Matches in Nanopublications for { ?s ?p "treating HepG2 cells with OM specifically leads to prominent increases of the levels of c/EBPbeta and Egr1 bound to the LDLR promoter in vivo the N-terminal transactivation domain of Egr1 specifically interacts with c/EBPbeta The OM treatment further enhances this interaction, resulting in a large increase in the Egr1 transactivating activity Egr1 regulates LDLR transcription via a novel mechanism of protein-protein interaction with c/EBPbeta." ?g. }
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- _7 value "treating HepG2 cells with OM specifically leads to prominent increases of the levels of c/EBPbeta and Egr1 bound to the LDLR promoter in vivo the N-terminal transactivation domain of Egr1 specifically interacts with c/EBPbeta The OM treatment further enhances this interaction, resulting in a large increase in the Egr1 transactivating activity Egr1 regulates LDLR transcription via a novel mechanism of protein-protein interaction with c/EBPbeta." provenance.
- _6 value "treating HepG2 cells with OM specifically leads to prominent increases of the levels of c/EBPbeta and Egr1 bound to the LDLR promoter in vivo the N-terminal transactivation domain of Egr1 specifically interacts with c/EBPbeta The OM treatment further enhances this interaction, resulting in a large increase in the Egr1 transactivating activity Egr1 regulates LDLR transcription via a novel mechanism of protein-protein interaction with c/EBPbeta." provenance.
- _7 value "treating HepG2 cells with OM specifically leads to prominent increases of the levels of c/EBPbeta and Egr1 bound to the LDLR promoter in vivo the N-terminal transactivation domain of Egr1 specifically interacts with c/EBPbeta The OM treatment further enhances this interaction, resulting in a large increase in the Egr1 transactivating activity Egr1 regulates LDLR transcription via a novel mechanism of protein-protein interaction with c/EBPbeta." provenance.
- _6 value "treating HepG2 cells with OM specifically leads to prominent increases of the levels of c/EBPbeta and Egr1 bound to the LDLR promoter in vivo the N-terminal transactivation domain of Egr1 specifically interacts with c/EBPbeta The OM treatment further enhances this interaction, resulting in a large increase in the Egr1 transactivating activity Egr1 regulates LDLR transcription via a novel mechanism of protein-protein interaction with c/EBPbeta." provenance.