Evidence map›Paper›PMID 23212377›Full record

ArticleNature communications2012

Identification and characterization of a human mitochondrial NAD kinase.

Kazuto Ohashi, Shigeyuki Kawai, Kousaku Murata

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
4.5field-weighted citation impact, top 6% 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

78 citing papers in PubMed, 124 citations in OpenAlex.

  1. DNA methylation alterations in muscle of critically ill patients.Journal of cachexia, sarcopenia and muscle · 2022
    Trial
  2. Inorganic polyphosphate chelates CaBiochemistry and biophysics reports · 2026
    Article
  3. Mitochondrial NADP(H)-dependent de novo dTMP biosynthesis counteracts the cytotoxicity of PARP inhibitors.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Phenomic and Transcriptomic Profiling of ZnS QD Response inNanomaterials (Basel, Switzerland) · 2026
    Article
  6. Mitochondrial NADK2-dependent NADPH controls tau oligomer uptake in human neurons.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026
    Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. NADPCurrent medicinal chemistry · 2025
    Review
  18. Article
  19. Regulation of and challenges in targeting NADNature reviews. Molecular cell biology · 2024
    Review
  20. Article

18 more citing papers are in PubMed but not listed here.

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.

Kazuto OhashiLaboratory of Basic and Applied Molecular Biotechnology, Division of Food and Biological Science, Graduate School of Agriculture, Kyoto University, Uji, Kyoto 611-0011, Japan.
Shigeyuki Kawai
Kousaku Murata
Kyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NAD kinase is the sole NADP(+) biosynthetic enzyme. Despite the great significance of NADP(+), to date no mitochondrial NAD kinase has been identified in human, and the source of human mitochondrial NADP(+) remains elusive. Here we present evidence demonstrating that a human protein of unknown function, C5orf33, is a human mitochondrial NAD kinase; this protein likely represents the missing source of human mitochondrial NADP(+). The C5orf33 protein exhibits NAD kinase activity, utilizing ATP or inorganic polyphosphate, and is localized in the mitochondria of human HEK293A cells. C5orf33 mRNA is more abundant than human cytosolic NAD kinase mRNA in almost all tissues examined. We further show by database searches that some animals and protists carry C5orf33 homologues as their sole NADP(+) biosynthetic enzyme, whereas plants and fungi possess no C5orf33 homologue. These observations provide insights into eukaryotic NADP(+) biosynthesis, which has pivotal roles in cells and organelles.

Indexed as

Adenosine TriphosphateBlotting, WesternHEK293 CellsHumansMicroscopy, FluorescenceMitochondriaMitochondrial ProteinsPhosphotransferases (Alcohol Group Acceptor)PolyphosphatesRNA, MessengerSaccharomyces cerevisiaeAdenosine TriphosphateMitochondrial ProteinsNADK2 protein, humanNAD kinasePhosphotransferases (Alcohol Group Acceptor)PolyphosphatesRNA, Messenger

Identifiers

PMID23212377
PMCPMC3535332
OpenAlexW1967487164

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.