Evidence map›Paper›PMID 33835130›Full record

ArticleThe Journal of general physiology2021

Structure versus function: Are new conformations of pannexin 1 yet to be resolved?

Carsten Mim, Guy Perkins, Gerhard Dahl

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

24 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Contribution of pannexin channels to afterimage signals in the amphibian retina.American journal of physiology. Cell physiology · 2025
    Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Structure-Based Design and Synthesis of StapledJournal of medicinal chemistry · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

3 authors at 3 institutions in 2 countries.

Carsten MimDepartment of Biomedical Engineering and Health Systems Royal Institute of Technology, Huddinge, Sweden.
Guy PerkinsNational Center for Microscopy and Imaging Research, University of California, San Diego School of Medicine, La Jolla, CA.
Gerhard DahlDepartment of Physiology, University of Miami School of Medicine, Miami, FL.
KTH Royal Institute of Technology · SEUniversity of California San Diego · USUniversity of Miami · US

Funding

National Center for Microscopy and Imaging Research: A BRAIN Technology Integration and Dissemination ResourceU24NS120055 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ELLISMAN, MARK H · 2021 to 2025
$5.4M
The National Center for Microscopy and Imaging Research, a Community-wide Scientific ResourceR24GM137200 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ELLISMAN, MARK H · 2020 to 2022
$3.0M
Functional and structural analysis of the closed and two open states of the Panx1 channel.R56HL136291 · NHLBI · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI DAHL, GERHARD P, LOCKLESS, STEVE W · 2018 to 2018
$587k
NHLBI NIH HHS R56 HL136291NIGMS NIH HHS R24 GM137200NINDS NIH HHS U24 NS120055
6 · The paper itself

Abstract

Pannexin 1 (Panx1) plays a decisive role in multiple physiological and pathological settings, including oxygen delivery to tissues, mucociliary clearance in airways, sepsis, neuropathic pain, and epilepsy. It is widely accepted that Panx1 exerts its role in the context of purinergic signaling by providing a transmembrane pathway for ATP. However, under certain conditions, Panx1 can also act as a highly selective membrane channel for chloride ions without ATP permeability. A recent flurry of publications has provided structural information about the Panx1 channel. However, while these structures are consistent with a chloride selective channel, none show a conformation with strong support for the ATP release function of Panx1. In this Viewpoint, we critically assess the existing evidence for the function and structure of the Panx1 channel and conclude that the structure corresponding to the ATP permeation pathway is yet to be determined. We also list a set of additional topics needing attention and propose ways to attain the large-pore, ATP-permeable conformation of the Panx1 channel.

Indexed as

ConnexinsNerve Tissue ProteinsAdenosine TriphosphateIon ChannelsSignal TransductionAdenosine TriphosphateConnexinsIon ChannelsNerve Tissue Proteins

Identifiers

PMID33835130
PMCPMC8042604
OpenAlexW3150227425

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.