Publications by authors named "Edmee Vandenboorn"
Article Synopsis
- The study investigates the interaction between the transcription factor PPARα and the orphan nuclear receptor ERRα, highlighting its dependence on specific ligands and potential physiological significance.
- Various assays confirmed that ERRα functions as a transcriptional repressor of PPARα target genes, implying a complex relationship between these two receptors.
- The research utilized mutagenesis and transactivation studies to characterize the interaction and suggested that ERRα influences PPARα activity through coregulators, especially under conditions like serum deprivation.
The stabilization of protein-protein interactions (PPIs) has emerged as a promising strategy in chemical biology and drug discovery. The identification of suitable starting points for stabilizing native PPIs and their subsequent elaboration into selective and potent molecular glues lacks structure-guided optimization strategies. We have previously identified a disulfide fragment that stabilized the hub protein 14-3-3σ bound to several of its clients, including ERα and C-RAF.
View Article and Find Full Text PDFSmall-molecule stabilization of protein-protein interactions (PPIs) is a promising strategy in chemical biology and drug discovery. However, the systematic discovery of PPI stabilizers remains a largely unmet challenge. Herein we report a fragment-linking approach targeting the interface of 14-3-3 and a peptide derived from the estrogen receptor alpha (ERα) protein.
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