Evidence map›Paper›PMID 24155910›Full record

ArticlePloS one2013

Insight into molecular and functional properties of NMNAT3 reveals new hints of NAD homeostasis within human mitochondria.

Roberta Felici, Andrea Lapucci, Matteo Ramazzotti, Alberto Chiarugi

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.3field-weighted citation impact, top 9% 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

41 citing papers in PubMed, 61 citations in OpenAlex.

  1. Mitochondrial NMNAT3 reduces amyloid aggregates inMitochondrial communications · 2026
    Article
  2. Update on Nicotinamide and Its Application in the Management of Glaucoma.International journal of molecular sciences · 2025
    Review
  3. NADNature metabolism · 2025
    Review
  4. Review
  5. Subcellular NADNature metabolism · 2024
    Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Balancing NADCellular and molecular life sciences : CMLS · 2022
    Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Location, Location, Location: Compartmentalization of NADTrends in biochemical sciences · 2020
    Review
  18. Subcellular NAMPT-mediated NADJournal of neurochemistry · 2019
    Article
  19. Article
  20. Review
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Roberta FeliciDepartment of Health Sciences, University of Florence, Florence, Italy.
Andrea Lapucci
Matteo Ramazzotti
Alberto Chiarugi
University of Florence · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Among the enzymes involved in NAD homeostasis, nicotinamide mononucleotide adenylyltransferases (NMNAT1-3) are central to intracellular NAD formation. Although NMNAT3 is postulated to be a mitochondrial enzyme contributing to NAD-dependent organelle functioning, information on endogenous proteins is lacking. We report that in human cells a single gene nmnat3 localized on chromosome 3 codes for two mRNA splice variants NMNATv1 and FKSG76, whereas the previously reported NMNAT3v2 transcript is not present. However, NMNAT3v1 and FKSG76 proteins are not detectable, consistent with the finding that an upstream ORF in their mRNAs negatively regulates translation. NMNAT3v1 transfection demonstrates that the protein is cytosolic and inactive, whereas FKSG76 is mitochondrial but operates NAD cleavage rather than synthesis. In keeping with the lack of NMNAT3, we show that extracellular NAD, but not its metabolic precursors, sustains mitochondrial NAD pool in an ATP-independent manner. Data of the present study modify the scenario of the origin of mitochondrial NAD by showing that, in human cells, NMNAT3 is absent in mitochondria, and, akin to plants and yeast, cytosolic NAD maintains the mitochondrial NAD pool.

Indexed as

HomeostasisBase SequenceGene Expression Regulation, EnzymologicGene SilencingHEK293 CellsHumansIntracellular SpaceMembrane Potential, MitochondrialMitochondriaMolecular Sequence DataNADNicotinamide-Nucleotide AdenylyltransferaseProtein IsoformsProtein TransportRNA, MessengerTransfectionNADNicotinamide-Nucleotide AdenylyltransferaseNMNAT1 protein, humanNMNAT2 protein, humanNMNAT3 protein, humanProtein IsoformsRNA, Messenger

Identifiers

PMID24155910
PMCPMC3796565
OpenAlexW2069882256

What OpenQuestion holds

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LicenceCC BY
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.