text: Hydrophobic tag degraders contain a binding domain in addition to a linker-separated hydrophobic moiety, such as adamantyl, to induce protein degradation. As exposed hydrophobicity is characteristic of protein misfolding, the native cell proteasome may recognize and degrade proteins tagged with the hydrophobic moiety. Taavi Neklesa and Craig Crews first reported hydrophobic tag degradation in 2011 as a tool to probe protein function in conjunction with cognate HaloTag fusion proteins. This principle has also been further used to effectively degrade transcription factors (a traditionally difficult class to drug) and cancer-linked EZH2 in in vitro models. As of yet, no drug candidates have been publicly identified making use of this technology.