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79, Supplementary Table 1 and 2, and Supplementary Data 1) demonstrate that rearrangement of surrounding residues could allow BV to bind with Ab Pcob in certain conformations, where hydrophobic interactions with residues in the binding pocket (e.g., Leu252, Trp289, Leu294, Arg297, Val299 and Val303) contribute to retain BV in the correct orientation (Fig

An allergic reaction is more likely to occur from exposure to sulfa-containing antibiotics

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Whether GSH-dependent copper trafficking and Fe-S cluster maintenance actively license ferroptosis or cuproptosis, rather than simply buffering stress, remains unclear

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Antioxidants (Basel, Switzerland), 10(9), 1352