The human proteome contains approximately 20,000 proteins, and it is estimated that more
than 600 of them are functionally important for various types of cancers, including nearly 400 …

Ubiquitin E3 ligases control every aspect of eukaryotic biology by promoting protein
ubiquitination and degradation. At the end of a three-enzyme cascade, ubiquitin ligases …

Ubiquitylation had been considered limited to protein lysine residues, but other substrates
have recently emerged. Here, we show that DELTEX E3 ligases specifically target the 3 …

Covalent attachment (conjugation) of one or more ubiquitin molecules to protein substrates
governs numerous eukaryotic cellular processes, including apoptosis, cell division and …

Ubiquitin-like proteins (Ubl's) are conjugated to target proteins or lipids to regulate their
activity, stability, subcellular localization, or macromolecular interactions. Similar to ubiquitin …

Peroxisomes are ubiquitous organelles whose dysfunction causes fatal human diseases.
Most peroxisomal enzymes are imported from the cytosol by the receptor PEX5, which …

Ubiquitin-conjugating enzymes (E2s) are the central players in the trio of enzymes
responsible for the attachment of ubiquitin (Ub) to cellular proteins. Humans have∼ 40 E2s …

Eukaryotic cell biology depends on cullin–RING E3 ligase (CRL)-catalysed protein
ubiquitylation, which is tightly controlled by the modification of cullin with the ubiquitin-like …

Transcription-coupled DNA repair removes bulky DNA lesions from the genome, and
protects cells against ultraviolet (UV) irradiation. Transcription-coupled DNA repair begins …

Small-molecule degraders of disease-driving proteins offer a clinically proven modality with
enhanced therapeutic efficacy and potential to tackle previously undrugged targets. Stable …