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1 s little to the permeation properties of the P2X2 receptor.
2 ionally interacting purinergic receptor: the P2X2 receptor.
3 epend on the intracellular C terminus of the P2X2 receptors.
4 sstalk occurs between alpha6beta4 nAChRs and P2X2 receptors.
5 l openings that were never seen in wild-type P2X2 receptors.
6 e key components of the zinc binding site in P2X2 receptors.
7 els incorporating the properties of P2X1 and P2X2 receptors.
8 -1.5) but was significantly higher (2.5) for P2X2 receptors.
9  neurons are likely to express predominantly P2X2 receptors.
10 X1 subunits to the equivalent amino acids on P2X2 receptors.
11 t EPAC is an important regulator of P2X1 and P2X2 receptors.
12 h half-maximal concentrations of 5 mM at the P2X2 receptor, 89 mM at the P2X3 receptor and 15 mM at b
13 ion, calcium permeability, and dye uptake as P2X2 receptors activated by ATP.
14 h frequent mating over days, suggesting that P2X2 receptor adds a selection advantage under these con
15                                              P2X2 receptors also functionally interact with alpha6bet
16                            Zinc binds to rat P2X2 receptors and acts as an allosteric modulator, pote
17 cells stably transfected with either P2X1 or P2X2 receptors and by absorption controls with the cogna
18 he cranial neural crest and does not express P2X2 receptors and fails to respond to alpha,beta-methyl
19 a6beta4-containing (alpha6beta4*) nAChRs and P2X2 receptors and/or P2X3 receptors have not been fully
20                                              P2X2 receptors are ATP-gated ion channels widely express
21 sures of P2X receptor mobility and show that P2X2 receptors are mobile ATP sensors, sampling more of
22 el, since ATP currents evoked at recombinant P2X2 receptors are potentiated by lowering extracellular
23 surface, indicating that the nonglycosylated P2X2 receptors are retained inside the cell.
24                         ATP-gated ionotropic P2X2 receptors are widely expressed in neurons.
25  taste neurons heterologously expressing rat P2X2 receptors as a screening platform.
26 robe the location of this zinc binding site, P2X2 receptors bearing mutations of the histidines at po
27  of removing N-linked glycosylation from the P2X2 receptor by using two different approaches, tunicam
28                     The slowly desensitizing P2X2 receptor can be activated by free ATP, but MgATP(2-
29                                Activation of P2X2 receptor channels by extracellular ATP is thought t
30 essing either wild-type or functional mutant P2X2 receptors containing a cysteine substitution in or
31 at a significant component of TTS represents P2X2 receptor-dependent purinergic hearing adaptation th
32 ing commonly described as non-desensitizing, P2X2 receptors do desensitize or inactivate.
33 distances in the transmembrane domain of the P2X2 receptor during activation.
34 sequential expression of the P2X5, P2Y1, and P2X2 receptors during the process of muscle regeneration
35             Similar results were obtained at P2X2 receptors even without previous agonist tethering:
36 , and to confirm its agonist activity on rat P2X2 receptors expressed in human cells.
37                                   Subsequent P2X2 receptor expression on newly formed myotubes showed
38       These data indicate that modulation of P2X2 receptor function, such as that evoked by acidifica
39  current is not detected in mice lacking the P2X2 receptor gene (P2rx2(-/-)).
40  is a noncompetitive antagonist at wild-type P2X2 receptors, had a pronounced agonist action at both
41 hough the electrophysiological properties of P2X2 receptors have been extensively studied, little is
42                                        Human P2X2 receptors (hP2X2) are strongly inhibited by zinc ov
43 nant expression and functional gating of the P2X2 receptor in baker's yeast.
44 of the first transmembrane domain of the rat P2X2 receptor in cation permeability and flux.
45    In the present study, the distribution of P2X2 receptor in the rat hypothalamus was studied with i
46 spontaneous gating, and rectification of rat P2X2 receptor in which polar and charged residues of the
47 lamp recordings to track quantum dot-labeled P2X2 receptors in the dendrites of rat hippocampal neuro
48 to Cd(2+) at substituted cysteines in TM2 of P2X2 receptors in the open and closed states.
49                  The propyl-MTS did not open P2X2 receptors in which the Val(48) side chain was remov
50 the unspliced, 472 amino acid isoform of the P2X2 receptor, inactivation required membrane disruption
51                   Each subunit of a trimeric P2X2 receptor is composed of intracellular N and C termi
52 clude that the C-terminal splice site of the P2X2 receptor is located within a region that is critica
53                 We find that plasma membrane P2X2 receptor lateral mobility in dendrites is heterogen
54 drites of rat hippocampal neurons to explore P2X2 receptor mobility and its regulation.
55 dge, a comparison of the closed and open rat P2X2 receptor models revealed a significant rearrangemen
56 els likely activates the broadly distributed P2X2 receptors on epithelial cells lining the endolympha
57 ults demonstrate that the loss of functional P2X2 receptors or distinct alterations of its functional
58 bout the plasma membrane lateral mobility of P2X2 receptors or whether receptor mobility is regulated
59                                          The P2X2 receptor (P2X2R) is a member of the ATP-gated ion c
60                                          The P2X2 receptor (P2X2R) is a slowly desensitizing adenosin
61 f ionic modulation that is characteristic of P2X2 receptors: potentiation by acidification and extrac
62  of the two transmembrane domains of the rat P2X2 receptor protein, and is likely to be close to the
63  direct evidence that calcium influx through P2X2 receptors results in the activation of the MAP kina
64 inc over the range of 2-100 muM, whereas rat P2X2 receptors (rP2X2) are strongly potentiated over the
65 amino-terminal region with the corresponding P2X2 receptor section (P2X7-2Nbeta) gave responses that
66                           Interpreted with a P2X2 receptor structural model of the closed state, our
67 ere we describe null mutant mice lacking the P2X2 receptor subunit (P2X2-/-) and double mutant mice l
68 asparagine residues 182, 239, and 298 of the P2X2 receptor subunit by showing that the protein is gly
69                                              P2X2 receptor subunit immunoreactivity was detected in a
70    HEK-293 cells stably transfected with the P2X2 receptor subunit showed little or no response to AT
71 n mice null for the P2RX2 gene (encoding the P2X2 receptor subunit), sustained 85-dB noise failed to
72  of the VLM respiratory neurones express the P2X2 receptor subunit.
73 w that ATP-gated ion channels assembled from P2X2 receptor subunits in the cochlea are necessary for
74  rostral ventrolateral medulla (VLM) express P2X2 receptor subunits of the ATP-gated ion channel, sin
75                                              P2X2 receptor subunits of the ATP-gated ion channels are
76  introducing pairs of cysteines into the rat P2X2 receptor that might form disulfide bonds within or
77                         We have engineered a P2X2 receptor that opens within milliseconds by irradiat
78                                       In rat P2X2 receptors, these intersect at Thr(339).
79 We have used chimeras between human P2X1 and P2X2 receptors to address the contribution of the extrac
80 nnels that physically couple with purinergic P2X2 receptors to trigger a functional cross-inhibition
81 ment for P2X1 receptors but had no effect on P2X2 receptor trafficking.
82 ist potency and specificity profiles for rat P2X2 receptors; triphosphate-bearing analogues display b
83                     Rat wild-type and mutant P2X2 receptors were expressed in Xenopus oocytes and cur
84                                              P2X2 receptors were forced into a prolonged desensitized
85                            P2RX2 encodes the P2X2 receptor, which is an adenosine triphosphate (ATP)
86  study, we used homology modeling of the rat P2X2 receptor with the zebrafish P2X4 X-ray template to