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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.

Original publication

DOI

10.1016/j.molcel.2015.05.007

Type

Journal article

Journal

Mol Cell

Publication Date

18/06/2015

Volume

58

Pages

935 - 946

Keywords

Catalytic Domain, Glycoside Hydrolases, Humans, Models, Molecular, Molecular Structure, Poly Adenosine Diphosphate Ribose, Poly(ADP-ribose) Polymerases, Protein Binding, Protein Structure, Tertiary, Thiolester Hydrolases