ArticleChemistry & biology2010
A general chemical method to regulate protein stability in the mammalian central nervous system.
Article in Chemistry & biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 238 papers.
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Who cites it
238 citing papers in PubMed, 401 citations in OpenAlex.
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- Engineering Protein Stability with Small Molecules: A Review of the ecDHFR Destabilizing Domain System.ACS chemical biology · 2026Review
- Systematic discovery of UFM1 receptors reveals a regulatory module in DNA repair directing non-homologous end-joining.Nature communications · 2026Article
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- BACH2 regulates T cell lineage state to enhance CAR T cell function.Nature immunology · 2026Article
- Target-stabilized base editors enable robust high-fidelity RNA editing.Nature communications · 2026Article
- High-throughput mapping of modular regulatory domains in human RNA-binding proteins.Cell systems · 2026Article
- A programmable genetic platform for engineering noninvasive biosensors.Science advances · 2026Article
- Ribosome-associated quality control of aberrant protein production during amino acid limitation.bioRxiv : the preprint server for biology · 2026Article
- Engineering IL-21 secretion in T cells using druggable ligand-responsive stabilized domains.Scientific reports · 2025Article
- A chemically inducible, leakless Cre recombinase by split-protein-based efficient and enhanced degradation (SPEED).Communications biology · 2025Article
- Chemically-inducible CRISPR/Cas9 circuits for ultra-high dynamic range gene perturbation.Nature communications · 2025Article
- Systematic characterization of existing and novel inducible transgenic systems in human pluripotent stem cells after prolonged differentiation.bioRxiv : the preprint server for biology · 2025Article
178 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The ability to make specific perturbations to biological molecules in a cell or organism is a central experimental strategy in modern research biology. We have developed a general technique in which the stability of a specific protein is regulated by a cell-permeable small molecule. Mutants of the Escherichia coli dihydrofolate reductase (ecDHFR) were engineered to be degraded, and, when this destabilizing domain is fused to a protein of interest, its instability is conferred to the fused protein resulting in rapid degradation of the entire fusion protein. A small-molecule ligand trimethoprim (TMP) stabilizes the destabilizing domain in a rapid, reversible, and dose-dependent manner, and protein levels in the absence of TMP are barely detectable. The ability of TMP to cross the blood-brain barrier enables the tunable regulation of proteins expressed in the mammalian central nervous system.
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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.