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

The penultimate arginine of the carboxyl terminus determines slow desensitization in a P2X receptor from the cattle tick Boophilus microplus.

Molecular pharmacology - 1 Apr 2011

Bavan Selvan, Farmer Louise, Singh Shire K, Straub Volko A, Guerrero Felix D, Ennion Steven J

Abstract excerpt

P2X ion channels have been functionally characterized from a range of eukaryotes. Although these receptors can be broadly classified into fast and slow desensitizing, the molecular mechanisms underlying current desensitization are not fully understood. Here, we describe the characterization of a P2X receptor from the cattle tick Boophilus microplus (BmP2X) displaying extremely slow current kinetics, little...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Arginine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cattle

Share to Peptide Fragments

Share to Protein Structure, Tertiary

Share to Time Factors

Share to Xenopus laevis

Source

Open in PubMed Open full text

Identifiers

PMID: 21212138
DOI: 10.1124/mol.110.070037
PMCID: PMC3063728

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

The penultimate arginine of the carboxyl terminus determines slow desensitization in a P2X receptor from the cattle tick Boophilus microplus.PMID 21212138Read ↗

Identification of negative residues in the P2X3 ATP receptor ectodomain as structural determinants for desensitization and the Ca2+-sensing modulatory sites.Semantic proximity Read ↗

A hydrophobic residue in position 15 of the rP2X3 receptor slows desensitization and reveals properties beneficial for pharmacological analysis and high-throughput screening.Semantic proximity Read ↗

Structural insights into the allosteric inhibition of P2X4 receptorsSemantic proximity Read ↗

Identification of amino acids within the P2X2 receptor C-terminus that regulate desensitization.Semantic proximity Read ↗

Heteromultimerization modulates P2X receptor functions through participating extracellular and C-terminal subdomains.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 ↗

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

Agonist antagonist interactions at the rapidly desensitizing P2X3 receptor.Semantic proximity Read ↗

Involvement of the cysteine-rich head domain in activation and desensitization of the P2X1 receptor.Semantic proximity Read ↗

Structural insights into the human P2X1 receptor and ligand interactionsSemantic proximity Read ↗

Gated access to the pore of a P2X receptor: structural implications for closed-open transitions.Semantic proximity Read ↗

Identification of a distinct desensitisation gate in the ATP-gated P2X2 receptor.Semantic proximity Read ↗

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