWheat germ extractKinase Chk2Identification of cofactorsReticulocyte lysateChk2Germ extractDNA damageTranslation systemActivationKinaseCofactorProteinATRLysatesPathway
1992
A 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
1988
Oncogenic activation of p185neu stimulates tyrosine phosphorylation in vivo.
Stern DF, Kamps MP, Cao H. Oncogenic activation of p185neu stimulates tyrosine phosphorylation in vivo. Molecular And Cellular Biology 1988, 8: 3969-3973. PMID: 2464744, PMCID: PMC365461, DOI: 10.1128/mcb.8.9.3969.Peer-Reviewed Original Research