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Population Limitations: As noted previously, the trials did not include elderly individuals, pregnant women, children, or those with certain medical conditions
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The main obstacle is the high structural conservation of the FAD-binding domain, ERO1 inhibitors also recognize other FAD-dependent enzymes like lysine-specific demethylase 1 (LSD-1) and MAO-A/B ( Bisphenol A, an endocrine disruptor, has been shown to significantly inhibit ERO1-PDI-mediated disulfide bond formation by obstructing the substrate-binding pocket in the b' domain of PDI and the phenol groups of Bisphenol A compete for a highly conserved tryptophan residue within the protruding -hairpin of ERO1 ( A high-throughput in vitro assay revealed that EN460 (IC 50 = 1.9 M) selectivity inhibited ERO1 activity in vivo as well as in vitro by forming an adduct with the thiol group of ERO1, resulting in the release of the FAD prosthetic group
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