Evidence map›Paper›PMID 18957376›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2009

Review. CLC-mediated anion transport in plant cells.

Alexis De Angeli, Dario Monachello, Geneviève Ephritikhine, Jean-Marie Frachisse, Sébastien Thomine, Franco Gambale, Hélène Barbier-Brygoo

Open access · greenAbstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
9.1field-weighted citation impact, top 2% 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

36 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Mutation of external glutamate residue reveals a new intermediate transport state and anion binding site in a CLC ClProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  16. Review
  17. Sensing of Abiotic Stress and Ionic Stress Responses in Plants.International journal of molecular sciences · 2018
    Review
  18. Article
  19. Review
  20. Two tonoplast MATE proteins function as turgor-regulating chloride channels inProceedings of the National Academy of Sciences of the United States of America · 2017
    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

7 authors at 4 institutions in 2 countries.

Alexis De AngeliInstitut des Sciences du Végétal, UPR2355 CNRS, Gif sur Yvette Cedex, France Istituto di Biofisica, CNR, Genova, Italy.
Dario Monachello
Geneviève Ephritikhine
Jean-Marie Frachisse
Sébastien Thomine
Franco Gambale
Hélène Barbier-Brygoo
Institut des Sciences du Végétal · FRCentre National de la Recherche Scientifique · FRDélégation Paris 7 · FRInstituto Biofisika · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plants need nitrate for growth and store the major part of it in the central vacuole of cells from root and shoot tissues. Based on few studies on the two model plants Arabidopsis thaliana and rice, members of the large ChLoride Channel (CLC) family have been proposed to encode anion channels/transporters involved in nitrate homeostasis. Proteins from the Arabidopsis CLC family (AtClC, comprising seven members) are present in various membrane compartments including the vacuolar membrane (AtClCa), Golgi vesicles (AtClCd and AtClCf) or chloroplast membranes (AtClCe). Through a combination of electrophysiological and genetic approaches, AtClCa was shown to function as a 2NO3-/1H+ exchanger that is able to accumulate specifically nitrate into the vacuole, in agreement with the main phenotypic trait of knockout mutant plants that accumulate 50 per cent less nitrate than their wild-type counterparts. The set-up of a functional complementation assay relying on transient expression of AtClCa cDNA in the mutant background opens the way for studies on structure-function relationships of the AtClCa nitrate transporter. Such studies will reveal whether important structural determinants identified in bacterial or mammalian CLCs are also crucial for AtClCa transport activity and regulation.

Indexed as

Plant CellsAnionsChloride ChannelsPlant ProteinsPlantsAnionsChloride ChannelsPlant Proteins

Identifiers

PMID18957376
PMCPMC2674092
OpenAlexW2168563860

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.