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Structures and Mechanisms of Enzymes Employed in the Synthesis and Degradation of PARP-Dependent Protein ADP-Ribosylation.

Authors: Barkauskaite, E  Jankevicius, G  Ahel, I 
Citation: Barkauskaite E, etal., Mol Cell. 2015 Jun 18;58(6):935-46. doi: 10.1016/j.molcel.2015.05.007.
Pubmed: (View Article at PubMed) PMID:26091342
DOI: Full-text: DOI:10.1016/j.molcel.2015.05.007

The poly(ADP-ribose) polymerases (PARPs) are a major family of enzymes capable of modifying proteins by ADP-ribosylation. Due to the large size and diversity of this family, PARPs affect almost every aspect of cellular life and have fundamental roles in DNA repair, transcription, heat shock and cytoplasmic stress responses, cell division, protein degradation, and much more. In the past decade, our understanding of the PARP enzymatic mechanism and activation, as well as regulation of ADP-ribosylation signals by the readers and erasers of protein ADP-ribosylation, has been significantly advanced by the emergence of new structural data, reviewed herein, which allow for better understanding of the biological roles of this widespread post-translational modification.


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RGD Object Information
RGD ID: 11100038
Created: 2016-06-14
Species: All species
Last Modified: 2016-06-14
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.