Role of poly(ADP-ribose) polymerase activation in the pathogenesis of shock and inflammation

Csaba Szabó

    Research output: Chapter in Book/Report/Conference proceedingChapter

    1 Scopus citations

    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 languageEnglish (US)
    Title of host publicationPARP as a Therapeutic Target
    PublisherCRC Press
    Pages169-204
    Number of pages36
    ISBN (Electronic)9781420042405
    ISBN (Print)0849300738, 9780849300738
    StatePublished - Jan 1 2002

    ASJC Scopus subject areas

    • Medicine(all)
    • Pharmacology, Toxicology and Pharmaceutics(all)
    • Biochemistry, Genetics and Molecular Biology(all)

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  • Cite this

    Szabó, C. (2002). Role of poly(ADP-ribose) polymerase activation in the pathogenesis of shock and inflammation. In PARP as a Therapeutic Target (pp. 169-204). CRC Press.