ArticleCell chemical biology2020
Inducible Degradation of Target Proteins through a Tractable Affinity-Directed Protein Missile System.
Article in Cell chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 70 citations in OpenAlex.
- Reductive Methylation: An Alternative to Lysine → Arginine Mutagenesis.Journal of peptide science : an official publication of the European Peptide Society · 2026Article
- The benchmarking and application of tag-degraders in vivo to validate therapeutic targets.Nature communications · 2026Article
- Development of PolyHis-Targeting PROTAC Degraders.Angewandte Chemie (International ed. in English) · 2026Article
- Specific proteolysis mediated by a p97-directed proteolysis-targeting chimera (p97-PROTAC).eLife · 2025Article
- Orthogonal IMiD-Degron Pairs Induce Selective Protein Degradation in Cells.ACS chemical biology · 2025Article
- Targeted degradation of the HPV oncoprotein E6 reduces tumor burden in cervical cancer.Molecular therapy : the journal of the American Society of Gene Therapy · 2025Article
- Review
- Article
- De novo design of peptide binders to conformationally diverse targets with contrastive language modeling.Science advances · 2025Article
- Advances and Challenges in RAS Signaling Targeted Therapy in Leukemia.Molecular cancer therapeutics · 2025Review
- Methylarginine targeting chimeras for lysosomal degradation of intracellular proteins.Nature chemical biology · 2024Article
- Article
- Lipid-mediated intracellular delivery of recombinant bioPROTACs for the rapid degradation of undruggable proteins.Nature communications · 2024Article
- A pan-KRAS degrader for the treatment of KRAS-mutant cancers.Cell discovery · 2024Article
- Degron tagging for rapid protein degradation in mice.Disease models & mechanisms · 2024Article
- Orthogonal IMiD-Degron Pairs Induce Selective Protein Degradation in Cells.bioRxiv : the preprint server for biology · 2024Article
- Subunits of an E3 Ligase Complex as Degrons for Efficient Degradation of Cytosolic, Nuclear, and Membrane Proteins.ACS synthetic biology · 2024Article
- Review
- Opportunities and challenges of protein-based targeted protein degradation.Chemical science · 2023Review
- Exploring switch II pocket conformation of KRAS(G12D) with mutant-selective monobody inhibitors.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
The affinity-directed protein missile (AdPROM) system utilizes specific polypeptide binders of intracellular proteins of interest (POIs) conjugated to an E3 ubiquitin ligase moiety to enable targeted proteolysis of the POI. However, a chemically tuneable AdPROM system is more desirable. Here, we use Halo-tag/VHL-recruiting proteolysis-targeting chimera (HaloPROTAC) technology to develop a ligand-inducible AdPROM (L-AdPROM) system. When we express an L-AdPROM construct consisting of an anti-GFP nanobody conjugated to the Halo-tag, we achieve robust degradation of GFP-tagged POIs only upon treatment of cells with the HaloPROTAC. For GFP-tagged POIs, ULK1, FAM83D, and SGK3 were knocked in with a GFP-tag using CRISPR/Cas9. By substituting the anti-GFP nanobody for a monobody that binds H- and K-RAS, we achieve robust degradation of unmodified endogenous RAS proteins only in the presence of the HaloPROTAC. Through substitution of the polypeptide binder, the highly versatile L-AdPROM system is useful for the inducible degradation of potentially any intracellular POI.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.