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

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Citation (Scopus)

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
Externally publishedYes

Fingerprint

Poly(ADP-ribose) Polymerases
Shock
Chemical activation
Inflammation
Catalytic Domain
Protein Isoforms
DNA
Poly Adenosine Diphosphate Ribose
Double-Stranded DNA Breaks
Zinc Fingers
Adenosine Diphosphate
Nucleotides
Zinc
Enzymes
Proteins

ASJC Scopus subject areas

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

Cite this

Szabo, 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.

Role of poly(ADP-ribose) polymerase activation in the pathogenesis of shock and inflammation. / Szabo, Csaba.

PARP as a Therapeutic Target. CRC Press, 2002. p. 169-204.

Research output: Chapter in Book/Report/Conference proceedingChapter

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