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Pharmacology of P2X channels

Pflügers Archiv - European Journal of Physiology, 2006
Significant progress in understanding the pharmacological characteristics and physiological importance of homomeric and heteromeric P2X channels has been achieved in recent years. P2X channels, gated by ATP and most likely trimerically assembled from seven known P2X subunits, are present in a broad distribution of tissues and are thought to play an ...
Michael Patrick Dillon   +4 more
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Signaling at Purinergic P2X Receptors

Annual Review of Physiology, 2009
P2X receptors are membrane cation channels gated by extracellular ATP. Seven P2X receptor subunits (P2X1-7) are widely distributed in excitable and nonexcitable cells of vertebrates. They play key roles in inter alia afferent signaling (including pain), regulation of renal blood flow, vascular endothelium, and inflammatory responses.
Surprenant, Annmarie, Alan North, R.
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P2X Receptors and Nociception

Pharmacological Reviews, 2001
The potential importance for nociception of P2X receptors, the ionotropic receptors activated by ATP, is underscored by the variety of pain states in which this endogenous ligand can be released. Several important findings have been made recently indicating that P2X receptors can be involved in pain mechanisms both centrally and in the periphery.
B A, Chizh, P, Illes
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Synaptic P2X receptors

Current Opinion in Neurobiology, 2001
Over the past two years, ATP has clearly been shown to act as a co-transmitter with GABA, glycine and probably glutamate in the central nervous system. Our understanding of the ATP-gated P2X receptors is progressing rapidly, and the pharmacology, stoichiometry and subunit combinations of heteropolymeric P2X channels has been substantially elucidated.
Robertson, SJ   +3 more
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P2X Receptors and Inflammation

Current Medicinal Chemistry, 2015
Until recently, P2X receptors have not received much attention in the context of immunology and inflammation. While this is justified to a certain extent for P2X1, P2X2, P2X3, P2X5 and P2X6, which still await identification of a convincing role in the pathophysiology of immune cells, it is clearly not any more the case for P2X4 and even more so for ...
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Pharmacology of Cloned P2X Receptors

Annual Review of Pharmacology and Toxicology, 2000
There are seven P2X receptor cDNAs currently known. Six homomeric (P2X1, P2X2, P2X3, P2X4, P2X5, P2X7) and three heteromeric (P2X2/P2X3, P2X4/P2X6, P2X1/P2X5) P2X receptor channels have been characterized in heterologous expression systems. Homomeric P2X1 and P2X3 receptors are readily distinguishable by their rapid desensitization, the agonist action
North, R. Alan, Surprenant, Annmarie
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P2X receptors and trigeminal neuralgia

NeuroReport, 2019
There is currently no effective cure for trigeminal neuralgia (TN) - a relatively common disease that causes long-term pain in patients. Previous research has shown that ionotropic ATP signaling through excitatory and calcium-permeable P2X receptor channels plays a critical role in pathological pain generation and maintenance.
Guo-Yong Xue   +3 more
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P2X receptor ligands and pain

Expert Opinion on Therapeutic Patents, 2006
P2X receptors belong to a superfamily of ligand-gated ion channels that conduct the influx of Ca(2+), Na(+) and K(+) cations following activation by extracellular nucleotides such as ATP. Molecular cloning studies have identified seven subunits, namely P2X(1-7), that share approximately 40 - 50% identity in amino acid sequences within the subfamily ...
Richard J. Perner   +3 more
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Molecular Structure of P2X Receptors

Current Topics in Medicinal Chemistry, 2004
P2X receptors are ligand-gated ion channels that transduce many of the physiological effects of extracellular ATP. There has been a dramatic increase in awareness of these receptors over the past 5 or so years, in great part due to their molecular cloning and characterization.
Terrance M. Egan   +2 more
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Molecular properties of P2X receptors

Pflügers Archiv - European Journal of Physiology, 2006
P2X receptors for adenosine tri-phosphate (ATP) are a distinct family of ligand-gated cation channels with two transmembrane domains, intracellular amino and carboxy termini and a large extracellular ligand binding loop. Seven genes (P2X(1-7)) have been cloned and the channels form as either homo or heterotrimeric channels giving rise to a wide range ...
Roberts, Jonathan A.   +6 more
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