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

Mutational Analysis of the Conserved Cysteines of the Rat P2X<sub>2</sub>Purinoceptor

15 May 2002

Abstract excerpt

P2X receptors are ATP-gated cation channels that are widely expressed in the brain. The extracellular domains of all seven P2X receptors contain 10 conserved cysteines, which could form disulfide bonds or binding sites for transition metals that modulate P2X receptors. To test whether these cysteines are critical for receptor function, we studied wild-type rat P2X(2) receptors and 10 mutant P2X(2) receptors, each...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine and Purinergic Signaling
Share to Neurological Complications and Syndromes
Share to Neuroscience of respiration and sleep

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 12019306
DOI: 10.1523/jneurosci.22-10-03873.2002

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutational Analysis of the Conserved Cysteines of the Rat P2X<sub>2</sub>PurinoceptorPMID 12019306Read ↗

Conserved cysteine residues in the extracellular loop of the human P2X(1) receptor form disulfide bonds and are involved in receptor trafficking to the cell surface.Semantic proximity Read ↗

Cysteine substitution mutagenesis and the effects of methanethiosulfonate reagents at P2X2 and P2X4 receptors support a core common mode of ATP action at P2X receptors.Semantic proximity Read ↗

High potency zinc modulation of human P2X2 receptors and low potency zinc modulation of rat P2X2 receptors share a common molecular mechanism.Semantic proximity Read ↗

Conserved ectodomain cysteines are essential for rat P2X7 receptor trafficking.Semantic proximity Read ↗

An intersubunit zinc binding site in rat P2X2 receptors.Semantic proximity Read ↗

Conserved extracellular cysteines differentially regulate the inhibitory effect of ethanol in rat P2X4 receptors.Semantic proximity Read ↗

Functional identification of close proximity amino acid side chains within the transmembrane-spanning helixes of the P2X2 receptor.Semantic proximity Read ↗

Histidine 140 plays a key role in the inhibitory modulation of the P2X4 nucleotide receptor by copper but not zinc.Semantic proximity Read ↗

Molecular Structure and Regulation of P2X Receptors With a Special Emphasis on the Role of P2X2 in the Auditory System.Semantic proximity Read ↗

Tyrosine 288 in the extracellular domain of the human P2X7 receptor is critical for receptor function revealed by structural modeling and site-directed mutagenesis.Semantic proximity Read ↗

Contribution of P2X1 receptor intracellular basic residues to channel properties.Semantic proximity Read ↗

Identification of residues in the first transmembrane domain of the P2X7 that regulates receptor trafficking, sensitization, and dye uptake function.Semantic proximity Read ↗

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