Evidence map›Paper›PMID 24759102›Full record

ArticleThe Journal of biological chemistry2014

YCL047C/POF1 is a novel nicotinamide mononucleotide adenylyltransferase (NMNAT) in Saccharomyces cerevisiae.

Michiko Kato, Su-Ju Lin

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
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

20 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. NADCells · 2025
    Review
  4. Article
  5. The Histone Deacetylases Hst1 and Rpd3 Integrate De Novo NADInternational journal of molecular sciences · 2023
    Article
  6. Article
  7. NADFrontiers in molecular biosciences · 2021
    Review
  8. Article
  9. Article
  10. Review
  11. NADBiomolecules · 2020
    Review
  12. Cross-talk in NADCurrent genetics · 2019
    Review
  13. Article
  14. Dual control of NADeLife · 2019
    Article
  15. Article
  16. A functional link between NADThe Journal of biological chemistry · 2018
    Article
  17. Article
  18. Article
  19. Article
  20. Review
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

2 authors at 1 institution in 1 country.

Michiko KatoFrom the Department of Microbiology and Molecular Genetics, College of Biological Sciences, University of California, Davis, California 95616.
Su-Ju LinFrom the Department of Microbiology and Molecular Genetics, College of Biological Sciences, University of California, Davis, California 95616 slin@ucdavis.edu.
University of California, Davis · US

Funding

Understanding the Regulation of NAD+Homeostasis and SignalingR01GM102297 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI LIN, SU-JU · 2012 to 2019
$2.2M
NIGMS NIH HHS GM102297NIGMS NIH HHS R01 GM102297
6 · The paper itself

Abstract

NAD(+) is an essential metabolic cofactor involved in various cellular biochemical processes. Nicotinamide riboside (NR) is an endogenously produced key pyridine metabolite that plays important roles in the maintenance of NAD(+) pool. Using a NR-specific cell-based screen, we identified mutants that exhibit altered NR release phenotype. Yeast cells lacking the ORF YCL047C/POF1 release considerably more NR compared with wild type, suggesting that POF1 plays an important role in NR/NAD(+) metabolism. The amino acid sequence of Pof1 indicates that it is a putative nicotinamide mononucleotide adenylyltransferase (NMNAT). Unlike other yeast NMNATs, Pof1 exhibits NMN-specific adenylyltransferase activity. Deletion of POF1 significantly lowers NAD(+) levels and decreases the efficiency of NR utilization, resistance to oxidative stress, and NR-induced life span extension. We also show that NR is constantly produced by multiple nucleotidases and that the intracellular NR pools are likely to be compartmentalized, which contributes to the regulation of NAD(+) homeostasis. Our findings may contribute to the understanding of the molecular basis and regulation of NAD(+) metabolism in higher eukaryotes.

Indexed as

Amino Acid SequenceHomeostasisMolecular Sequence DataNADNiacinamideNicotinamide-Nucleotide AdenylyltransferasePyridinium CompoundsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsNADNiacinamidenicotinamide-beta-ribosideNicotinamide-Nucleotide AdenylyltransferasePOF1 protein, S cerevisiaePyridinium CompoundsSaccharomyces cerevisiae ProteinsCell MetabolismMetabolic RegulationNAD BiosynthesisNicotinamide Mononucleotide AdenylyltransferaseNicotinamide Riboside SalvageYeast GeneticsYeast Metabolism

Identifiers

PMID24759102
PMCPMC4140913
OpenAlexW2028062494

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.