Evidence map›Paper›PMID 23038248›Full record

ArticleThe Journal of biological chemistry2012

Poly(ADP-ribose) contributes to an association between poly(ADP-ribose) polymerase-1 and xeroderma pigmentosum complementation group A in nucleotide excision repair.

Brenee S King, Karen L Cooper, Ke Jian Liu, Laurie G Hudson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

47 citing papers in PubMed, 66 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Fueling genome maintenance: On the versatile roles of NADThe Journal of biological chemistry · 2022
    Review
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Review
  15. XPA: DNA Repair Protein of Significant Clinical Importance.International journal of molecular sciences · 2020
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Brenee S KingDepartment of Pharmaceutical Sciences, College of Pharmacy, University of New Mexico, Albuquerque, New Mexico 87131, USA.
Karen L Cooper
Ke Jian Liu
Laurie G Hudson
University of New Mexico · US

Funding

WOMEN'S CANCERS RESEARCH PROGRAMP30CA118100 · NCI · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI Yolanda Sanchez · 2005 to 2026
$57.1M
UNM Initiative to Maximize Student Diversity (IMSD)R25GM060201 · NIGMS · UNIVERSITY OF NEW MEXICO · PI WERNER-WASHBURNE, MARGRET C. · 2000 to 2017
$9.9M
Arsenic co-carcinogenesis with UVR: nitrosation and oxidation of target proteinsR01ES021100 · NIEHS · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI HUDSON, LAURIE G, LIU, KE JIAN · 2012 to 2016
$2.4M
Arsenic-enhanced skin carcinogenesis by UV radiationR01ES015826 · NIEHS · UNIVERSITY OF NEW MEXICO · PI LIU, KE JIAN · 2007 to 2011
$2.3M
Role of poly (ADP-ribose)in the Repair of Ultraviolet Induced DNA DamageF31ES019823 · NIEHS · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI KING, BRENEE SHEMEIR · 2011 to 2012
$60k
NCI NIH HHS P30 CA118100NCI NIH HHS P30CA118100NIEHS NIH HHS F31 ES019823NIEHS NIH HHS F31ES019823NIEHS NIH HHS R01 ES015826NIEHS NIH HHS R01ES015826NIEHS NIH HHS R01 ES021100NIGMS NIH HHS R25 GM060201
6 · The paper itself

Abstract

Exposure to ultraviolet radiation (UVR) promotes the formation of UVR-induced, DNA helix distorting photolesions such as (6-4) pyrimidine-pyrimidone photoproducts and cyclobutane pyrimidine dimers. Effective repair of such lesions by the nucleotide excision repair (NER) pathway is required to prevent DNA mutations and chromosome aberrations. Poly(ADP-ribose) polymerase-1 (PARP-1) is a zinc finger protein with well documented involvement in base excision repair. PARP-1 is activated in response to DNA damage and catalyzes the formation of poly(ADP-ribose) subunits that assist in the assembly of DNA repair proteins at sites of damage. In this study, we present evidence for PARP-1 contributions to NER, extending the knowledge of PARP-1 function in DNA repair beyond the established role in base excision repair. Silencing the PARP-1 protein or inhibiting PARP activity leads to retention of UVR-induced photolesions. PARP activation following UVR exposure promotes association between PARP-1 and XPA, a central protein in NER. Administration of PARP inhibitors confirms that poly(ADP-ribose) facilitates PARP-1 association with XPA in whole cell extracts, in isolated chromatin complexes, and in vitro. Furthermore, inhibition of PARP activity decreases UVR-stimulated XPA chromatin association, illustrating that these relationships occur in a meaningful context for NER. These results provide a mechanistic link for PARP activity in the repair of UVR-induced photoproducts.

Indexed as

DNA DamageCell LineChromatinDNA RepairEnzyme InhibitorsHumansKeratinocytesPoly Adenosine Diphosphate RibosePoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesUltraviolet RaysXeroderma Pigmentosum Group A ProteinChromatinEnzyme InhibitorsPARP1 protein, humanPoly Adenosine Diphosphate RibosePoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesXeroderma Pigmentosum Group A ProteinXPA protein, human

Identifiers

PMID23038248
PMCPMC3501068
OpenAlexW2095264331

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.