GPX4 and pancreatic neoplasm: Cu2+ could directly bind to the C107/148 cysteine residues of GPX4, leading to subsequent ubiquitination and aggregation of GPX4, which was then accepted by the autophagic receptor Tax1 binding protein 1 (TAX1BP1) and degraded in the autophagosome.[129] The copper‐dependent degradation of GPX4 elicited ferroptosis in pancreatic cancer cells, a process that could be alleviated by the copper chelator tetrathiomolybdate or ferroptosis inhibitors ferrostatin‐1/liproxstatin‐1, yet not by other types of cell death inhibitors.