Featured Publications
NFBD1/KIAA0170 Is a Chromatin-associated Protein Involved in DNA Damage Signaling Pathways*
Xu X, Stern DF. NFBD1/KIAA0170 Is a Chromatin-associated Protein Involved in DNA Damage Signaling Pathways*. Journal Of Biological Chemistry 2002, 278: 8795-8803. PMID: 12499369, DOI: 10.1074/jbc.m211392200.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceBase SequenceCell Cycle ProteinsChromatinDNA DamageDNA PrimersDNA ReplicationDNA-Binding ProteinsFluorescent Antibody Technique, IndirectG2 PhaseHeLa CellsHumansMitosisMolecular Sequence DataNuclear ProteinsPhosphorylationSequence Homology, Amino AcidSignal TransductionTrans-ActivatorsConceptsN-terminal FHA domainChromatin-associated proteinsDNA damageDNA Damage Signaling PathwayDNA double-strand breaksDiscrete nuclear fociDNA damage responseNumber of proteinsDouble-strand breaksBRCT domainFHA domainGamma-H2AX fociNuclear fociRad50 fociDamage responseDNA repairNFBD1Signaling pathwaysTandem repeatsProteinNuclear factorUntreated cellsHydroxyurea treatmentPathwayDiffuse nuclear staining
2010
Centrosomal Chk2 in DNA damage responses and cell cycle progession
Golan A, Pick E, Tsvetkov L, Nadler Y, Kluger H, Stern DF. Centrosomal Chk2 in DNA damage responses and cell cycle progession. Cell Cycle 2010, 9: 2647-2656. PMID: 20581449, PMCID: PMC3233491, DOI: 10.4161/cc.9.13.12121.Peer-Reviewed Original Research
2005
The Plk1 Polo Box Domain Mediates a Cell Cycle and DNA Damage Regulated Interaction with Chk2
Tsvetkov LM, Tsekova RT, Xu X, Stern DF. The Plk1 Polo Box Domain Mediates a Cell Cycle and DNA Damage Regulated Interaction with Chk2. Cell Cycle 2005, 4: 602-610. PMID: 15876876, DOI: 10.4161/cc.4.4.1599.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCatalytic DomainCell CycleCell Cycle ProteinsCell DivisionCell SeparationCheckpoint Kinase 2DNA DamageDNA RepairG2 PhaseGenetic VectorsGlutathione TransferaseHeLa CellsHumansImmunoblottingImmunoprecipitationIn Vitro TechniquesMitosisPhosphorylationProtein BindingProtein KinasesProtein Serine-Threonine KinasesProtein Structure, TertiaryProto-Oncogene ProteinsSignal TransductionConceptsPlk1 polo-box domainDNA damage checkpointPolo-box domainPolo-like kinase 1Eukaryotic proteinsDamage checkpointMitotic regulationBox domainRegulated interactionPlk1 activityProtein kinaseSignaling cascadesChk2Kinase 1Tumor suppressorCell cycleDNA damageS phasePlk1M phaseMitosisMultiple processesPotential mechanismsPhosphorylatesKinase
2003
NFBD1/MDC1 regulates ionizing radiation‐induced focus formation by DNA checkpoint signaling and repair factors
Xu X, Stern DF. NFBD1/MDC1 regulates ionizing radiation‐induced focus formation by DNA checkpoint signaling and repair factors. The FASEB Journal 2003, 17: 1842-1848. PMID: 14519663, DOI: 10.1096/fj.03-0310com.Peer-Reviewed Original ResearchConceptsNFBD1/MDC1DNA checkpointMRN complexRepair factorsIRIF formationATM/ATR substratesRadiation-induced nuclear fociRadiation-induced focus formationDNA damageBRCT domainFHA domainATR substratesNbs1 complexMre11-Rad50Nuclear fociNFBD1Repair proteinsTandem repeatsFoci formationMre11NBS1MDC1CheckpointNuclear factorBinds
1991
Membrane-anchored forms of EGF stimulate focus formation and intercellular communication.
Dobashi Y, Stern DF. Membrane-anchored forms of EGF stimulate focus formation and intercellular communication. Oncogene 1991, 6: 1151-9. PMID: 1861865.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell CommunicationCell LineEpidermal Growth FactorErbB ReceptorsFibroblastsFluorescent Antibody TechniqueGene ExpressionGenes, ImmunoglobulinGenetic VectorsHeLa CellsImmunoblottingMembrane GlycoproteinsMembrane ProteinsPlasmidsProtein Sorting SignalsRatsRecombinant Fusion ProteinsSignal TransductionTransfectionViral Envelope ProteinsConceptsSoluble epidermal growth factorEpidermal growth factorEGF receptorFusion proteinFoci formationFunction of EGFG fusion proteinCytoplasmic domain sequencesMembrane-anchored formRat fibroblastsLarge propeptideTransmembrane domainAutocrine transformationPlasma membraneDomain sequencesExpression systemSoluble proteinForms of EGFIntercellular communicationHeLa cellsNeighboring cellsProteinSmall familyAnchored formCell lines
1990
The epidermal growth factor receptor and the product of the neu protooncogene are members of a receptor tyrosine phosphorylation cascade.
Connelly PA, Stern DF. The epidermal growth factor receptor and the product of the neu protooncogene are members of a receptor tyrosine phosphorylation cascade. Proceedings Of The National Academy Of Sciences Of The United States Of America 1990, 87: 6054-6057. PMID: 1974718, PMCID: PMC54470, DOI: 10.1073/pnas.87.16.6054.Peer-Reviewed Original Research
1989
The Ick tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain
Shaw A, Amrein K, Hammond C, Stern D, Sefton B, Rose J. The Ick tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain. Cell 1989, 59: 627-636. PMID: 2582490, DOI: 10.1016/0092-8674(89)90008-1.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCD4 AntigensCytoplasmHeLa CellsHumansLymphocyte Specific Protein Tyrosine Kinase p56(lck)Macromolecular SubstancesMembrane GlycoproteinsMolecular Sequence DataMutationOligonucleotide ProbesPhosphoproteinsPlasmidsProtein BindingProtein MultimerizationProtein-Tyrosine KinasesT-LymphocytesTransfectionConceptsAmino-terminal domainCytoplasmic domainTyrosine protein kinase p56lckUnique amino-terminal domainT cell-specific proteinsTyrosine protein kinaseSpecific transmembrane proteinsCell-specific proteinsIntracellular tyrosine kinaseAmino-terminal residuesCarboxy-terminal residuesTransmembrane proteinCytoplasmic tailSrc familyProtein kinaseKinase p56lckTyrosine kinaseHeLa cellsCell surfaceProteinDeleted formsSurface glycoproteinP56lckKinaseResidues