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The deglutamylation activities of AsGGT1, AsGGT2, and AsGGT3 toward -glutamyl- S -allyl-L-cysteine were elevated in the presence of the dipeptide glycylglycine as a -glutamyl acceptor substrate, although these proteins can act as hydrolases in the absence of a proper acceptor substrate, except water
Cut-offs for significance were set to an adjusted p -value of 0.05, and a log2 fold change of 1, with significance subject to BenjaminiHochberg FDR correction
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This is the highest-consistency window, driving GHK-Cu exposure while BPC-157, TB-500, and KPV support blood flow, migration, and inflammation control
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