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Because it is unlikely that Glu would be modified by 4-OXO-DHA, our results support that 4-OXO-DHA (an electrophilic Michael acceptor) can covalently bind to the peptide containing the sequence of the active site of NF-B p50 protein to form a covalent linkage with the nucleophilic Cysteine-S 62 residue (marked in bold and italic in Table 1)
RAS-RAF-MEK-dependent oxidative cell death involving voltage-dependent anion channels
Research consistently demonstrates that the apo-peptide alone does not replicate the full signaling profile of the copper-bound complex
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