NAD+ [1000mg]

Research over the past two decades has established NAD+ as the obligate co-substrate for three distinct enzyme superfamilies: sirtuins (SIRT1–7, NAD+-dependent protein deacylases), poly(ADP-ribose) polymerases (PARPs, DNA damage sensors), and cyclic ADP-ribose synthases (CD38, CD157). Work from David Sinclair's laboratory at Harvard Medical School and Johan Auwerx's group at EPFL has focused on the consequences of age-related NAD+ depletion for mitochondrial biogenesis, electron transport chain function, and genomic stability in rodent models. Charles Brenner at the University of Iowa characterized the nicotinamide riboside (NR) and NMN salvage biosynthesis pathways as routes to replenish cellular NAD+ pools. All findings referenced here derive from preclinical or early-phase research models and have not been validated in controlled human clinical trials.