Evidence map›Paper›PMID 10455009›Full record

ReviewThe Biochemical journal1999

Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions.

D D'Amours, S Desnoyers, I D'Silva, G G Poirier

Registry-linked trialOpen access · greenAbstract readReview
In one paragraph

Review in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT00678132 (A Phase I Combination Study of AZD2281 and Cisplatin Plus Gemcitabine in Adults With Solid Tumors), which is not on this map. Cited by 796 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
796citing papers in PubMed, 1 pooled it
21.3field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

NCT00678132 phase1completednot on this mapstarted 2008, after this paper: background citation

A Phase I Combination Study of AZD2281 and Cisplatin Plus Gemcitabine in Adults With Solid Tumors

TypeinterventionalSponsorNational Cancer Institute (NCI)Ran2008 to 2010Enrolled23ConditionsNeoplasmsArmsAZD 2281, Cisplatin, Gemcitabine
3 · Its place in the literature

Who cites it

796 citing papers in PubMed, 1 synthesis or guideline pooled it, 1,815 citations in OpenAlex.

  1. Pooled it
  2. NADRSC chemical biology · 2026
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Yeast as a Platform to Dissect Poly(ADP-Ribose) Polymerase Function fromInternational journal of molecular sciences · 2026
    Article
  9. Article
  10. Dynamic Assemblies in Genome Maintenance.Advances in experimental medicine and biology · 2026
    Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. PARP Inhibitors in Genitourinary Cancer: A New Paradigm Beyond Prostate Cancer.International journal of urology : official journal of the Japanese Urological Association · 2025
    Review
  18. Review
  19. Article
  20. Review

736 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

D D'AmoursWellcome/CRC Institute of Cancer and Developmental Biology, Cambridge CB2 1QR, U.K.
S Desnoyers
I D'Silva
G G Poirier
Université Laval · CACold Spring Harbor Laboratory · US

Funding

Wellcome Trust
6 · The paper itself

Abstract

Poly(ADP-ribosyl)ation is a post-translational modification of proteins. During this process, molecules of ADP-ribose are added successively on to acceptor proteins to form branched polymers. This modification is transient but very extensive in vivo, as polymer chains can reach more than 200 units on protein acceptors. The existence of the poly(ADP-ribose) polymer was first reported nearly 40 years ago. Since then, the importance of poly(ADP-ribose) synthesis has been established in many cellular processes. However, a clear and unified picture of the physiological role of poly(ADP-ribosyl)ation still remains to be established. The total dependence of poly(ADP-ribose) synthesis on DNA strand breaks strongly suggests that this post-translational modification is involved in the metabolism of nucleic acids. This view is also supported by the identification of direct protein-protein interactions involving poly(ADP-ribose) polymerase (113 kDa PARP), an enzyme catalysing the formation of poly(ADP-ribose), and key effectors of DNA repair, replication and transcription reactions. The presence of PARP in these multiprotein complexes, in addition to the actual poly(ADP-ribosyl)ation of some components of these complexes, clearly supports an important role for poly(ADP-ribosyl)ation reactions in DNA transactions. Accordingly, inhibition of poly(ADP-ribose) synthesis by any of several approaches and the analysis of PARP-deficient cells has revealed that the absence of poly(ADP-ribosyl)ation strongly affects DNA metabolism, most notably DNA repair. The recent identification of new poly(ADP-ribosyl)ating enzymes with distinct (non-standard) structures in eukaryotes and archaea has revealed a novel level of complexity in the regulation of poly(ADP-ribose) metabolism.

Indexed as

AnimalsBinding SitesCatalytic DomainCell DeathCell NucleusChromatinDNADNA DamageDNA RepairDNA ReplicationGlycoside HydrolasesHumansModels, BiologicalNADNucleic AcidsPoly Adenosine Diphosphate RiboseChromatinDNAGlycoside HydrolasesNADNucleic AcidsPoly Adenosine Diphosphate Ribosepoly ADP-ribose glycohydrolasePoly(ADP-ribose) Polymerases

Identifiers

PMID10455009
PMCPMC1220459
OpenAlexW2014150894

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.