author={Alexander B{\"u}rkle},
  journal={The FEBS Journal},
  • A. Bürkle
  • Published 1 September 2005
  • Biology
  • The FEBS Journal
One of the most drastic post‐translational modification of proteins in eukaryotic cells is poly(ADP‐ribosyl)ation, catalysed by a family enzymes termed poly(ADP‐ribose) polymerases (PARPs). In the human genome, 18 different genes have been identified that all encode PARP family members. Poly(ADP‐ribose) metabolism plays a role in a wide range of biological structures and processes, including DNA repair and maintenance of genomic stability, transcriptional regulation, centromere function and… 

Functions of the poly(ADP-ribose) polymerase superfamily in plants

The current state of plant research into poly(ADP-ribosyl)ation and the PARP superfamily in plants is summarized and members of the SRO family have been shown to be necessary for normal sporophytic development.

Functional regulation of proteins involved in genomic maintenance by poly(ADP-ribose)

The present study demonstrates that DEK owns also the capability of PAR binding in a non-covalent manner, and identifies three distinct putative PAR binding motifs that mediate a strong binding to the polymer with higher affinity to long chains, suggesting the existence of a “PAR code” with distinct roles of PAR of different chain length.

Poly(ADP-ribosyl)ation in mammalian ageing

A body of correlative data suggests a link between DNA damage-induced poly(ADP-ribosyl)ation and mammalian longevity and several candidate mechanisms through which poly(ADEp-ribose)ation might act as a factor that limits the rate of ageing.

Poly(ADP-ribosyl)ation by PARP1: reaction mechanism and regulatory proteins

Old and up-to-date literature is summarized to clarify several points concerning PARylation mechanism and discuss different ways for regulation of PAR synthesis by accessory proteins reported thus far.

Physiological relevance of the endogenous mono(ADP‐ribosyl)ation of cellular proteins

The mono(ADP‐ribosyl)ation reaction is a post‐translational modification that is catalysed by both bacterial toxins and eukaryotic enzymes, and that results in the transfer of ADP‐ribose from βNAD+

Readers of poly(ADP-ribose): designed to be fit for purpose

An overview on the current understanding of the writers of this modification and their targets, as well as the enzymes that degrade and thereby modify and erase poly(ADP-ribose) (PAR).



The PARP superfamily

This review summarizes the present knowledge of this emerging superfamily of Poly(ADP‐ribose) polymerases, which might ultimately improve pharmacological strategies to enhance both antitumor efficacy and the treatment of a number of inflammatory and neurodegenerative disorders.

Importance of poly(ADP-ribose) glycohydrolase in the control of poly(ADP-ribose) metabolism.

The question of its putative nucleo-cytoplasmic shuttling that could enable the tight regulation of pADPr metabolism would contribute to the elucidation of the biological significance of poly(ADP-ribosyl)ation.

Loss of poly(ADP-ribose) glycohydrolase causes progressive neurodegeneration in Drosophila melanogaster

  • S. HanaiM. Kanai M. Miwa
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 2003
The results suggest that poly(ADP-ribose) metabolism is required for maintenance of the normal function of neuronal cells in Drosophila and might be useful to understand neurodegenerative conditions such as the Alzheimer's and Parkinson's diseases.

Poly(ADP-ribose) polymerase localizes to the centrosomes and chromosomes.

It is found that PARP is localized to the centrosomes and the chromosomes at cell-division phase and interphase by indirect immunofluorescence and PARP protein was found to associate with theCentrosomes during mitosis, suggesting thatPARP may be involved in maintenance of chromosomal stability.

Poly(ADP‐ribosyl)ation inhibitors: Promising drug candidates for a wide variety of pathophysiologic conditions

Inhibition of ADP‐ribose polymer formation has been shown to be effective, on the one hand, in the treatment of cancer in combination with alkylating agents by suppressing DNA repair and thus driving tumour cells into apoptosis, and on the other hand it appears to be a promising drug target for the Treatment of pathologic conditions involving oxidative stress.

Poly(ADP-ribosyl)ation during chromatin remodeling steps in rat spermiogenesis

It is hypothesize that transient ADP-ribose polymer formation may facilitate DNA strand break management during the chromatin remodeling steps of sperm cell maturation.

Tankyrase, a poly(ADP-ribose) polymerase at human telomeres.

Tankyrase, a protein with homology to ankyrins and to the catalytic domain of poly(adenosine diphosphate-ribose) polymerase (PARP), was identified and localized to human telomeres, suggesting that telomere function in human cells is regulated by poly(ADP-ribosyl)ation.

Poly(ADP-ribose) Binds to Specific Domains in DNA Damage Checkpoint Proteins*

The poly(ADP-ribose)-binding motif was found to overlap with five important functional domains responsible for protein-protein interactions, DNA binding, nuclear localization, nuclear export, and protein degradation, Thus, PARPs may target specific signal network proteins via poly(ADE)ribose and regulate their domain functions.