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Molecular properties of P2X receptors
Pflügers Archiv - European Journal of Physiology, 2006P2X 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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P2X receptors in peripheral neurons
Progress in Neurobiology, 2001P2X 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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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 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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Seminars in Neuroscience, 1996
Abstract Six P2X receptor subunits are currently known, encoded on different genes. The proteins deduced from their cDNAs have 379 to 472 amino acids; they are 36–48% identical. They are thought to have two transmembrane segments, with most of the protein forming a large extracellular loop. In-situ hybridization shows a widespread tissue distribution
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Abstract Six P2X receptor subunits are currently known, encoded on different genes. The proteins deduced from their cDNAs have 379 to 472 amino acids; they are 36–48% identical. They are thought to have two transmembrane segments, with most of the protein forming a large extracellular loop. In-situ hybridization shows a widespread tissue distribution
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Science's STKE, 2007
Fountain et al . report the identification and characterization of an ATP receptor in Dictyostelium discoideum that is homologous to vertebrate P2X receptors. When heterologously expressed in the human embryonic kidney (HEK) cell line, the protein was localized to the plasma membrane, was ...
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Fountain et al . report the identification and characterization of an ATP receptor in Dictyostelium discoideum that is homologous to vertebrate P2X receptors. When heterologously expressed in the human embryonic kidney (HEK) cell line, the protein was localized to the plasma membrane, was ...
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The Cytolytic P2Z Receptor for Extracellular ATP Identified as a P2X Receptor (P2X7)
Science, 1996A. Surprenant +4 more
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2019
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P2X receptors in cancer growth and progression.
Biochemical Pharmacology, 2020F. Di Virgilio +2 more
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