Author: Collin D. Heer; Daniel J. Sanderson; Yousef M.O. Alhammad; Mark S. Schmidt; Samuel A.J. Trammell; Stanley Perlman; Michael S. Cohen; Anthony R. Fehr; Charles Brenner
Title: Coronavirus Infection and PARP Expression Dysregulate the NAD Metabolome: A Potentially Actionable Component of Innate Immunity Document date: 2020_4_18
ID: 033phqmd_3
Snippet: PARPs have an absolute requirement for NAD + (Cohen, 2020; Gupte, Liu, & Kraus, 2017) . However, rather than using NAD + as an electron acceptor, PARPs consume NAD + in order to transfer the ADP-ribose moiety to protein side chains . CC-BY-ND 4.0 International license author/funder. It is made available under a The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.04.17.047480 doi: bioRxiv prep.....
Document: PARPs have an absolute requirement for NAD + (Cohen, 2020; Gupte, Liu, & Kraus, 2017) . However, rather than using NAD + as an electron acceptor, PARPs consume NAD + in order to transfer the ADP-ribose moiety to protein side chains . CC-BY-ND 4.0 International license author/funder. It is made available under a The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.04.17.047480 doi: bioRxiv preprint (Belenky et al., 2007) . The best-known members of the PARP superfamily, PARP1 and PARP2, form polymers of ADP-ribose, largely in response to DNA damage.
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