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

Residues 155 and 348 contribute to the determination of P2X7 receptor function via distinct mechanisms revealed by single-nucleotide polymorphisms.

The Journal of biological chemistry - 11 Mar 2011

Bradley Helen J, Baldwin Jocelyn M, Goli G Ranjan, Johnson Brian, Zou Jie, Sivaprasadarao Asipu, Baldwin Stephen A, Jiang Lin-Hua

Abstract excerpt

P2X(7) receptors are important in mediating the physiological functions of extracellular ATP, and altered receptor expression and function have a causative role in the disease pathogenesis. Here, we investigated the mechanisms determining the P2X(7) receptor function by following two human single-nucleotide polymorphism (SNP) mutations that replace His-155 and Ala-348 in the human (h) P2X(7) receptor with the...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Amino Acid Substitution

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HEK293 Cells

Share to Models, Molecular

Share to Mutation, Missense

Share to Receptors, Purinergic P2X7

Share to Zebrafish

Source

Open in PubMed Open full text

Identifiers

PMID: 21205829
DOI: 10.1074/jbc.M110.211284
PMCID: PMC3048704

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

Residues 155 and 348 contribute to the determination of P2X7 receptor function via distinct mechanisms revealed by single-nucleotide polymorphisms.PMID 21205829Read ↗

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 Val/Ile87 residue in the extracellular domain in agonist-induced current responses of the human and rat P2X7 receptors.Semantic proximity Read ↗

Single nucleotide polymorphisms that were identified in affective mood disorders affect ATP-activated P2X7 receptor functions.Semantic proximity Read ↗

Non-synonymous single nucleotide polymorphisms in the P2X receptor genes: association with diseases, impact on receptor functions and potential use as diagnosis biomarkers.Semantic proximity Read ↗

Significance of P2X7 receptor variants to human health and disease.Semantic proximity Read ↗

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

Gain and loss of function of P2X7 receptors: mechanisms, pharmacology and relevance to diabetic neuropathic pain.Semantic proximity Read ↗

A P2RX7 single nucleotide polymorphism haplotype promotes exon 7 and 8 skipping and disrupts receptor function.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 ↗

A His-155 to Tyr polymorphism confers gain-of-function to the human P2X7 receptor of human leukemic lymphocytes.Semantic proximity Read ↗

An Ile-568 to Asn polymorphism prevents normal trafficking and function of the human P2X7 receptor.Semantic proximity Read ↗

Functional differences between ATP-gated human and rat P2X3 receptors are caused by critical residues of the intracellular C-terminal domain.Semantic proximity Read ↗

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