Evidence map›Paper›PMID 19745225›Full record

ArticleThe Journal of biological chemistry2009

Molecular identification and functional characterization of Arabidopsis thaliana mitochondrial and chloroplastic NAD+ carrier proteins.

Ferdinando Palmieri, Benjamin Rieder, Angela Ventrella, Emanuela Blanco, Phuc Thi Do, Adriano Nunes-Nesi, A Ulrike Trauth, Giuseppe Fiermonte, Joachim Tjaden, Gennaro Agrimi and 4 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

89 citing papers in PubMed, 169 citations in OpenAlex.

  1. Identification of CCR4C as a chloroplast-localized NADP(H) phosphatase regulating NAD(P)(H) balance inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Emerging interactions between mitochondria and NADTrends in endocrinology and metabolism: TEM · 2025
    Review
  7. Review
  8. The Main Functions of Plastids.Methods in molecular biology (Clifton, N.J.) · 2024
    Review
  9. Review
  10. Article
  11. NADNature communications · 2023
    Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article

29 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

14 authors at 4 institutions in 2 countries.

Ferdinando PalmieriDepartment of Pharmaco-Biology, Laboratory of Biochemistry and Molecular Biology, University of Bari, Bari, Italy.
Benjamin Rieder
Angela Ventrella
Emanuela Blanco
Phuc Thi Do
Adriano Nunes-Nesi
A Ulrike Trauth
Giuseppe Fiermonte
Joachim Tjaden
Gennaro Agrimi
Simon Kirchberger
Eleonora Paradies
Alisdair R Fernie
H Ekkehard Neuhaus
University of Kaiserslautern · DEUniversity of Bari Aldo Moro · ITMax Planck Institute of Molecular Plant Physiology · DEInstitute of Biomembranes, Bioenergetics and Molecular Biotechnologies · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Arabidopsis thaliana L. genome contains 58 membrane proteins belonging to the mitochondrial carrier family. Two mitochondrial carrier family members, here named AtNDT1 and AtNDT2, exhibit high structural similarities to the mitochondrial nicotinamide adenine dinucleotide (NAD(+)) carrier ScNDT1 from bakers' yeast. Expression of AtNDT1 or AtNDT2 restores mitochondrial NAD(+) transport activity in a yeast mutant lacking ScNDT. Localization studies with green fluorescent protein fusion proteins provided evidence that AtNDT1 resides in chloroplasts, whereas only AtNDT2 locates to mitochondria. Heterologous expression in Escherichia coli followed by purification, reconstitution in proteoliposomes, and uptake experiments revealed that both carriers exhibit a submillimolar affinity for NAD(+) and transport this compound in a counter-exchange mode. Among various substrates ADP and AMP are the most efficient counter-exchange substrates for NAD(+). Atndt1- and Atndt2-promoter-GUS plants demonstrate that both genes are strongly expressed in developing tissues and in particular in highly metabolically active cells. The presence of both carriers is discussed with respect to the subcellular localization of de novo NAD(+) biosynthesis in plants and with respect to both the NAD(+)-dependent metabolic pathways and the redox balance of chloroplasts and mitochondria.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsCarrier ProteinsChloroplastsGene Expression Regulation, PlantMitochondriaMolecular Sequence DataNADProtein TransportSequence AlignmentArabidopsis ProteinsCarrier ProteinsNAD

Identifiers

PMID19745225
PMCPMC2781523
OpenAlexW1974237236

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.