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. Author manuscript; available in PMC: 2022 Aug 20.
Published in final edited form as: Free Radic Biol Med. 2021 Jul 2;172:562–577. doi: 10.1016/j.freeradbiomed.2021.07.002

Fig. 2.

Fig. 2.

S-Nitrosylation of PDI impairs its chaperone and disulfide isomerase activity that modulates protein folding. When an excessive amount of NO is present under pathological conditions, PDI is S-nitrosylated at its active site cysteines, thus inhibiting its protein folding and chaperone activity, resulting in accumulation of misfolded proteins with increased cell damage and death.