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Comment
. 2017 Apr 20;24(4):431-432.
doi: 10.1016/j.chembiol.2017.04.003.

ADP-Ribosylation Goes Normal: Serine as the Major Site of the Modification

Qiang Liu  1 , Bogdan I Florea  1 , Dmitri V Filippov  2
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Free article
Comment

ADP-Ribosylation Goes Normal: Serine as the Major Site of the Modification

Qiang Liu et al. Cell Chem Biol. .
Free article

Abstract

Proteins containing adenosine diphosphate ribosylserine as a posttranslational modification are widespread and formed via HPF1-assisted, PARP-1-mediated PARylation as Bonfiglio et al. (2017) report in a recent issue of Molecular Cell.

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  • Serine ADP-Ribosylation Depends on HPF1.
    Bonfiglio JJ, Fontana P, Zhang Q, Colby T, Gibbs-Seymour I, Atanassov I, Bartlett E, Zaja R, Ahel I, Matic I. Bonfiglio JJ, et al. Mol Cell. 2017 Mar 2;65(5):932-940.e6. doi: 10.1016/j.molcel.2017.01.003. Epub 2017 Feb 9. Mol Cell. 2017. PMID: 28190768 Free PMC article.

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