2011
Differential Recruitment of Methyl CpG‐Binding Domain Factors and DNA Methyltransferases by the Orphan Receptor Germ Cell Nuclear Factor Initiates the Repression and Silencing of Oct4
Gu P, Xu X, Le Menuet D, Chung A, Cooney AJ. Differential Recruitment of Methyl CpG‐Binding Domain Factors and DNA Methyltransferases by the Orphan Receptor Germ Cell Nuclear Factor Initiates the Repression and Silencing of Oct4. Stem Cells 2011, 29: 1041-1051. PMID: 21608077, PMCID: PMC3468724, DOI: 10.1002/stem.652.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell DifferentiationCell Line, TumorCpG IslandsDNA (Cytosine-5-)-MethyltransferasesDNA MethylationDNA Methyltransferase 3ADNA-Binding ProteinsEmbryonic Stem CellsGene Expression Regulation, DevelopmentalGene Knockdown TechniquesMiceMolecular Sequence DataNuclear Receptor Subfamily 6, Group A, Member 1Octamer Transcription Factor-3Promoter Regions, GeneticProtein BindingTranscription FactorsConceptsGerm cell nuclear factorEmbryonic stem cellsOct4 promoterDNA methylationDNA methyltransferasesRepressive functionEpigenetic modificationsTranscription factorsProximal promoterDifferentiation of ESCsWild-type embryonic stem cellsDe novo DnmtsGene-specific repressionKey transcription factorDifferential recruitmentNuclear factorGCNF bindsESC differentiationPluripotency genesOct4 geneSomatic cellsMethyl-CpGCis elementsMBD3Gene expression
2005
Evolutionary Trace-based Peptides Identify a Novel Asymmetric Interaction That Mediates Oligomerization in Nuclear Receptors*
Gu P, Morgan DH, Sattar M, Xu X, Wagner R, Raviscioni M, Lichtarge O, Cooney AJ. Evolutionary Trace-based Peptides Identify a Novel Asymmetric Interaction That Mediates Oligomerization in Nuclear Receptors*. Journal Of Biological Chemistry 2005, 280: 31818-31829. PMID: 15994320, DOI: 10.1074/jbc.m501924200.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Vesicular TransportAmino Acid SequenceCell LineDimerizationDNA-Binding ProteinsEvolution, MolecularGenes, ReporterMolecular Sequence DataNuclear Receptor Subfamily 6, Group A, Member 1PeptidesPoint MutationProtein Structure, SecondaryProtein Structure, TertiaryReceptor Cross-TalkReceptors, Cytoplasmic and NuclearReceptors, Retinoic AcidResponse ElementsConceptsGerm cell nuclear factorEvolutionary trace analysisNuclear receptorsKey functional sitesOrphan nuclear receptorDR0 elementsGCNF bindsComplex formationEssential genesEvolutionary traceMolecular basisOligomerization propertiesHelix 3Heterotypic interactionsTargeted mutationsLarge complexesNovel helixFunctional sitesHelix 11HomodimerNuclear factorDimerizationOligomerizationHelixMutations