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Copper normally travels bound to proteins like ceruloplasmin, but GHKs tripeptide chain has a particularly high affinity for copper (II) ions, forming a stable chelate complex that can shuttle copper efficiently into cells
Proteins undergo removal of the S-nitrosylation via the action of denitrosylases
Inhibiting the enzyme is therefore investigated as a route to preserving both methyl donor pools and NAD+ availability, with downstream effects on sirtuin-dependent signaling
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