Molecular proximity orchestrates biological function, and blocking existing proximities is an
established therapeutic strategy. By contrast, strengthening or creating neoproximity with …

Targeted protein degradation refers to the use of small molecules to induce the selective
degradation of proteins. In its most common form, this degradation is achieved through …

Only around 20% of the human proteome is considered to be druggable with small-molecule
antagonists. This leaves some of the most compelling therapeutic targets outside the reach …

Targeted protein degradation (TPD) is an emerging modality for research and therapeutics.
Most TPD approaches harness cellular ubiquitin-dependent proteolytic pathways …

The field of targeted protein degradation (TPD) is a rapidly developing therapeutic modality
with the promise to tame disease-relevant proteins in ways that are difficult or impossible to …

Ubiquitin ligation is typically executed by hallmark E3 catalytic domains. Two such
domains,'cullin–RING'and 'RBR', are individually found in several hundred human E3 …

Protein ubiquitylation controls diverse processes within eukaryotic cells, including protein
degradation, and is often dysregulated in disease. Moreover, small-molecule degraders that …

Cullin-RING ligases (CRLs) ubiquitylate specific substrates selected from other cellular
proteins. Substrate discrimination and ubiquitin transferase activity were thought to be strictly …

Molecular glue (MG) degraders are monovalent small molecule compounds that co-opt E3
ubiquitin ligases to target neo-substrates for proteasomal degradation. Here, we provide a …

The field of induced proximity therapeutics is in its ascendancy but is limited by a lack of
scalable tools to systematically explore effector-target protein pairs in an unbiased manner …