Evidence map›Paper›PMID 24552824›Full record

ArticleCell cycle (Georgetown, Tex.)2014

The NAD+ synthesizing enzyme nicotinamide mononucleotide adenylyltransferase 2 (NMNAT-2) is a p53 downstream target.

Lu-Zhe Pan, Dae-Gyun Ahn, Tanveer Sharif, Derek Clements, Shashi A Gujar, Patrick W K Lee

Open access · hybridAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

24 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. A Molecular Perspective and Role of NADInternational journal of molecular sciences · 2024
    Review
  5. Inhibitors of NADInternational journal of molecular sciences · 2024
    Review
  6. Impact of NAD+ metabolism on ovarian aging.Immunity & ageing : I & A · 2023
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Small Molecule Regulators Targeting NADCurrent medicinal chemistry · 2022
    Article
  12. Article
  13. Article
  14. Caffeine and NADAntioxidants (Basel, Switzerland) · 2020
    Article
  15. Article
  16. Subcellular compartmentalization of NADPharmacology & therapeutics · 2019
    Review
  17. NMNAT2-mediated NADAging cell · 2019
    Article
  18. NAD Metabolism in Cancer Therapeutics.Frontiers in oncology · 2018
    Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Lu-Zhe PanDepartment of Microbiology and Immunology; Dalhousie University; Halifax, Nova Scotia, Canada.
Dae-Gyun AhnDepartment of Microbiology and Immunology; Dalhousie University; Halifax, Nova Scotia, Canada.
Tanveer SharifDepartment of Microbiology and Immunology; Dalhousie University; Halifax, Nova Scotia, Canada.
Derek ClementsDepartment of Pathology; Dalhousie University; Halifax, Nova Scotia, Canada.
Shashi A GujarDepartment of Microbiology and Immunology; Dalhousie University; Halifax, Nova Scotia, Canada; Strategy & Organizational Performance; IWK Health Centre; Halifax, Nova Scotia, Canada.
Patrick W K LeeDepartment of Microbiology and Immunology; Dalhousie University; Halifax, Nova Scotia, Canada; Department of Pathology; Dalhousie University; Halifax, Nova Scotia, Canada.
Dalhousie University · CANova Scotia Health Authority · CA

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

NAD(+) metabolism plays key roles not only in energy production but also in diverse cellular physiology. Aberrant NAD(+) metabolism is considered a hallmark of cancer. Recently, the tumor suppressor p53, a major player in cancer signaling pathways, has been implicated as an important regulator of cellular metabolism. This notion led us to examine whether p53 can regulate NAD(+) biosynthesis in the cell. Our search resulted in the identification of nicotinamide mononucleotide adenylyltransferase 2 (NMNAT-2), a NAD(+) synthetase, as a novel downstream target gene of p53. We show that NMNAT-2 expression is induced upon DNA damage in a p53-dependent manner. Two putative p53 binding sites were identified within the human NMNAT-2 gene, and both were found to be functional in a p53-dependent manner. Furthermore, knockdown of NMNAT-2 significantly reduces cellular NAD(+) levels and protects cells from p53-dependent cell death upon DNA damage, suggesting an important functional role of NMNAT-2 in p53-mediated signaling. Our demonstration that p53 modulates cellular NAD(+) synthesis is congruent with p53's emerging role as a key regulator of metabolism and related cell fate.

Indexed as

Binding SitesCell DeathCell Line, TumorDNA DamageHumansNADNicotinamide-Nucleotide AdenylyltransferaseTumor Suppressor Protein p53NADNicotinamide-Nucleotide AdenylyltransferaseNMNAT2 protein, humanTumor Suppressor Protein p53apoptosisNAD+ biosynthesisNMNAT-2p53

Identifiers

PMID24552824
PMCPMC3984302
OpenAlexW2005613774

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.