Evidence map›Paper›PMID 23440275›Full record

ArticleThe Journal of general physiology2013

Regulation of AQP0 water permeability is enhanced by cooperativity.

Karin L Németh-Cahalan, Daniel M Clemens, James E Hall

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

23 citing papers in PubMed, 31 citations in OpenAlex.

  1. CatExperimental eye research · 2026
    Article
  2. Article
  3. Review
  4. Endothelial Dysfunction in Neurodegenerative Diseases.International journal of molecular sciences · 2023
    Review
  5. Review
  6. Expression Regulation and Trafficking of Aquaporins.Advances in experimental medicine and biology · 2023
    Review
  7. Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels.International journal of molecular sciences · 2022
    Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. C-Terminal End of Aquaporin 0 Regulates Lens Gap Junction Channel Function.Investigative ophthalmology & visual science · 2019
    Article
  13. Cooperativity and allostery in aquaporin 0 regulation by CaBiochimica et biophysica acta. Biomembranes · 2019
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. The pH sensitivity of Aqp0 channels in tetraploid and diploid teleosts.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015
    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 1 institution in 1 country.

Karin L Németh-CahalanDepartment of Physiology and Biophysics, University of California, Irvine, Irvine, CA 92697, USA.
Daniel M Clemens
James E Hall
University of California, Irvine · US

Funding

STRUCTURE /FUNCTION OF LENS CHANNELSR01EY005661 · NEI · UNIVERSITY OF CALIFORNIA-IRVINE · PI HALL, JAMES EWBANK · 1985 to 2018
$7.9M
NEI NIH HHS EY5661NEI NIH HHS R01 EY005661
6 · The paper itself

Abstract

Aquaporin 0 (AQP0), essential for lens clarity, is a tetrameric protein composed of four identical monomers, each of which has its own water pore. The water permeability of AQP0 expressed in Xenopus laevis oocytes can be approximately doubled by changes in calcium concentration or pH. Although each monomer pore functions as a water channel, under certain conditions the pores act cooperatively. In other words, the tetramer is the functional unit. In this paper, we show that changes in external pH and calcium can induce an increase in water permeability that exhibits either a positive cooperativity switch-like increase in water permeability or an increase in water permeability in which each monomer acts independently and additively. Because the concentrations of calcium and hydrogen ions increase toward the center of the lens, a concentration signal could trigger a regulatory change in AQP0 water permeability. It thus seems plausible that the cooperative modes of water permeability regulation by AQP0 tetramers mediated by decreased pH and elevated calcium are the physiologically important ones in the living lens.

Indexed as

AnimalsAquaporinsCalciumEye ProteinsHydrogenHydrogen-Ion ConcentrationLens, CrystallineOocytesPermeabilityWaterXenopus laevisaquaporin 0AquaporinsCalciumEye ProteinsHydrogenWater

Identifiers

PMID23440275
PMCPMC3581697
OpenAlexW2097744719

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.