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The Cytolytic P2Z Receptor for Extracellular ATP Identified as a P2X Receptor (P2X7)
TLDR
The P2X7 (or P2Z) receptor is a bifunctional molecule that could function in both fast synaptic transmission and the ATP-mediated lysis of antigen-presenting cells. Expand
Pannexin‐1 mediates large pore formation and interleukin‐1β release by the ATP‐gated P2X7 receptor
TLDR
Pannexin‐1, a recently described mammalian protein that functions as a hemichannel when ectopically expressed, is identified as this dye‐uptake pathway and signalling through pannexin•1 is required for processing of caspase‐1 and release of mature IL‐1β induced by P2X7 receptor activation. Expand
Cloning OF P2X5 and P2X6 receptors and the distribution and properties of an extended family of ATP-gated ion channels
TLDR
The functional properties and tissue distribution of these six P2X receptors indicate new roles for ATP-gated ion channels, particularly in brain and spinal cord. Expand
Coexpression of P2X2 and P2X3 receptor subunits can account for ATP-gated currents in sensory neurons
TLDR
The cloning of a complementary DNA from rat dorsal root ganglia that had properties dissimilar to those of sensory neurons is reported, indicating that ATP-gated channels of sensory neuron may form by a specific heteropolymerization of P2X receptor subunits. Expand
Pharmacology of cloned P2X receptors.
TLDR
The heteromeric P2X2/P2X3 receptor resembles P2 X2 in slow desensitization kinetics and potentiation by low pH and is similar to P2x3 with respect to agonism by alpha beta methyleneATP and block by 2',3'-O-(2,4,6-trinitrophenyl)-ATP. Expand
Brilliant blue G selectively blocks ATP-gated rat P2X(7) receptors.
TLDR
It is shown that Coomassie Brilliant Blue G selectively inhibits P2X(7) receptors with nanomolar affinity, which is at least 1000-fold more potent at rat P2x( 7) receptors than atRat P2 X(4) receptors. Expand
An antagonist‐insensitive P2X receptor expressed in epithelia and brain.
TLDR
A cDNA was cloned which encodes a new ATP‐gated ion channel (P2X4 receptor) and an amino acid residue involved in antagonist binding is identified, and a new phenotype for ATP responses at P2X receptors is introduced–insensitivity to currently known antagonists. Expand
Effects of divalent cations, protons and calmidazolium at the rat P2X7 receptor
TLDR
Calmidazolium can block activation of the ionic channel but this does not prevent the formation of the large permeabilizing pore, and results suggest that these divalent cations and protons all act primarily as allosteric modulators to alter the affinity of ATP binding to the P2X7 receptor. Expand
Trinitrophenyl-substituted nucleotides are potent antagonists selective for P2X1, P2X3, and heteromeric P2X2/3 receptors.
TLDR
It is found that the 2', 3'-O-(2,4,6-trinitrophenyl)-substituted analogs of ATP are selective and potent antagonists at some but not all P2X receptors. Expand
Signaling at purinergic P2X receptors.
TLDR
The evidence for key roles of P2X receptors in inter alia afferent signaling, regulation of renal blood flow, vascular endothelium, and inflammatory responses is summarized, emphasizing experimental work with selective receptor antagonists or with knockout mice. Expand
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