Targeted protein degradation: from mechanisms to clinic
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Springer Science and Business Media LLC
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https://www.nature.com/articles/s41580-024-00729-9.pdf
Reference215 articles.
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2. Zhao, L., Zhao, J., Zhong, K., Tong, A. & Jia, D. Targeted protein degradation: mechanisms, strategies and application. Signal Transduct. Target. Ther. 7, 113 (2022).
3. Chamberlain, P. P. et al. Structure of the human cereblon-DDB1-lenalidomide complex reveals basis for responsiveness to thalidomide analogs. Nat. Struct. Mol. Biol. 21, 803–809 (2014). This study shows the crystal structure of cereblon bound to lenalidomide, revealing the binding site and of IMiD drugs.
4. Fischer, E. S. et al. Structure of the DDB1-CRBN E3 ubiquitin ligase in complex with thalidomide. Nature 512, 49–53 (2014). This study shows that the crystal structure of cereblon bound to thalidomide, lenalidomide and pomalidomide reveals the binding site of IMiD drugs and provides rationale for their activity.
5. Banik, S. M. et al. Lysosome-targeting chimaeras for degradation of extracellular proteins. Nature 584, 291–297 (2020). This paper provides the first, to our knowledge, description of the LYTAC system and the first example of its use for the degradation of extracellular proteins.
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