Evidence map›Paper›PMID 28389204›Full record

ReviewBiochimica et biophysica acta. Biomembranes2018

Interactions of Pannexin1 channels with purinergic and NMDA receptor channels.

Shuo Li, Ivana Bjelobaba, Stanko S Stojilkovic

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Biomembranes, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

9 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Review
  3. Intra-carotid body inter-cellular communication.Journal of the Royal Society of New Zealand · 2023
    Review
  4. Review
  5. Review
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  7. Article
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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 3 countries.

Shuo LiTianjin Key Laboratory of Animal and Plant Resistance, College of Life Sciences, Tianjin Normal University, Tianjin 300387, China.
Ivana BjelobabaInstitute for Biological Research "Sinisa Stankovic", University of Belgrade, 11000 Belgrade, Serbia.
Stanko S StojilkovicEunice Kennedy Shriver National Institute of Child Health and Human Development, NIH, Bethesda, MD 20892, USA. Electronic address: stojilks@mail.nih.gov.
Eunice Kennedy Shriver National Institute of Child Health and Human Development · USTianjin Normal University · CNUniversity of Belgrade · RS

Funding

Intracellular Signaling In Endocrine CellsZIAHD000195 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI STOJILKOVIC, STANKO S. · 2009 to 2025
$18.8M
INTRACELLULAR SIGNALING IN ENDOCRINE CELLSZ01HD000195 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI STOJILKOVIC, STANKO S. · 1994 to 2008
$2.4M
Intramural NIH HHS Z01 HD000195Intramural NIH HHS ZIA HD000195
6 · The paper itself

Abstract

Pannexins are a three-member family of vertebrate plasma membrane spanning molecules that have homology to the invertebrate gap junction forming proteins, the innexins. However, pannexins do not form gap junctions but operate as plasma membrane channels. The best-characterized member of these proteins, Pannexin1 (Panx1) was suggested to be functionally associated with purinergic P2X and N-methyl-D-aspartate (NMDA) receptor channels. Activation of these receptor channels by their endogenous ligands leads to cross-activation of Panx1 channels. This in turn potentiates P2X and NMDA receptor channel signaling. Two potentiation concepts have been suggested: enhancement of the current responses and/or sustained receptor channel activation by ATP released through Panx1 pore and adenosine generated by ectonucleotidase-dependent dephosphorylation of ATP. Here we summarize the current knowledge and hypotheses about interactions of Panx1 channels with P2X and NMDA receptor channels. This article is part of a Special Issue entitled: Gap Junction Proteins edited by Jean Claude Herve.

Indexed as

AdenosineAdenosine TriphosphateAnimalsConnexinsHumansNerve Tissue ProteinsReceptors, N-Methyl-D-AspartateReceptors, Purinergic P2XAdenosineAdenosine TriphosphateConnexinsNerve Tissue ProteinsPANX1 protein, humanReceptors, N-Methyl-D-AspartateReceptors, Purinergic P2XATPMegaporeNMDA receptorsP2X receptorsPannexin1Purinergic receptors

Identifiers

PMID28389204
PMCPMC5628093
OpenAlexW2605296449

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.