You are seeing a free-to-access but limited selection of the activity Altmetric has collected about this research output.
Click here to find out more.
| Chapter title |
Hydrolysis of ADP-Ribosylation by Macrodomains
|
|---|---|
| Chapter number | 14 |
| Book title |
ADP-ribosylation and NAD+ Utilizing Enzymes
|
| Published in |
Methods in molecular biology, August 2018
|
| DOI | 10.1007/978-1-4939-8588-3_14 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-8587-6, 978-1-4939-8588-3
|
| Authors |
Melanija Posavec Marjanovic´, Gytis Jankevicius, Ivan Ahel, Posavec Marjanovic´, Melanija, Jankevicius, Gytis, Ahel, Ivan |
| Abstract |
ADP-ribosylation is the process of transferring the ADP-ribose moiety from NAD+ to a substrate. While a number of proteins represent well described substrates accepting ADP-ribose modification, a recent report demonstrated biological role for DNA ADP-ribosylation as well. The conserved macrodomain fold of several known hydrolyses was found to possess de-ADP-ribosylating activity and the ability to hydrolyze (reverse) ADP-ribosylation. Here we summarize the methods that can be employed to study mono-ADP-ribosylation hydrolysis by macrodomains. |