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

Contribution of individual subunits to the multimeric P2X(2) receptor: estimates based on methanethiosulfonate block at T336C.

Molecular pharmacology - 1 Nov 1999

Stoop R, Thomas S, Rassendren F, Kawashima E, Buell G, Surprenant A, North R A

Abstract excerpt

P2X receptors are membrane proteins that incorporate a cation-selective ion channel that can be opened by the binding of extracellular ATP. They associate as hetero- and homo-multimers of currently unknown stoichiometry. In this study, we have used Xenopus laevis oocytes to express rat P2X(2) receptor subunits, which carry a cysteine mutation at position 336. ATP-induced currents at this mutant receptor subunit...

Read the complete abstract on PubMed

Topics

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

Share to DNA, Complementary
Share to Mesylates

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Oocytes

Share to Receptors, Purinergic P2

Share to Xenopus laevis

Source

Identifiers

PMID: 10531403
DOI: 10.1124/mol.56.5.973

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Contribution of individual subunits to the multimeric P2X(2) receptor: estimates based on methanethiosulfonate block at T336C.PMID 10531403Read ↗

ATP binding site mutagenesis reveals different subunit stoichiometry of functional P2X2/3 and P2X2/6 receptors.Semantic proximity Read ↗

Activation of trimeric P2X2 receptors by fewer than three ATP molecules.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 ↗

P2X5 Subunit Assembly Requires Scaffolding by the Second Transmembrane Domain and a Conserved AspartateSemantic proximity Read ↗

P2X2 and P2X5 subunits define a new heteromeric receptor with P2X7-like properties.Semantic proximity Read ↗

Voltage- and ATP-dependent structural rearrangements of the P2X2 receptor associated with the gating of the pore.Semantic proximity Read ↗

Occupancy of a single anesthetic binding pocket is sufficient to enhance glycine receptor function.Semantic proximity Read ↗

Differential α4(+)/(-)β2 Agonist-binding Site Contributions to α4β2 Nicotinic Acetylcholine Receptor Function within and between Isoforms.Semantic proximity Read ↗

Conformational flexibility of the agonist binding jaw of the human P2X3 receptor is a prerequisite for channel opening.Semantic proximity Read ↗

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 ↗

Mutational Analysis of the Conserved Cysteines of the Rat P2X<sub>2</sub>PurinoceptorSemantic proximity Read ↗

Flexible subunit stoichiometry of functional human P2X2/3 heteromeric receptors.Semantic proximity Read ↗

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