2004
Phosphorylation of Plk1 at S137 and T210 is Inhibited in Response to DNA Damage
Tsvetkov L, Stern DF. Phosphorylation of Plk1 at S137 and T210 is Inhibited in Response to DNA Damage. Cell Cycle 2004, 4: 166-171. PMID: 15611664, DOI: 10.4161/cc.4.1.1348.Peer-Reviewed Original ResearchMeSH KeywordsAtaxia Telangiectasia Mutated ProteinsCaffeineCDC2 Protein KinaseCdc25 PhosphatasesCell Cycle ProteinsCell DivisionCell Line, TumorCheckpoint Kinase 1Checkpoint Kinase 2Cyclin BDNA DamageDNA-Binding ProteinsDoxorubicinEnzyme ActivationG2 PhaseHumansMitosisNocodazolePhosphorylationProtein KinasesProtein Serine-Threonine KinasesProto-Oncogene ProteinsSerineSignal TransductionStaurosporineThreonineTumor Suppressor ProteinsConceptsDNA damage checkpointThreonine 210Damage checkpointPlk1 phosphorylationDNA damageCdc2/cyclin B kinaseATR-dependent checkpoint pathwayChk2 protein kinaseDNA damage-induced inhibitionATM/ATRCyclin B kinasePolo-like kinase 1Phosphorylation of PLK1Activation of Cdc25CNuclear importPhosphopeptide mappingMitotic entryActivation loopPhosphorylation sitesVivo phosphorylationPlk1 activityKinase domainProtein kinasePrevents phosphorylationActive mutant
2003
Rad53 Phosphorylation Site Clusters Are Important for Rad53 Regulation and Signaling
Lee SJ, Schwartz MF, Duong JK, Stern DF. Rad53 Phosphorylation Site Clusters Are Important for Rad53 Regulation and Signaling. Molecular And Cellular Biology 2003, 23: 6300-6314. PMID: 12917350, PMCID: PMC180918, DOI: 10.1128/mcb.23.17.6300-6314.2003.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmino Acid SubstitutionBinding SitesCell Cycle ProteinsCheckpoint Kinase 2DNA DamageFungal ProteinsIntracellular Signaling Peptides and ProteinsMAP Kinase Kinase 1Mitogen-Activated Protein Kinase KinasesMutationPhosphorylationProtein KinasesProtein Serine-Threonine KinasesProtein Structure, TertiarySaccharomyces cerevisiae ProteinsSaccharomycetalesSchizosaccharomyces pombe ProteinsSignal TransductionConceptsDNA damage-induced interactionsPhosphorylation of Rad53Rad53 kinase activityTel1-dependent mannerEssential protein kinaseDNA damageConsensus phosphorylation sitesRad53 activationRad53 phosphorylationFHA domainPhosphorylation sitesCheckpoint functionUpstream kinaseYeast Rad53Protein kinaseRad53Kinase activityAlanine substitutionsReplication blockadeBasal interactionSubstitution mutationsImpaired interactionDun1Mec1Site clusters
2000
Production of Antibodies That Recognize Specific Tyrosine‐Phosphorylated Peptides
DiGiovanna M, Roussel R, Stern D. Production of Antibodies That Recognize Specific Tyrosine‐Phosphorylated Peptides. Current Protocols In Molecular Biology 2000, 50: 18.6.1-18.6.19. PMID: 18265171, DOI: 10.1002/0471142727.mb1806s50.BooksConceptsAnti-phosphopeptide antibodiesIndividual phosphorylation sitesAnalysis of phosphoproteinsAnti-phosphoamino acid antibodiesPhosphorylation sitesUnphosphorylated proteinTyrosine phosphorylated peptidesCognate proteinPhosphorylated stateParticular proteinAffinity matrixProteinUnique specificityPhosphoproteinFunctional stateDifferential isolationSuch reagentsPhosphotyrosinePeptidesSupport protocolSpeciesAbundanceProduction of antibodiesConventional antibodies