Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A permeant regulating its permeation pore: inhibition of pannexin 1 channels by ATP.

American journal of physiology. Cell physiology - 1 Feb 2009

Qiu Feng, Dahl Gerhard

Abstract excerpt

Pannexin 1 forms a large membrane channel that, based on its biophysical properties and its expression pattern, is a prime candidate to represent an ATP release channel. Pannexin 1 channel activity is potentially deleterious for cells as indicated by its involvement in the P2X7 death complex. Her...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell Membrane Permeability
Share to Connexins
Share to Feedback, Physiological

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Membrane Potentials

Share to Patch-Clamp Techniques

Share to Receptors, Purinergic P2

Share to Receptors, Purinergic P2X7

Share to Xenopus

Source

Open in PubMed Open full text

Identifiers

PMID: 18945939
DOI: 10.1152/ajpcell.00433.2008
PMCID: PMC2643853

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-18945939-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A permeant regulating its permeation pore: inhibition of pannexin 1 channels by ATP.PMID 18945939Read ↗

The Pannexin1 membrane channel: distinct conformations and functions.Semantic proximity Read ↗

Pharmacological characterization of pannexin-1 currents expressed in mammalian cells.Semantic proximity Read ↗

Structures of human pannexin 1 reveal ion pathways and mechanism of gating.Semantic proximity Read ↗

<i>Panx1</i> channels promote both anti- and pro-seizure-like activities in the zebrafish via <i>p2rx7</i> receptors and ATP signalingSemantic proximity Read ↗

Allosteric modulation of ATP-gated P2X receptor channels.Semantic proximity Read ↗

Splice variants of the P2X7 receptor reveal differential agonist dependence and functional coupling with pannexin-1.Semantic proximity Read ↗

Cardiomyocyte ATP release through pannexin 1 aids in early fibroblast activation.Semantic proximity Read ↗

A metastasis-associated pannexin-1 mutant (Panx11-89) forms a minimalist ATP release channel.Semantic proximity Read ↗

Characteristics of P2X7 receptors from human B lymphocytes expressed in Xenopus oocytes.Semantic proximity Read ↗

A novel heterozygous missense variant of PANX1 causes human oocyte death and female infertilitySemantic proximity Read ↗

Structural basis of ATP release and ion selectivity in Pannexin1 channelsSemantic proximity Read ↗

Mutational effects of Pannexin 1 R217H depend on the carboxyl-terminus.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.