Evidence map›Paper›PMID 30481609›Full record

ReviewCurrent opinion in structural biology2018

PARP family enzymes: regulation and catalysis of the poly(ADP-ribose) posttranslational modification.

Marie-France Langelier, Travis Eisemann, Amanda A Riccio, John M Pascal

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.

0numbers the graph read from it
0cells of the map it votes in
114citing papers in PubMed
7.1field-weighted citation impact, top 2% 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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

114 citing papers in PubMed, 188 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Cryo-EM structure of ALC1 in an open conformation bound to a PARylated nucleosome.Acta crystallographica. Section D, Structural biology · 2026
    Article
  5. Review
  6. Cancer-associated TRF1 mutations alter PARP1 interaction dynamics: an in silico study.Mammalian genome : official journal of the International Mammalian Genome Society · 2026
    Article
  7. Review
  8. PAR-Driven Condensation Maintains Stalled Replication Fork Stability.bioRxiv : the preprint server for biology · 2026
    Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Review
  14. Review
  15. Article
  16. Prospects for PARG inhibitors in cancer therapy.Journal of molecular cell biology · 2025
    Review
  17. Article
  18. Poly ADP-Ribosylation in a Plant Pathogenic OomyceteJournal of fungi (Basel, Switzerland) · 2025
    Article
  19. An NADTetrahedron · 2024
    Article
  20. Subcellular NADNature metabolism · 2024
    Article

54 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 1 institution in 1 country.

Marie-France LangelierDepartment of Biochemistry and Molecular Medicine, Université de Montréal, Montréal, Québec, Canada.
Travis EisemannDepartment of Biochemistry and Molecular Medicine, Université de Montréal, Montréal, Québec, Canada.
Amanda A RiccioDepartment of Biochemistry and Molecular Medicine, Université de Montréal, Montréal, Québec, Canada.
John M PascalDepartment of Biochemistry and Molecular Medicine, Université de Montréal, Montréal, Québec, Canada. Electronic address: john.pascal@umontreal.ca.
Université de Montréal · CA

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
CIHR BMA342854CIHR PJT374609NCI NIH HHS P01 CA092584
6 · The paper itself

Abstract

Poly(ADP-ribose) is a posttranslational modification and signaling molecule that regulates many aspects of human cell biology, and it is synthesized by enzymes known as poly(ADP-ribose) polymerases, or PARPs. A diverse collection of domain structures dictates the different cellular roles of PARP enzymes and regulates the production of poly(ADP-ribose). Here we primarily review recent structural insights into the regulation and catalysis of two family members: PARP-1 and Tankyrase. PARP-1 has multiple roles in the cellular response to DNA damage and the regulation of gene transcription, and Tankyrase regulates a diverse set of target proteins involved in cellular processes such as mitosis, genome integrity, and cell signaling. Both enzymes offer interesting modes of regulating the production and the target site selectivity of the poly(ADP-ribose) modification.

Indexed as

DNA-Binding ProteinsHumansPoly (ADP-Ribose) Polymerase-1Protein DomainsTankyrasesDNA-Binding ProteinsPARP1 protein, humanPoly (ADP-Ribose) Polymerase-1TankyrasesTNKS2 protein, humanTNKS protein, human

Identifiers

PMID30481609
PMCPMC6687463
OpenAlexW2901569771

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.