1. Volume 27, Issue 23, Pages R1256-R1258 (December 2017)
PARPs 
Anthony K.L. Leung 
Current Biology 
Volume 27, Issue 23, Pages R1256-R1258 (December 2017)
DOI: /j.cub
Copyright © 2017 Elsevier Ltd Terms and Conditions

2. Figure 1 Writers, erasers and readers of ADP-ribosylation.
Writers: PARP/ARTD nomenclature conversion table along with common names. Asterisks indicate those PARPs that have altered activities when partnered with other proteins. See text for more details. Erasers: Amino acids known to be ADP-ribosylated are outlined with a dashed border, where the amino acid specific eraser is indicated on the top right corner. Notably, the erasers for several ADP-ribosylated amino acids have yet to be identified and it is unclear whether other polar amino acids (e.g., Tyr and Gln) can be modified. A modified histidine called diphthamide (Dph) is known to be ADP-ribosylated (dotted border). Readers: ADP-ribose has two 2’ OH groups that allow conjugation to the 1’ position at the non-adenine ribose of another ADP-ribose. If adenine-linked ribose is joined to a non-adenine ribose, a linear polymer is formed. If two non-adenine riboses are linked together, a branch point is created. Shown are examples of different parts of protein-conjugated ADP-ribose that are recognized by specific protein domains.
Current Biology  , R1256-R1258DOI: ( /j.cub )
Copyright © 2017 Elsevier Ltd Terms and Conditions