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Funding This work was supported by the National Natural Science Foundation of China (No.81871185), Chongqing Municipal Education Commission (KJZD-K202100407), Chongqing Science & Technology Commission (cstc2021jcyj-msxmX0213), Kuanren Talents Programs of the Second Affiliated Hospital of Chongqing Medical University

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Consequently, the accumulated NAPQI binds covalently to the cysteine, methionine, tyrosine, and tryptophan residues of various proteins, forming NAPQI-protein adducts within the cell that disrupt normal physiological protein functions