Evidence map›Paper›PMID 32048993›Full record

ArticleeLife2020

The Cryo-EM structure of pannexin 1 reveals unique motifs for ion selection and inhibition.

Kevin Michalski, Johanna L Syrjanen, Erik Henze, Julia Kumpf, Hiro Furukawa, Toshimitsu Kawate

Open access · goldAbstract readVideo-Audio Media
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed
9.0field-weighted citation impact, top 1% 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

100 citing papers in PubMed, 158 citations in OpenAlex.

  1. Article
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  7. Article
  8. Pannexins in the vasculature.American journal of physiology. Heart and circulatory physiology · 2025
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Contribution of pannexin channels to afterimage signals in the amphibian retina.American journal of physiology. Cell physiology · 2025
    Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. A mechanism of CALHM1 ion channel gating.American journal of physiology. Cell physiology · 2025
    Article
  20. Novel Naphthyridones Targeting Pannexin 1 for Colitis Management.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article

40 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Kevin Michalski *Department of Molecular Medicine, Cornell University, Ithaca, United States.
Johanna L Syrjanen *WM Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, Cold Spring Harbor, United States.
Erik HenzeDepartment of Molecular Medicine, Cornell University, Ithaca, United States.
Julia KumpfDepartment of Molecular Medicine, Cornell University, Ithaca, United States.ORCID 0000-0002-3813-1255
Hiro FurukawaWM Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, Cold Spring Harbor, United States.
Toshimitsu KawateDepartment of Molecular Medicine, Cornell University, Ithaca, United States.ORCID 0000-0002-5005-2031
Cornell University · USCold Spring Harbor Laboratory · US

Funding

TRAINING IN MOLECULAR PHYSICS OF BIOLOGICAL SYSTEMST32GM008267 · NIGMS · CORNELL UNIVERSITY ITHACA · PI WANG, MICHELLE D. · 1988 to 2021
$9.6M
Structure and Function of Hetero-Multimeric Ligand-Gated Ion ChannelsR01NS111745 · NINDS · COLD SPRING HARBOR LABORATORY · PI Hiroyasu Furukawa · 2019 to 2026
$4.2M
Structure and Function of Pannexins: Activation MechanismR01GM114379 · NIGMS · CORNELL UNIVERSITY · PI KAWATE, TOSHIMITSU · 2015 to 2025
$3.1M
Structure and Function of Neuronal HemichannelsRF1NS113632 · NINDS · COLD SPRING HARBOR LABORATORY · PI FURUKAWA, HIROYASU · 2019 to 2019
$2.7M
NIGMS NIH HHS R01 GM114379NIGMS NIH HHS T32 GM008267NINDS NIH HHS R01 NS111745NINDS NIH HHS RF1 NS113632
6 · The paper itself

Abstract

Pannexins are large-pore forming channels responsible for ATP release under a variety of physiological and pathological conditions. Although predicted to share similar membrane topology with other large-pore forming proteins such as connexins, innexins, and LRRC8, pannexins have minimal sequence similarity to these protein families. Here, we present the cryo-EM structure of a frog pannexin 1 (Panx1) channel at 3.0 Å. We find that Panx1 protomers harbor four transmembrane helices similar in arrangement to other large-pore forming proteins but assemble as a heptameric channel with a unique constriction formed by Trp74 in the first extracellular loop. Mutating Trp74 or the nearby Arg75 disrupt ion selectivity, whereas altering residues in the hydrophobic groove formed by the two extracellular loops abrogates channel inhibition by carbenoxolone. Our structural and functional study establishes the extracellular loops as important structural motifs for ion selectivity and channel inhibition in Panx1.

Indexed as

Amino Acid SequenceAnimalsCarbenoxoloneConnexinsCryoelectron MicroscopyHEK293 CellsHumansProtein Structure, TertiaryXenopus laevisXenopus ProteinsCarbenoxoloneConnexinsPanx1 protein, XenopusXenopus ProteinsATP releasecarbenoxoloneextracellular loopheptameric channelhumanion selectivitymolecular biophysicsneurosciencepannexinstructural biologyxenopus

Identifiers

PMID32048993
PMCPMC7108861
OpenAlexW3006320685

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.