A rapid, reversible, and tunable method to regulate protein function in living cells using synthetic small molecules.

By Laura A. Banaszynski, Ling-chun Chen, Lystranne A. Maynard-Smith, A. G. L. Ooi, T. Wandless. Cell, 2006

887 citations recorded by the source corpus.

Subfields: Molecular Biology, Organic Chemistry

View Paper: https://www.semanticscholar.org/paper/f6ae4e259d3cbb8ac6c0b071d5f8fdb0e28706ee

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. J. Campisi
2. Masato T. Kanemaki
3. F. Rodier
4. Kai Johnsson
5. B. Sankaran
6. M. J. Bick
7. Per Greisen
8. David Baker

In Organic Chemistry

1. David Baker
2. Jon Clardy
3. Frances H. Arnold

Citations in the corpus

• Single-cell dynamics of genome-nuclear lamina interactions. (2013, background): “Inducible Dam-Lamin B1 expression was established by the fusion of a destabilization domain (DD) (Banaszynski et al., 2006), which causes DamLamin B1 to be rapidly targeted for proteosomal degradation unless the protein is shielded by the synthetic small molecule Shield1.”
• Target identification using drug affinity responsive target stability (DARTS) (2009, background): “For instance, whereas unstable FRB domain and FKBP12 mutants are stabilized by the presence of ligands (6, 51) and topoisomerase-1 is destabilized by camptothecin (47), binding of estrogen receptor ligands each affects receptor stability differently (53).”
• An auxin-based degron system for the rapid depletion of proteins in nonplant cells (2009, methodology): “Another method involves fusion with the destabilizing domain derived from FKBP12 (ddFKBP”
• A Versatile Viral System for Expression and Depletion of Proteins in Mammalian Cells (2009, methodology): “Therefore, we tested whether we could provide faster temporal control using FKBP destabilization domain fusion proteins, because this degradation can be reversibly and rapidly halted by addition of the protective ligand termed Shld1 to the extracellular media [29,30].”
• Computational design of environmental sensors for the potent opioid fentanyl (2017, methodology): “To this end, we incorporated our fentanyl binders into a transcription factor (TF)-based biosensor system, which couples ligand binding to transcription activation by stabilizing the protein against degradation (Banaszynski et al., 2006; Feng et al., 2015).”