Evidence map›Paper›PMID 26391948›Full record

ArticleMolecular and cellular biology2015

Differential and Concordant Roles for Poly(ADP-Ribose) Polymerase 1 and Poly(ADP-Ribose) in Regulating WRN and RECQL5 Activities.

Prabhat Khadka, Joseph K Hsu, Sebastian Veith, Takashi Tadokoro, Raghavendra A Shamanna, Aswin Mangerich, Deborah L Croteau, Vilhelm A Bohr

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed, 1 pooled it
0.7field-weighted citation impact, top 26% 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

11 citing papers in PubMed, 1 synthesis or guideline pooled it, 16 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Human RecQ Helicases in DNA Double-Strand Break Repair.Frontiers in cell and developmental biology · 2021
    Review
  8. Review
  9. Review
  10. Article
  11. Article
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

8 authors at 2 institutions in 2 countries.

Prabhat KhadkaLaboratory of Molecular Gerontology, Biomedical Research Center, National Institute on Aging, NIH, Baltimore, Maryland, USA.
Joseph K HsuLaboratory of Molecular Gerontology, Biomedical Research Center, National Institute on Aging, NIH, Baltimore, Maryland, USA.
Sebastian VeithMolecular Toxicology Group, Department of Biology, University of Konstanz, Konstanz, Germany.
Takashi TadokoroLaboratory of Molecular Gerontology, Biomedical Research Center, National Institute on Aging, NIH, Baltimore, Maryland, USA.
Raghavendra A ShamannaLaboratory of Molecular Gerontology, Biomedical Research Center, National Institute on Aging, NIH, Baltimore, Maryland, USA.
Aswin MangerichMolecular Toxicology Group, Department of Biology, University of Konstanz, Konstanz, Germany.
Deborah L CroteauLaboratory of Molecular Gerontology, Biomedical Research Center, National Institute on Aging, NIH, Baltimore, Maryland, USA.
Vilhelm A BohrLaboratory of Molecular Gerontology, Biomedical Research Center, National Institute on Aging, NIH, Baltimore, Maryland, USA vbohr@nih.gov.
National Institute on Aging · USUniversity of Konstanz · DE

Funding

The Function of Werner Syndrome ProteinZIAAG000721 · NIA · NATIONAL INSTITUTE ON AGING · PI FERRUCCI, LUIGI · 2009 to 2022
$7.7M
Intramural NIH HHS
6 · The paper itself

Abstract

Poly(ADP-ribose) (PAR) polymerase 1 (PARP1) catalyzes the poly(ADP-ribosyl)ation (PARylation) of proteins, a posttranslational modification which forms the nucleic acid-like polymer PAR. PARP1 and PAR are integral players in the early DNA damage response, since PARylation orchestrates the recruitment of repair proteins to sites of damage. Human RecQ helicases are DNA unwinding proteins that are critical responders to DNA damage, but how their recruitment and activities are regulated by PARPs and PAR is poorly understood. Here we report that all human RecQ helicases interact with PAR noncovalently. Furthermore, we define the effects that PARP1, PARylated PARP1, and PAR have on RECQL5 and WRN, using both in vitro and in vivo assays. We show that PARylation is involved in the recruitment of RECQL5 and WRN to laser-induced DNA damage and that RECQL5 and WRN have differential responses to PARylated PARP1 and PAR. Furthermore, we show that the loss of RECQL5 or WRN resulted in increased sensitivity to PARP inhibition. In conclusion, our results demonstrate that PARP1 and PAR actively, and in some instances differentially, regulate the activities and cellular localization of RECQL5 and WRN, suggesting that PARylation acts as a fine-tuning mechanism to coordinate their functions in time and space during the genotoxic stress response.

Indexed as

Protein Interaction MapsAdenosine TriphosphatasesDNA Breaks, Double-StrandedDNA RepairEnzyme ActivationExodeoxyribonucleasesHEK293 CellsHeLa CellsHumansPoly Adenosine Diphosphate RibosePoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) Polymerase InhibitorsPoly(ADP-ribose) PolymerasesRecQ HelicasesWerner Syndrome HelicaseAdenosine TriphosphatasesExodeoxyribonucleasesPARP1 protein, humanPoly Adenosine Diphosphate RibosePoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) Polymerase InhibitorsPoly(ADP-ribose) PolymerasesRecQ HelicasesRECQL5 protein, humanWerner Syndrome HelicaseWRN protein, human

Identifiers

PMID26391948
PMCPMC4628069
OpenAlexW2174867240

What OpenQuestion holds

Textmetadata
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.