Evidence map›Paper›PMID 30871717›Full record

ReviewBiophysical journal2019

Biophysics and Structure-Function Relationships of LRRC8-Formed Volume-Regulated Anion Channels.

Benjamin König, Tobias Stauber

Abstract readReview
In one paragraph

Review in Biophysical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
–field-weighted citation impact
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

37 citing papers in PubMed.

  1. Article
  2. Exploring the selective inhibitory effects of Flavoxate and its analogues on two chloride channels and neuronal action potentials.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2026
    Article
  3. Article
  4. The function of chloride channels in digestive system disease (Review).International journal of molecular medicine · 2025
    Review
  5. Article
  6. Model-based evaluation of connexin hemichannel permeability.Computational and structural biotechnology journal · 2025
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. The Integral Role of Chloride & With-No-Lysine Kinases in Cell Volume Regulation & Hypertension.International journal of nephrology and renovascular disease · 2023
    Review
  13. Lysosomal solute and water transport.The Journal of cell biology · 2022
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Ion Channels and Transporters in Muscle Cell Differentiation.International journal of molecular sciences · 2021
    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.

Benjamin KönigFreie Universität Berlin, Institute of Chemistry and Biochemistry, Berlin, Germany.
Tobias StauberFreie Universität Berlin, Institute of Chemistry and Biochemistry, Berlin, Germany. Electronic address: tobias.stauber@fu-berlin.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Volume-regulated anion channels (VRACs) are key players in regulatory volume decrease of vertebrate cells by mediating the extrusion of chloride and organic osmolytes. They play additional roles in various physiological processes beyond their role in osmotic volume regulation. VRACs are formed by heteromers of LRRC8 proteins; LRRC8A (also called SWELL1) is an essential subunit that combines with any of its paralogs, LRRC8B-E, to form hexameric VRAC complexes. The subunit composition of VRACs determines electrophysiological characteristics of their anion transport such as single-channel conductance, outward rectification, and depolarization-dependent inactivation kinetics. In addition, differently composed VRACs conduct diverse substrates, such as LRRC8D enhancing VRAC permeability to organic substances like taurine or cisplatin. Here, after a recapitulation of the biophysical properties of VRAC-mediated ion and osmolyte transport, we summarize the insights gathered since the molecular identification of VRACs. We describe the recently solved structures of LRRC8 complexes and discuss them in terms of their structure-function relationships. These studies open up many potential avenues for future research.

Indexed as

Ion Channel GatingAnimalsHumansMembrane PotentialsMembrane ProteinsProtein DomainsLRRC8A protein, humanMembrane Proteins

Identifiers

PMID30871717
PMCPMC6451053

What OpenQuestion holds

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Registered trials

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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.