Title |
Investigation of PARP-1, PARP-2, and PARG interactomes by affinity-purification mass spectrometry
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Published in |
Proteome Science, April 2010
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DOI | 10.1186/1477-5956-8-22 |
Pubmed ID | |
Authors |
Maxim Isabelle, Xavier Moreel, Jean-Philippe Gagné, Michèle Rouleau, Chantal Ethier, Pierre Gagné, Michael J Hendzel, Guy G Poirier |
Abstract |
Poly(ADP-ribose) polymerases (PARPs) catalyze the formation of poly(ADP-ribose) (pADPr), a post-translational modification involved in several important biological processes, namely surveillance of genome integrity, cell cycle progression, initiation of the DNA damage response, apoptosis, and regulation of transcription. Poly(ADP-ribose) glycohydrolase (PARG), on the other hand, catabolizes pADPr and thereby accounts for the transient nature of poly(ADP-ribosyl)ation. Our investigation of the interactomes of PARP-1, PARP-2, and PARG by affinity-purification mass spectrometry (AP-MS) aimed, on the one hand, to confirm current knowledge on these interactomes and, on the other hand, to discover new protein partners which could offer insights into PARPs and PARG functions. |
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Geographical breakdown
Country | Count | As % |
---|---|---|
Germany | 2 | 1% |
United States | 2 | 1% |
Brazil | 1 | <1% |
France | 1 | <1% |
Denmark | 1 | <1% |
United Kingdom | 1 | <1% |
Unknown | 155 | 95% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 35 | 21% |
Researcher | 28 | 17% |
Student > Bachelor | 22 | 13% |
Student > Master | 20 | 12% |
Student > Postgraduate | 7 | 4% |
Other | 18 | 11% |
Unknown | 33 | 20% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 54 | 33% |
Biochemistry, Genetics and Molecular Biology | 49 | 30% |
Medicine and Dentistry | 10 | 6% |
Chemistry | 8 | 5% |
Pharmacology, Toxicology and Pharmaceutical Science | 4 | 2% |
Other | 8 | 5% |
Unknown | 30 | 18% |