2013
Single strand DNA binding proteins 1 and 2 protect newly replicated telomeres
Gu P, Deng W, Lei M, Chang S. Single strand DNA binding proteins 1 and 2 protect newly replicated telomeres. Cell Research 2013, 23: 705-719. PMID: 23459151, PMCID: PMC3641597, DOI: 10.1038/cr.2013.31.Peer-Reviewed Original ResearchMeSH KeywordsAllelesAnimalsCell LineChromatidsDNA DamageDNA RepairDNA, Single-StrandedDNA-Binding ProteinsGenomic InstabilityHumansMiceMice, KnockoutMitochondrial ProteinsProtein BindingRadiation, IonizingRNA InterferenceRNA, Small InterferingShelterin ComplexTelomereTelomere-Binding ProteinsTelomeric Repeat Binding Protein 2ConceptsGenome stabilitySingle-strand DNAHeterotrimeric protein complexDNA damage responseTelomere end protectionProtein 1Subset of telomeresTelomeric ssDNAProtein complexesTelomeric DNADamage responseG-overhangsEnd protectionConditional knockout miceTelomeresΔ miceDNAPOT1aDevelopmental abnormalitiesStrand DNACritical roleKnockout miceINTS3F allelePOT1b
2005
Orphan Nuclear Receptor GCNF Is Required for the Repression of Pluripotency Genes during Retinoic Acid-Induced Embryonic Stem Cell Differentiation
Gu P, LeMenuet D, Chung A, Mancini M, Wheeler DA, Cooney AJ. Orphan Nuclear Receptor GCNF Is Required for the Repression of Pluripotency Genes during Retinoic Acid-Induced Embryonic Stem Cell Differentiation. Molecular And Cellular Biology 2005, 25: 8507-8519. PMID: 16166633, PMCID: PMC1265758, DOI: 10.1128/mcb.25.19.8507-8519.2005.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, NorthernBlotting, WesternCell DifferentiationCell LineCell NucleusChromatin ImmunoprecipitationDNA-Binding ProteinsDown-RegulationEmbryo, MammalianFemaleFibroblast Growth Factor 4GenotypeHomeodomain ProteinsIn Situ HybridizationMaleMiceMice, TransgenicMicroscopy, FluorescenceModels, GeneticNanog Homeobox ProteinNuclear Receptor Subfamily 6, Group A, Member 1Octamer Transcription Factor-3PhenotypePlasmidsProtein BindingReceptors, Cytoplasmic and NuclearResponse ElementsReverse Transcriptase Polymerase Chain ReactionSignal TransductionSOXB1 Transcription FactorsStem CellsTime FactorsTrans-ActivatorsTransfectionTretinoinConceptsLoss of repressionES cell differentiationPluripotency genesCell differentiationTranscription factorsEmbryonic developmentES cellsEmbryonic stem cell pluripotencyEmbryonic stem cell differentiationEarly mouse embryonic developmentStem cell pluripotencyMouse embryonic developmentPluripotency gene expressionEarly embryonic developmentInitiation of differentiationStem cell differentiationRetinoic acidCell pluripotencyNanog geneGenes Oct4Somatic cellsUndifferentiated stateGene expressionGCNFRepressionEvolutionary 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