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A TRIM21-based method for targeted protein degradation.
Acta Biochim Biophys Sin (Shanghai)
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State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai 200031, China.
Redirecting the specificity of tripartite motif containing-21 scaffolds using a novel discovery and design approach.
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Department of Chemical and Biomolecular Engineering, Johns Hopkins University, Baltimore, Maryland, USA; Translational Tissue Engineering Center, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA; Bloomberg∼Kimmel Institute for Cancer Immunotherapy, Johns Hopkins University, Baltimore, Maryland, USA; Sidney Kimmel Comprehensive Cancer Center, Johns Hopkins University, Baltimore, Maryland, USA; Department of Biomedical Engineering, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA; Department of Oncology, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA; Department of Ophthalmology, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA. Electronic address:
Hijacking the ubiquitin proteasome system to elicit targeted protein degradation (TPD) has emerged as a promising therapeutic strategy to target and destroy intracellular proteins at the post-translational level. Small molecule-based TPD approaches, such as proteolysis-targeting chimeras (PROTACs) and molecular glues, have shown potential, with several agents currently in clinical trials. Biological PROTACs (bioPROTACs), which are engineered fusion proteins comprised of a target-binding domain and an E3 ubiquitin ligase, have emerged as a complementary approach for TPD.
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