2002
Signaling disrupts mSin3A binding to the Mad1‐like Sin3‐interacting domain of TIEG2, an Sp1‐like repressor
Ellenrieder V, Zhang J, Kaczynski J, Urrutia R. Signaling disrupts mSin3A binding to the Mad1‐like Sin3‐interacting domain of TIEG2, an Sp1‐like repressor. The EMBO Journal 2002, 21: 2451-2460. PMID: 12006497, PMCID: PMC126002, DOI: 10.1093/emboj/21.10.2451.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAmino Acid SequenceAnimalsBinding SitesCell Cycle ProteinsCHO CellsConsensus SequenceCricetinaeGenes, ReporterKruppel-Like Transcription FactorsMicePhosphorylationProtein BindingRecombinant ProteinsRepressor ProteinsSignal TransductionSin3 Histone Deacetylase and Corepressor ComplexSp1 Transcription FactorTranscription FactorsTransfectionZinc FingersConceptsSin3 interaction domainTranscriptional repressionAnti-proliferative functionMad proteinsRepressor proteinRepression activitySerine/threonine sitesTranscription factorsConstitutive mannerSignaling pathwayRepressionGrowth suppressionFunctional impactTIEG2ProteinRepressorSerine/threonineTIEGTranscriptionPhosphorylationDomainSignalPathwayInteractionBinding
2000
Detailed domain structure and MAP kinase-mediated phosphorylation of the growth suppressor transcription factor, TIEG2
Ellenrieder V, Kaczynski J, Hedin K, Urrutia R. Detailed domain structure and MAP kinase-mediated phosphorylation of the growth suppressor transcription factor, TIEG2. Gastroenterology 2000, 118: a639. DOI: 10.1016/s0016-5085(00)84693-4.Peer-Reviewed Original Research