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Poly(ADP-ribose) polymerase family member 11 (PARP11) is an enzyme belonging to the poly(ADP-ribose) polymerase family, which is involved in post-translational modification of proteins through mono-ADP-ribosylation using NAD+ as a substrate[1][4][5]. PARP11 is localized in the nuclear envelope, cytosol, and nuclear bodies, and plays a key role in nuclear envelope stability as well as nuclear remodeling during sperm development[1]. It can modulate the immune response by inhibiting type I interferon signaling, specifically through mono-ADP-ribosylation of beta-TrCP/BTRC to promote ubiquitination and protect from proteasomal degradation[1]. Additionally, PARP11 acts as an antiviral factor, in part through cooperation with PARP12, to degrade Zika virus proteins and inhibit viral replication, independent of interferon signaling or its own enzymatic activity[1]. While other members of the PARP family, particularly PARP1/2, are established therapeutic targets in cancer, PARP11 is an emerging molecular target with roles in host-pathogen interactions and immune signaling, though no approved drugs currently act specifically on this enzyme[1][3].
Not established for any clinical drug; for other PARP family members, inhibitors prevent ADP-ribosylation, typically by competing at the NAD+ binding site
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