ArticleThe Journal of physiology2020
Pannexin 1 activation and inhibition is permeant-selective.
Article in The Journal of physiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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.
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
27 citing papers in PubMed, 49 citations in OpenAlex.
- Discovery of membrane channel modulators via DNA encoded library screening using native like membrane protein nanoparticles.Scientific reports · 2026Article
- Panx1 and drug discovery: from non-specific inhibitors to tailored drug compounds.Cell and tissue research · 2026Review
- ATP increases murine neuroblastoma cell size through a PANX1- and macropinocytosis-dependent mechanism.Biology open · 2025Article
- Pannexins in the vasculature.American journal of physiology. Heart and circulatory physiology · 2025Review
- Pannexin channels in the kidney.American journal of physiology. Renal physiology · 2025Review
- Distinct properties and activation of hexameric and heptameric Pannexin 1 channel concatemers.The Journal of general physiology · 2025Article
- The C-terminal activating domain promotes pannexin 1 channel opening.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Large-pore connexin hemichannels function like molecule transporters independent of ion conduction.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- CaProceedings of the National Academy of Sciences of the United States of America · 2024Article
- The C-terminal activating domain promotes Panx1 channel opening.bioRxiv : the preprint server for biology · 2024Article
- Neuronal Panx1 drives peripheral sensitization in experimental plantar inflammatory pain.Military Medical Research · 2024Article
- Review
- Pannexin-3 stabilizes the transcription factor Bcl6 in a channel-independent manner to protect against vascular oxidative stress.Science signaling · 2024Article
- Structure-Based Design and Synthesis of StapledJournal of medicinal chemistry · 2023Article
- The Impact of Plasma Membrane Ion Channels on Bone Remodeling in Response to Mechanical Stress, Oxidative Imbalance, and Acidosis.Antioxidants (Basel, Switzerland) · 2023Review
- Article
- A novel heterozygous variant in PANX1 causes primary infertility due to oocyte death.Journal of assisted reproduction and genetics · 2023Article
- Brivaracetam and Levetiracetam Suppress Astroglial L-Glutamate Release through Hemichannel via Inhibition of Synaptic Vesicle Protein.International journal of molecular sciences · 2022Article
- Pannexin 1 as a driver of inflammation and ischemia-reperfusion injury.Purinergic signalling · 2021Review
- Structure versus function: Are new conformations of pannexin 1 yet to be resolved?The Journal of general physiology · 2021Article
Corrections and comments
- Commented on by
Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
key pointsThe large-pore channel pannexin 1 (Panx1) is expressed in many cell types and can open upon different, yet not fully established, stimuli. Panx1 permeability is often inferred from channel permeability to fluorescent dyes, but it is currently unknown whether dye permeability translates to permeability to other molecules. Cell shrinkage and C-terminal cleavage led to a Panx1 open-state with increased permeability to atomic ions (current), but did not alter ethidium uptake. Panx1 inhibitors affected Panx1-mediated ion conduction differently from ethidium permeability, and inhibitor efficiency towards a given molecule therefore cannot be extrapolated to its effects on the permeability of another. We conclude that ethidium permeability does not reflect equal permeation of other molecules and thus is no measure of general Panx1 activity. ABSTRACT: Pannexin 1 (Panx1) is a large-pore membrane channel connecting the extracellular milieu with the cell interior. While several activation regimes activate Panx1 in a variety of cell types, the selective permeability of an open Panx1 channel remains unresolved: does a given activation paradigm increase Panx1's permeability towards all permeants equally and does fluorescent dye flux serve as a proxy for biological permeation through an open channel? To explore permeant-selectivity of Panx1 activation and inhibition, we employed Panx1-expressing Xenopus laevis oocytes and HEK293T cells. We report that different mechanisms of activation of Panx1 differentially affected ethidium and atomic ion permeation. Most notably, C-terminal truncation or cell shrinkage elevated Panx1-mediated ion conductance, but had no effect on ethidium permeability. In contrast, extracellular pH changes predominantly affected ethidium permeability but not ionic conductance. High [K
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.