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FSEN1 was identified as a small-molecule inhibitor of FSP1 through chemical screening 118 , and subsequent structural analyses revealed that FSEN1 occupies the substrate-binding pocket of FSP1 in a position analogous to CoQ observed in the enzyme active site, providing structural insight into inhibitor recognition 119

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For instance, in mouse embryonic stem cells, targeted disruption of glucose-6-phosphate dehydrogenase, which is the rate-limiting enzyme in the pentose phosphate pathway, the predominant metabolic pathway for the generation of NADPH (a cofactor of GR), renders cells extremely sensitive to H 2 O 2 -induced cell death 34

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