ReviewThe Journal of physiology2025
Recent advances in structural characterization of volume-regulated anion channels (VRACs).
Review in The Journal of physiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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.
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.
Who cites it
5 citing papers in PubMed.
- The intracellular subdomain of the volume-regulated anion channel subunit LRRC8A is a hotspot of channel activation.Nature communications · 2026Article
- Large-Pore Channels at the Maternal-Fetal Interface: Progress and Open Research Avenues.Biology · 2026Review
- Plant-Derived Natural Products and Selective Apoptosis: A Cancer-Cell Vulnerability-State Framework from Redox Imbalance to Membrane-Ion Dysregulation.Pharmaceuticals (Basel, Switzerland) · 2026Review
- A conserved mechanism of LRRC8 channel inhibition by two structurally distinct drugs.Communications biology · 2025Article
- The ion transport, GPCR, and RTK toolkit expression in the human cerebrovascular endothelial cell line, hCMEC/D3: an Omics perspective.Frontiers in physiology · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Volume-regulated anion channels (VRACs) encoded by the LRRC8 gene family play essential roles in diverse and fundamentally important physiological processes in vertebrate cells. The recent determination of high-resolution cryo-electron microscopy (cryo-EM) structures of homomeric and heteromeric LRRC8 channel complexes has created unprecedented opportunities for understanding the molecular basis of VRAC structure, function and pharmacology. Native LRRC8 channels are obligatory heteromers composed of at least one LRRC8A subunit together with one of the other paralogues (LRRC8B-E) with an unknown stoichiometry. This heteromeric nature of endogenously expressed VRACs and the difficulties associated with controlling the composition and stoichiometry of heterologously expressed LRRC8 channels present considerable experimental challenges. The development of LRRC8 chimeras, which exhibit normal functional and regulatory properties and that can be expressed as homomeric channels, circumvents many of these challenges. In this review, we discuss the recent advances in the structural characterization of LRRC8 channels, with a primary focus on the cryo-EM structures of one such chimera, created by swapping 25 residues from LRRC8A subunits to LRRC8C subunits and termed as 8C-8A(IL1
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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.