2003
Sp1- and Krüppel-like transcription factors
Kaczynski J, Cook T, Urrutia R. Sp1- and Krüppel-like transcription factors. Genome Biology 2003, 4: 206. PMID: 12620113, PMCID: PMC151296, DOI: 10.1186/gb-2003-4-2-206.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesDNA-Binding ProteinsEvolution, MolecularGene Expression RegulationHumansKruppel-Like Transcription FactorsMolecular Sequence DataPhylogenyRepressor ProteinsSequence Homology, Amino AcidSp1 Transcription FactorTranscription FactorsTranscription, GeneticZinc FingersConceptsKruppel-like factorCellular functionsCell- and promoter-specific mannerSp1-like proteinsGC-rich promoterTranscriptional activation domainCellular transcription machineryZinc-finger proteinPromoter-specific mannerSp1-like factorsTranscription machineryHuman genomeTranscriptional regulationDNA bindingActivation domainAmino terminusGene expressionProteinCell proliferationNeoplastic transformationFamily membersPromoterExpressionGenomeRepressorFundamentals of Transcription Factors and their Impact on Pancreatic Development and Cancer
Fernandez-Zapico M, Bramati P, Zakaria S, Kaczynski J, Urrutia R. Fundamentals of Transcription Factors and their Impact on Pancreatic Development and Cancer. Pancreatology 2003, 3: 276-283. PMID: 12890989, DOI: 10.1159/000071765.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsTranscription factorsEffectors of signaling pathwaysSynthesis of messenger RNARegulate gene expressionPancreatic developmentCellular functionsGene transcriptionTransduce signalsGene expressionTranscriptionSignaling pathwayHuman cellsDevelopment of diseaseBiology of human cellsMessenger RNACell membraneDominant control pointsProteinExpressionCellsGenesRNAApoptosisEffectorPathway
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
2001
A Conserved α-Helical Motif Mediates the Interaction of Sp1-Like Transcriptional Repressors with the Corepressor mSin3A
Zhang J, Moncrieffe M, Kaczynski J, Ellenrieder V, Prendergast F, Urrutia R. A Conserved α-Helical Motif Mediates the Interaction of Sp1-Like Transcriptional Repressors with the Corepressor mSin3A. Molecular And Cellular Biology 2001, 21: 5041-5049. PMID: 11438660, PMCID: PMC87230, DOI: 10.1128/mcb.21.15.5041-5049.2001.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsApoptosis Regulatory ProteinsBlotting, WesternCell Cycle ProteinsCell DivisionCHO CellsCircular DichroismCricetinaeGenetic VectorsGlutathione TransferaseLuciferasesMolecular Sequence DataMutationPeptide BiosynthesisPlasmidsPrecipitin TestsProtein BindingProtein BiosynthesisProtein Structure, TertiaryRecombinant Fusion ProteinsRepressor ProteinsSequence Homology, Amino AcidSin3 Histone Deacetylase and Corepressor ComplexSp1 Transcription FactorTranscription, GeneticTransforming Growth Factor betaZinc FingersConceptsSp1-like proteinsRepress transcriptionDeacetylase complexRepression motifTranscriptional repressionSin3 histone deacetylase complexBind GC-rich sequencesMechanism of transcriptional repressionSp1-like transcription factorsMSin3A-histone deacetylase complexGC-rich sequencesMammalian cell homeostasisCorepressor mSin3ARepression domainTranscriptional repressorA-helicesMSin3ATranscription factorsTIEG2Antiproliferative functionCell homeostasisMotifTranscriptionRepressionProteinMolecular mechanisms of transcriptional repression shared by the growth regulatory Sp1-like proteins and the tumor suppressor Mad1
Zhang J, Moncrieffe M, Kaczynski J, Prendergast F, Urrutia R. Molecular mechanisms of transcriptional repression shared by the growth regulatory Sp1-like proteins and the tumor suppressor Mad1. Gastroenterology 2001, 120: a139. DOI: 10.1016/s0016-5085(08)80685-3.Peer-Reviewed Original ResearchFour different Sp1-like proteins bind to the BTE box element present in the promoter of the carcinogen encoding enzyme P4501A1 gene
Conley A, Kaczynski J, Ellenrieder V, Urrutia R. Four different Sp1-like proteins bind to the BTE box element present in the promoter of the carcinogen encoding enzyme P4501A1 gene. Gastroenterology 2001, 120: a340. DOI: 10.1016/s0016-5085(08)81692-7.Peer-Reviewed Original ResearchMolecular mechanisms of transcriptional repression shared by the growth regulatory Sp1-like proteins and the tumor suppressor Mad1
ZHANG J, MONCRIEFFE M, KACZYNSKI J, PRENDERGAST F, URRUTIA R. Molecular mechanisms of transcriptional repression shared by the growth regulatory Sp1-like proteins and the tumor suppressor Mad1. Gastroenterology 2001, 120: a139-a139. DOI: 10.1016/s0016-5085(01)80685-5.Peer-Reviewed Original ResearchFour different Sp1-like proteins bind to the BTE box element present in the promoter of the carcinogen encoding enzyme P4501A1 gene
CONLEY A, KACZYNSKI J, ELLENRIEDER V, URRUTIA R. Four different Sp1-like proteins bind to the BTE box element present in the promoter of the carcinogen encoding enzyme P4501A1 gene. Gastroenterology 2001, 120: a340-a340. DOI: 10.1016/s0016-5085(01)81692-9.Peer-Reviewed Original Research