Evidence map›Paper›PMID 19131966›Full record

ArticleThe EMBO journal2009

Conversion of the 2 Cl(-)/1 H+ antiporter ClC-5 in a NO3(-)/H+ antiporter by a single point mutation.

Giovanni Zifarelli, Michael Pusch

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
7.3field-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

55 citing papers in PubMed, 103 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Chloride Channel Family in the EuhalophyteInternational journal of molecular sciences · 2023
    Article
  5. Article
  6. Review
  7. ClThe Journal of biological chemistry · 2020
    Article
  8. Review
  9. New Insights into the Mechanism of NOJournal of the American Society of Nephrology : JASN · 2019
    Article
  10. Article
  11. Changes inFrontiers in plant science · 2018
    Article
  12. Article
  13. Article
  14. Functional coupling of V-ATPase and CLC-5.World journal of nephrology · 2017
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review
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

2 authors at 1 institution in 1 country.

Giovanni ZifarelliIstituto di Biofisica, CNR, Via De Marini, Genova, Italy.
Michael Pusch
Instituto Biofisika · ES

Funding

Telethon GGP08064
6 · The paper itself

Abstract

Several members of the CLC family are secondary active anion/proton exchangers, and not passive chloride channels. Among the exchangers, the endosomal ClC-5 protein that is mutated in Dent's disease shows an extreme outward rectification that precludes a precise determination of its transport stoichiometry from measurements of the reversal potential. We developed a novel imaging method to determine the absolute proton flux in Xenopus oocytes from the extracellular proton gradient. We determined a transport stoichiometry of 2 Cl(-)/1 H+. Nitrate uncoupled proton transport but mutating the highly conserved serine 168 to proline, as found in the plant NO3(-)/H+ antiporter atClCa, led to coupled NO3(-)/H+ exchange. Among several amino acids tested at position 168, S168P was unique in mediating highly coupled NO3(-)/H+ exchange. We further found that ClC-5 is strongly stimulated by intracellular protons in an allosteric manner with an apparent pK of approximately 7.2. A 2:1 stoichiometry appears to be a general property of CLC anion/proton exchangers. Serine 168 has an important function in determining anionic specificity of the exchange mechanism.

Indexed as

ProtonsAmino Acid SequenceAmino Acid SubstitutionAnimalsAnion Transport ProteinsAntiportersChloride ChannelsChloridesElectric ConductivityFluorescenceHumansHydrogen-Ion ConcentrationIntracellular SpaceMolecular Sequence DataMutant ProteinsNitratesAnion Transport ProteinsAntiportersChloride ChannelsChloridesCLC-5 chloride channelMutant ProteinsNitratesNitrate TransportersProtonsSucrose

Identifiers

PMID19131966
PMCPMC2637338
OpenAlexW2071881662

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.