Evidence map›Paper›PMID 23499662›Full record

ReviewNeuropharmacology2013

The bizarre pharmacology of the ATP release channel pannexin1.

Gerhard Dahl, Feng Qiu, Junjie Wang

Open access · greenAbstract readReview
In one paragraph

Review in Neuropharmacology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

77 citing papers in PubMed, 128 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Structure-Based Design and Synthesis of StapledJournal of medicinal chemistry · 2023
    Article
  15. Meningeal P2X7 Signaling Mediates Migraine-Related Intracranial Mechanical Hypersensitivity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023
    Article
  16. Article
  17. Article
  18. Article
  19. Pharmacology of pannexin channels.Current opinion in pharmacology · 2023
    Review
  20. Article

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

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 1 institution in 1 country.

Gerhard DahlDepartment of Physiology and Biophysics, University of Miami, School of Medicine, PO Box 016430, Miami, FL 33101, USA. Electronic address: gdahl@miami.edu.
Feng QiuDepartment of Physiology and Biophysics, University of Miami, School of Medicine, PO Box 016430, Miami, FL 33101, USA.
Junjie WangDepartment of Physiology and Biophysics, University of Miami, School of Medicine, PO Box 016430, Miami, FL 33101, USA.
University of Miami · US

Funding

FORMATION OF CELL-CELL CHANNELSR01GM048610 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI DAHL, GERHARD P · 1993 to 2010
$2.8M
NIGMS NIH HHS R01 GM048610
6 · The paper itself

Abstract

Pannexins were originally thought to represent a second and redundant family of gap junction proteins in addition to the well characterized connexins. However, it is now evident that pannexins function as unapposed membrane channels and the major role of Panx1 is that of an ATP release channel. Despite the contrasting functional roles, connexins, innexins and pannexins share pharmacological properties. Most gap junction blockers also attenuate the function of Panx1, including carbenoxolone, mefloquine and flufenamic acid. However, in contrast to connexin based gap junction channels, Panx1 channel activity can be attenuated by several groups of drugs hitherto considered very specific for other proteins. The drugs affecting Panx1 channels include several transport inhibitors, chloride channel blockers, mitochondrial inhibitors, P2X7 receptor ligands, inflammasome inhibitors and malaria drugs. These observations indicate that Panx1 may play an extended role in a wider spectrum of physiological functions. Alternatively, Panx1 may share structural domains with other proteins, not readily revealed by sequence alignments. This article is part of the Special Issue Section entitled 'Current Pharmacology of Gap Junction Channels and Hemichannels'.

Indexed as

Adenosine TriphosphateAnimalsConnexinsGap JunctionsHumansMembrane PotentialsMembrane Transport ModulatorsAdenosine TriphosphateConnexinsMembrane Transport Modulators2-(trimethylammonium)ethyl methanethiosulfonate3′-O-(4-benzoyl)benzoyl adenosine 5′-triphosphate5-nitro-2-(3-phenylpropylamino)benzoic acidApoptosisBzATPcarbenoxoloneCBXDIDSdisodium 4,4′-diisothiocyanatostilbene-2,2′-disulfonatedisodium 4-acetamido-4′-isothiocyanato-stilben-2,2′-disulfonateFFAflufenamic acidGAGap junctionGlibenclamideglycyrrethinic acidIAA-94IL-1bindanyloxyacetic acid 94Inflammasomeinterleukin-1bMalariamaleimidobutyrylbiocytinMBBMitochondriumMTSETNPPBPannexinProbenecidSITSTCEPtris(2-carboxyethyl)phosphine

Identifiers

PMID23499662
PMCPMC3711969
OpenAlexW1999673165

What OpenQuestion holds

Textmetadata
LicenceTDM
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.