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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 ...
Char-Chang, Shieh   +3 more
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Purine Ionotropic (P2X) Receptors

Current Pharmaceutical Design, 2007
Purinergic signaling is involved in the proper functioning of virtually all organs of the body. Although in some cases purines have a major influence on physiological functions (e.g. thrombocyte aggregation), more often they are just background modulators contributing to fine tuning of biological events.
L, Köles, S, Fürst, P, Illes
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P2X Receptor Activation

2017
Extracellular ATP-gated P2X receptors are trimeric non-selective cation channels important for many physiological events including immune response and neural transmission. These receptors belong to a unique class of ligand-gated ion channels composed of only six transmembrane helices and a relatively small extracellular domain that harbors three ATP ...
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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
openaire   +3 more sources

P2X Receptors in Epithelia

2015
P2X receptors are ubiquitously expressed in all epithelial tissues, but their functional roles are less well studied. Here we review the current state of knowledge by focusing on functional effects of P2X receptor in secretory and in absorptive tissues. In glandular tissue like the parotid gland, basolateral P2X receptors stimulate ion secretion via an
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P2X receptors in peripheral neurons

Progress in Neurobiology, 2001
P2X receptors are a family of ligand-gated ion channels, activated by extracellular ATP. The seven subunits cloned (P2X1-7) can assemble to form homomeric and heteromeric receptors. Peripheral neurons of neural crest origin (e.g. those in dorsal root, trigeminal, sympathetic and enteric ganglia) and placodal origin (e.g.
P M, Dunn, Y, Zhong, G, Burnstock
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Homology Modeling of P2X Receptors

2019
Since the X-ray structure of the zebra fish P2X4 receptor in the closed state was published in 2009 homology modeling has been used to generate structural models for P2X receptors. In this chapter, we outline how to use the MODELLER software to generate such structural models for P2X receptors whose structures have not been solved yet.
Anastasios, Stavrou   +2 more
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P2X Receptors in Health and Disease

2011
Seven P2X receptor subunits have been cloned which form functional homo- and heterotrimers. These are cation-selective channels, equally permeable to Na(+) and K(+) and with significant Ca(2+) permeability. The three-dimensional structure of the P2X receptor is described.
G, Burnstock, C, Kennedy
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P2X Receptors and Pain

2013
P2X receptors are ATP-gated channels and form the third major family of ligand-gated channels. Unlike other neurotransmitter-gated channels, P2X receptors have a widespread distribution outside the brain and are involved in many physiological functions. A main function associated to P2X receptors is chronic pain.
François Rassendren, Lauriane Ulmann
openaire   +1 more source

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