Abstract
Poly(ADP-ribose) polymerase (PARP) is a protein-modifying and nucleotide-polymerizing enzyme that is abundantly present in the nucleus. PARP consists of the DNA-binding N-terminal domain, the central automodification domain, and the Cterminal catalytic domain. The DNA-binding domain utilizes two zinc fingers, which recognize breaks in double-stranded DNA. The central, highly conserved domain can be auto-poly-ADP-ribosylated by PARP. The C-terminal catalytic domain is involved in the synthesis of poly(ADP-ribose) polymer.1,2 Recent work identifies several isoforms of PARP. For the current review, “PARP” generally refers to the firstly identified, common isoform, which is now also termed PARP-1.
| Original language | English (US) |
|---|---|
| Title of host publication | PARP as a Therapeutic Target |
| Publisher | CRC Press |
| Pages | 169-204 |
| Number of pages | 36 |
| ISBN (Electronic) | 9781420042405 |
| ISBN (Print) | 0849300738, 9780849300738 |
| State | Published - Jan 1 2002 |
| Externally published | Yes |
ASJC Scopus subject areas
- General Pharmacology, Toxicology and Pharmaceutics
- General Biochemistry, Genetics and Molecular Biology
- General Medicine