Ubiquitination, an important type of protein posttranslational modification (PTM), plays a
crucial role in controlling substrate degradation and subsequently mediates the “quantity” …

Ubiquitination is an essential regulator of most, if not all, signalling pathways, and defects in
cellular signalling are central to cancer initiation, progression and, eventually, metastasis …

Many diseases are driven by proteins that are aberrantly ubiquitinated and degraded. These
diseases would be therapeutically benefited by targeted protein stabilization (TPS). Here we …

The deubiquitylating enzymes (DUBs, also known as deubiquitylases or deubiquitinases)
maintain the dynamic state of the cellular ubiquitome by releasing conjugated ubiquitin from …

Tumor suppressor genes cooperate with each other in tumors. Three important tumor
suppressor proteins, retinoblastoma (Rb), p53, phosphatase, and tensin homolog deleted …

Protein ubiquitination is one of the most powerful posttranslational modifications of proteins,
as it regulates a plethora of cellular processes in distinct manners. Simple …

Although cell-cycle arrest, senescence, and apoptosis are established mechanisms of tumor
suppression, accumulating evidence reveals that ferroptosis, an iron-dependent …

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 …

The removal of misfolded, ubiquitinated proteins is an essential part of the protein quality
control. The ubiquitin‐proteasome system (UPS) and autophagy are two interconnected …

Upregulation of programmed death ligand 1 (PD-L1) helps tumor cells escape from immune
surveillance, and therapeutic antibodies targeting PD-1/PD-L1 have shown better patient …