Evidence map›Paper›PMID 34866305›Full record

ReviewIUBMB life2022

The key role of the NAD biosynthetic enzyme nicotinamide mononucleotide adenylyltransferase in regulating cell functions.

Carlo Fortunato, Francesca Mazzola, Nadia Raffaelli

Open access · hybridAbstract readReview
In one paragraph

Review in IUBMB life, 2022. 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
2.3field-weighted citation impact, top 12% 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, 29 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Microbiome-Derived Metabolites Shape CD4bioRxiv : the preprint server for biology · 2026
    Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Subcellular NADNature metabolism · 2024
    Article
  12. Review
  13. SARM1-Dependent Axon Degeneration: Nucleotide Signaling, Neurodegenerative Disorders, Toxicity, and Therapeutic Opportunities.The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry · 2024
    Review
  14. Article
  15. Inhibitors of NADInternational journal of molecular sciences · 2024
    Review
  16. Review
  17. Review
  18. NADAntioxidants & redox signaling · 2023
    Review
  19. Review
  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

3 authors at 1 institution in 1 country.

Carlo FortunatoDepartment of Agricultural, Food and Environmental Sciences, Polytechnic University of Marche, Ancona, Italy.
Francesca MazzolaDepartment of Clinical Sciences, Polytechnic University of Marche, Ancona, Italy.
Nadia RaffaelliDepartment of Agricultural, Food and Environmental Sciences, Polytechnic University of Marche, Ancona, Italy.ORCID 0000-0002-4458-1789
Marche Polytechnic University · IT

Funding

Fondazione Cassa di Risparmio di Verona Vicenza Belluno e Ancona NADBES 2018.0773Ministero dell' Università e della Ricerca PRIN Project 2017CBNCYT
6 · The paper itself

Abstract

The enzyme nicotinamide mononucleotide adenylyltransferase (NMNAT) catalyzes a reaction central to all known NAD biosynthetic routes. In mammals, three isoforms with distinct molecular and catalytic properties, different subcellular and tissue distribution have been characterized. Each isoform is essential for cell survival, with a critical role in modulating NAD levels in a compartment-specific manner. Each isoform supplies NAD to specific NAD-dependent enzymes, thus regulating their activity with impact on several biological processes, including DNA repair, proteostasis, cell differentiation, and neuronal maintenance. The nuclear NMNAT1 and the cytoplasmic NMNAT2 are also emerging as relevant targets in specific types of cancers and NMNAT2 has a key role in the activation of antineoplastic compounds. This review recapitulates the biochemical properties of the three isoforms and focuses on recent advances on their protective function, involvement in human diseases and role as druggable targets.

Indexed as

Nicotinamide-Nucleotide AdenylyltransferaseAnimalsCell NucleusCytosolHumansMammalsNADProtein IsoformsNADNicotinamide-Nucleotide AdenylyltransferaseNMNAT1 protein, humanProtein IsoformschaperonescoenzymesenzymologyNAD biosynthesisneurodegenerative disordersNMNAT

Identifiers

PMID34866305
PMCPMC9299865
OpenAlexW4200417201

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.