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• W2113092034 abstract "We present an NMR-based antagonist induced dissociation assay (AIDA) for validation of inhibitor action on protein−protein interactions. As opposed to many standard NMR methods, AIDA directly validates the inhibitor potency in an in vitro NMR competition binding experiment. AIDA requires a large protein fragment (larger than 30 kDa) to bind to a small reporter protein (less than 20 kDa). We show here that a small fragment of a protein fused to glutathione S-transferase (GST) can effectively substitute the large protein component. We successfully used a GST-tagged N-terminal 73-residue p53 domain for binding studies with the human MDM2 protein. Other interactions we studied involved complexes of CDK2, cyclin A, p27, and the retinoblastoma protein. All these proteins play a key role in the cell division cycle, are associated with tumorigenesis, and are thus the subject of anticancer therapy strategies." @default.
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• W2113092034 date "2007-08-16" @default.
• W2113092034 modified "2023-10-17" @default.
• W2113092034 title "An NMR-Based Antagonist Induced Dissociation Assay for Targeting the Ligand−Protein and Protein−Protein Interactions in Competition Binding Experiments" @default.
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• W2113092034 doi "https://doi.org/10.1021/jm070365v" @default.
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