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- W4213080212 endingPage "402" @default.
- W4213080212 startingPage "391" @default.
- W4213080212 abstract "Ubiquitination is a key regulatory mechanism vital for maintenance of cellular homeostasis. Protein degradation is induced by E3 ligases via attachment of ubiquitin chains to substrates. Pharmacological exploitation of this phenomenon via targeted protein degradation (TPD) can be achieved with molecular glues or bifunctional molecules facilitating the formation of ternary complexes between an E3 ligase and a given protein of interest (POI), resulting in ubiquitination of the substrate and subsequent proteolysis by the proteasome. Recently, the development of novel covalent fragment screening approaches has enabled the identification of first-in-class ligands for E3 ligases and deubiquitinases revealing so far unexplored binding sites which highlights the potential of these methods to uncover and expand druggable space for new target classes." @default.
- W4213080212 created "2022-02-24" @default.
- W4213080212 creator A5075280201 @default.
- W4213080212 creator A5078336595 @default.
- W4213080212 creator A5086766171 @default.
- W4213080212 date "2022-02-23" @default.
- W4213080212 modified "2023-09-26" @default.
- W4213080212 title "Covalent fragment-based ligand screening approaches for identification of novel ubiquitin proteasome system modulators" @default.
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