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1 ionally interacting purinergic receptor: the P2X2 receptor.
2 s little to the permeation properties of the P2X2 receptor.
3 sstalk occurs between alpha6beta4 nAChRs and P2X2 receptors.
4 l openings that were never seen in wild-type P2X2 receptors.
5 e key components of the zinc binding site in P2X2 receptors.
6 els incorporating the properties of P2X1 and P2X2 receptors.
7 -1.5) but was significantly higher (2.5) for P2X2 receptors.
8 epend on the intracellular C terminus of the P2X2 receptors.
9 neurons are likely to express predominantly P2X2 receptors.
10 h half-maximal concentrations of 5 mM at the P2X2 receptor, 89 mM at the P2X3 receptor and 15 mM at b
12 h frequent mating over days, suggesting that P2X2 receptor adds a selection advantage under these con
15 cells stably transfected with either P2X1 or P2X2 receptors and by absorption controls with the cogna
16 he cranial neural crest and does not express P2X2 receptors and fails to respond to alpha,beta-methyl
17 a6beta4-containing (alpha6beta4*) nAChRs and P2X2 receptors and/or P2X3 receptors have not been fully
19 sures of P2X receptor mobility and show that P2X2 receptors are mobile ATP sensors, sampling more of
20 el, since ATP currents evoked at recombinant P2X2 receptors are potentiated by lowering extracellular
23 robe the location of this zinc binding site, P2X2 receptors bearing mutations of the histidines at po
24 of removing N-linked glycosylation from the P2X2 receptor by using two different approaches, tunicam
26 essing either wild-type or functional mutant P2X2 receptors containing a cysteine substitution in or
27 at a significant component of TTS represents P2X2 receptor-dependent purinergic hearing adaptation th
30 sequential expression of the P2X5, P2Y1, and P2X2 receptors during the process of muscle regeneration
35 is a noncompetitive antagonist at wild-type P2X2 receptors, had a pronounced agonist action at both
36 hough the electrophysiological properties of P2X2 receptors have been extensively studied, little is
39 In the present study, the distribution of P2X2 receptor in the rat hypothalamus was studied with i
40 spontaneous gating, and rectification of rat P2X2 receptor in which polar and charged residues of the
41 lamp recordings to track quantum dot-labeled P2X2 receptors in the dendrites of rat hippocampal neuro
44 the unspliced, 472 amino acid isoform of the P2X2 receptor, inactivation required membrane disruption
45 clude that the C-terminal splice site of the P2X2 receptor is located within a region that is critica
48 dge, a comparison of the closed and open rat P2X2 receptor models revealed a significant rearrangemen
49 els likely activates the broadly distributed P2X2 receptors on epithelial cells lining the endolympha
50 bout the plasma membrane lateral mobility of P2X2 receptors or whether receptor mobility is regulated
52 f ionic modulation that is characteristic of P2X2 receptors: potentiation by acidification and extrac
53 of the two transmembrane domains of the rat P2X2 receptor protein, and is likely to be close to the
54 direct evidence that calcium influx through P2X2 receptors results in the activation of the MAP kina
55 inc over the range of 2-100 muM, whereas rat P2X2 receptors (rP2X2) are strongly potentiated over the
56 amino-terminal region with the corresponding P2X2 receptor section (P2X7-2Nbeta) gave responses that
58 ere we describe null mutant mice lacking the P2X2 receptor subunit (P2X2-/-) and double mutant mice l
59 asparagine residues 182, 239, and 298 of the P2X2 receptor subunit by showing that the protein is gly
61 HEK-293 cells stably transfected with the P2X2 receptor subunit showed little or no response to AT
62 n mice null for the P2RX2 gene (encoding the P2X2 receptor subunit), sustained 85-dB noise failed to
64 w that ATP-gated ion channels assembled from P2X2 receptor subunits in the cochlea are necessary for
65 rostral ventrolateral medulla (VLM) express P2X2 receptor subunits of the ATP-gated ion channel, sin
67 introducing pairs of cysteines into the rat P2X2 receptor that might form disulfide bonds within or
70 We have used chimeras between human P2X1 and P2X2 receptors to address the contribution of the extrac
71 nnels that physically couple with purinergic P2X2 receptors to trigger a functional cross-inhibition
75 study, we used homology modeling of the rat P2X2 receptor with the zebrafish P2X4 X-ray template to
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