Dianke Li

Abstract E3 ubiquitin ligases recognize substrates through specific interfaces. Accurate delineation of these interfaces is essential, as mutations disrupting them impair protein ubiquitination and drive cancer progression. However, available E3–substrate interface data are sparse and systematic prediction methods remain lacking.

Abstract Protein ubiquitination regulates a wide range of cellular processes. The degree of protein ubiquitination is determined by the delicate balance between ubiquitin ligase (E3)-mediated ubiquitination and deubiquitinase (DUB)-mediated deubiquitination. In comparison to the E3-substrate interactions, the DUB-substrate interactions (DSIs) remain insufficiently investigated.

Patient cohorts Treatment-naïve patients with resectable NSCLC with EGFR/ALK mutation negative were enrolled in this study from September 2019 to May 2021 in our center. The patients received 2–4 cycles (3 weeks per cycle) of neoadjuvant therapy (PD-1 antibody + platinum-based chemotherapy), and then underwent surgery.