|
|
|
|
| LEADER |
01625 am a22002413u 4500 |
| 001 |
84682 |
| 042 |
|
|
|a dc
|
| 100 |
1 |
0 |
|a Rood, Jennifer E.
|e author
|
| 100 |
1 |
0 |
|a Massachusetts Institute of Technology. Department of Biology
|e contributor
|
| 100 |
1 |
0 |
|a Koch Institute for Integrative Cancer Research at MIT
|e contributor
|
| 100 |
1 |
0 |
|a Rood, Jennifer E.
|e contributor
|
| 100 |
1 |
0 |
|a Leung, Anthony
|e contributor
|
| 100 |
1 |
0 |
|a Chang, Paul
|e contributor
|
| 700 |
1 |
0 |
|a Leung, Anthony
|e author
|
| 700 |
1 |
0 |
|a Chang, Paul
|e author
|
| 245 |
0 |
0 |
|a Methods for Purification of Proteins Associated with Cellular Poly(ADP-Ribose) and PARP-Specific Poly(ADP-Ribose)
|
| 260 |
|
|
|b Springer Science+Business Media,
|c 2014-02-07T17:31:16Z.
|
| 856 |
|
|
|z Get fulltext
|u http://hdl.handle.net/1721.1/84682
|
| 520 |
|
|
|a available in PMC 2012 November 09
|
| 520 |
|
|
|a Poly(ADP-ribose) (pADPr) is a posttranslational modification that regulates protein function through two major mechanisms: covalent modification of acceptor proteins and noncovalent binding of proteins to pADPr. pADPr is synthesized by a family of enzymes called poly(ADP-ribose) polymerases (PARPs) that are themselves major targets of pADPr modification. Here, we outline two methods for the purification of pADPr-binding proteins via pADPr purification under native conditions: purification of cellular pADPr and pADPr covalently linked to specific PARPs. Together, these methods provide complementary approaches to the identification of noncovalent pADPr-protein interactions in the cell.
|
| 546 |
|
|
|a en_US
|
| 655 |
7 |
|
|a Article
|
| 773 |
|
|
|t Poly(ADP-ribose) Polymerase: Methods and Protocols
|
