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- W3033081520 abstract "Stabilization of protein–protein interactions (PPIs) holds great potential for therapeutic agents, as illustrated by the successful drugs rapamycin and lenalidomide. However, how such interface-binding molecules can be created in a rational, bottom-up manner is a largely unanswered question. We report here how a fragment-based approach can be used to identify chemical starting points for the development of small-molecule stabilizers that differentiate between two different PPI interfaces of the adapter protein 14-3-3. The fragments discriminately bind to the interface of 14-3-3 with the recognition motif of either the tumor suppressor protein p53 or the oncogenic transcription factor TAZ. This X-ray crystallography driven study shows that the rim of the interface of individual 14-3-3 complexes can be targeted in a differential manner with fragments that represent promising starting points for the development of specific 14-3-3 PPI stabilizers." @default.
- W3033081520 created "2020-06-12" @default.
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- W3033081520 date "2020-06-05" @default.
- W3033081520 modified "2023-10-12" @default.
- W3033081520 title "Fragment-based Differential Targeting of PPI Stabilizer Interfaces" @default.
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- W3033081520 doi "https://doi.org/10.1021/acs.jmedchem.9b01942" @default.
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