Evidence map›Paper›PMID 22342689›Full record

ReviewMolecular aspects of medicine

Structure, function and translational relevance of aquaporin dual water and ion channels.

Andrea J Yool, Ewan M Campbell

Abstract readReview
In one paragraph

Review in Molecular aspects of medicine. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
1.6field-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

47 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
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  15. Review
  16. Review
  17. Methods for studying mammalian aquaporin biology.Biology methods & protocols · 2023
    Review
  18. Transport Characteristics of Aquaporins.Advances in experimental medicine and biology · 2023
    Article
  19. Article
  20. Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels.International journal of molecular sciences · 2022
    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.

Andrea J YoolSchool of Medical Sciences and The Adelaide Centre for Neuroscience Research, Medical School South, Frome Road, University of Adelaide, Adelaide, SA 5005, Australia. andrea.yool@adelaide.edu.au
Ewan M Campbell
University of Adelaide · AU

Funding

STRUCTURAL BASIS OF ION CHANNEL FUNCTION IN AQUAPORIN-1R01GM059986 · NIGMS · UNIVERSITY OF ARIZONA · PI STAMER, W DANIEL · 2000 to 2007
$1.9M
NIGMS NIH HHS R01 GM059986
6 · The paper itself

Abstract

Aquaporins have been assumed to be selective for water alone, and aquaglyceroporins are accepted as carrying water and small uncharged solutes including glycerol. This review presents an expanded view of aquaporins as channels with more complex mechanisms of regulation and diverse repertoires of substrate permeabilities than were originally appreciated in the early establishment of the field. The role of aquaporins as dual water and gated ion channels is likely to have physiological and potentially translational relevance, and can be evaluated with newly developed molecular and pharmacological tools. Ion channel activity has been shown for Aquaporins -0, -1, and -6, Drosphila Big Brain, and plant Nodulin-26. Although the concept of ion channel function in aquaporins remains controversial, research advances are beginning to define not only the ion channel function but also the detailed molecular mechanisms that govern and mediate the multifunctional capabilities. With regard to physiological relevance, the adaptive benefit of expression of ion channel activity in aquaporins, implied by amino acid sequence conservation of the ion channel gating domains, suggests they provide more than water or glycerol and solute transport. Dual ion and water channels are of interest for understanding the modulation of transmembrane fluid gradients, volume regulation, and possible signal transduction in tissues expressing classes of aquaporins that have the dual function capability. Other aquaporin classes might be found in future work to have ion channel activities, pending identification of the possible signaling pathways that could govern activation.

Indexed as

Amino Acid SequenceAnimalsAquaglyceroporinsAquaporinsBiological TransportGlycerolHumansMolecular Sequence DataPlantsProtein Structure, TertiarySequence Homology, Amino AcidWaterWater-Electrolyte BalanceAquaglyceroporinsAquaporinsGlycerolWater

Identifiers

PMID22342689
PMCPMC3419283
OpenAlexW2023821031

What OpenQuestion holds

Textmetadata
LicenceTDM
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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.