Evidence map›Paper›PMID 19448972›Full record

ReviewCellular and molecular life sciences : CMLS2009

Nicotinamide/nicotinic acid mononucleotide adenylyltransferase, new insights into an ancient enzyme.

Rong Grace Zhai, Menico Rizzi, Silvia Garavaglia

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

49 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Evaluation ofFrontiers in veterinary science · 2025
    Article
  6. International journal of molecular sciences · 2024
    Article
  7. International journal of molecular sciences · 2024
    Article
  8. Article
  9. Article
  10. Review
  11. Heliyon · 2022
    Article
  12. Balancing NADCellular and molecular life sciences : CMLS · 2022
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Phagocytosis and self-destruction break down dendrites ofProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  18. Article
  19. NicotinamideBiomolecules · 2021
    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 2 institutions in 2 countries.

Rong Grace ZhaiDepartment of Molecular and Cellular Pharmacology, Neuroscience Center, Miller School of Medicine, University of Miami, Miami, FL 33136, USA. gzhai@med.miami.edu
Menico Rizzi
Silvia Garavaglia
Università degli Studi del Piemonte Orientale “Amedeo Avogadro” · ITUniversity of Miami · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nicotinamide/nicotinic acid mononucleotide adenylyltransferase (NMNAT) has long been known as the master enzyme in NAD biosynthesis in living organisms. A burst of investigations on NMNAT, going beyond enzymology, have paralleled increasing discoveries of key roles played by NAD homeostasis in a number or patho-physiological conditions. The availability of in-depth kinetics and structural enzymology analyses carried out on NMNATs from different organisms offer a powerful tool for uncovering fascinating evolutionary relationships. On the other hand, additional functions featuring NMNAT have emerged from investigations aimed at unraveling the molecular mechanisms responsible for complex biological phenomena such as neurodegeneration. NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at a crossroads of multiple cellular processes. The resultant wealth of biochemical data has built a robust framework upon which design of NMNAT activators, inhibitors or enzyme variants of potential medical interest can be based.

Indexed as

Nicotinamide-Nucleotide AdenylyltransferaseAdenosine TriphosphateAnimalsBinding SitesDNA RepairHumansIsoenzymesModels, MolecularMolecular ChaperonesMolecular Sequence DataNADNiacinamidePoly(ADP-ribose) PolymerasesProtein ConformationSubstrate SpecificityTissue DistributionAdenosine TriphosphateIsoenzymesMolecular ChaperonesNADNiacinamideNicotinamide-Nucleotide Adenylyltransferasenicotinic acid mononucleotide adenylyltransferasePoly(ADP-ribose) Polymerases

Identifiers

PMID19448972
PMCPMC11115848
OpenAlexW2042240740

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.