INT120261

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Context Info
Confidence 0.28
First Reported 2004
Last Reported 2010
Negated 0
Speculated 1
Reported most in Body
Documents 19
Total Number 25
Disease Relevance 5.80
Pain Relevance 6.72

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

plasma membrane (P2rx2)
Anatomy Link Frequency
neurons 1
pore 1
P2rx2 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
Pain 71 99.78 Very High Very High Very High
nociceptor 32 99.78 Very High Very High Very High
antagonist 146 99.60 Very High Very High Very High
Inflammatory mediators 2 99.02 Very High Very High Very High
agonist 273 98.48 Very High Very High Very High
Inflammation 79 97.92 Very High Very High Very High
noradrenaline 25 97.88 Very High Very High Very High
Potency 208 97.12 Very High Very High Very High
Spontaneous pain 10 94.44 High High
Thermal hyperalgesia 18 93.20 High High
Disease Link Frequency Relevance Heat
Nociception 61 100.00 Very High Very High Very High
Pain 91 99.40 Very High Very High Very High
INFLAMMATION 88 98.82 Very High Very High Very High
Ataxia 2 98.20 Very High Very High Very High
Hyperalgesia 32 93.20 High High
Ganglion Cysts 216 92.80 High High
Hypersensitivity 11 87.64 High High
Coagulation Disorder 7 87.52 High High
Inflammatory Pain 22 86.96 High High
Neuropathic Pain 110 78.52 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
This may indicate that in the P2X2 receptor the lysine residue interacts with another amino acid that is not conserved at the P2X1 receptor to regulate gating.
P2X2 Binding (interacts) of
1) Confidence 0.28 Published 2008 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2459275 Disease Relevance 0 Pain Relevance 0.24
A peculiar phenotype is inherent to heteromeric P2X2/P2X3 (P2X2+3) receptors, which feature ??
P2X2 Binding (heteromeric) of
2) Confidence 0.27 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072911 Disease Relevance 0.30 Pain Relevance 0.22
A peculiar phenotype is inherent to heteromeric P2X2/P2X3 (P2X2+3) receptors, which feature ??
P2X2 Binding (heteromeric) of
3) Confidence 0.24 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072911 Disease Relevance 0.31 Pain Relevance 0.22
Since peripheral inflammation increases the levels of various inflammatory mediators in the inflamed area [32, 115], there may be an interaction between P2X receptors and these mediators that produces the functional upregulation of P2X receptors.
P2X Binding (interaction) of associated with inflammatory mediators and inflammation
4) Confidence 0.21 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2096756 Disease Relevance 0.52 Pain Relevance 0.38
How many subunits make a P2X receptor?
P2X Binding (receptor) of
5) Confidence 0.19 Published 2010 Journal Trends in Pharmacological Sciences Section Body Doc Link PMC2954318 Disease Relevance 0 Pain Relevance 0.13
Current interpretation of the functional properties of P2X receptors in terms of atomic structure will presage a much more detailed understanding of how ligands bind to these receptors.
P2X Binding (bind) of
6) Confidence 0.19 Published 2010 Journal Trends in Pharmacological Sciences Section Body Doc Link PMC2954318 Disease Relevance 0.22 Pain Relevance 0.29
Determining the residues involved in the binding of the ever-increasing number of P2X receptor antagonists [9,33], and designing new selective antagonists de novo using in silico methods will be very important.


P2X Binding (binding) of associated with antagonist
7) Confidence 0.19 Published 2010 Journal Trends in Pharmacological Sciences Section Body Doc Link PMC2954318 Disease Relevance 0 Pain Relevance 0.24
This supports results from mutagenesis studies at P2X2 and P2X4 receptors, where cysteine mutants of these residues were not affected by MTS reagents and were considered inaccessible to these compounds (Roberts et al., 2008).
P2X2 Binding (receptors) of
8) Confidence 0.17 Published 2010 Journal British Journal of Pharmacology Section Body Doc Link PMC2972645 Disease Relevance 0 Pain Relevance 0.19
The association of P2X receptors with interacting proteins (e.g.
P2X Binding (association) of
9) Confidence 0.17 Published 2010 Journal British Journal of Pharmacology Section Body Doc Link PMC2972645 Disease Relevance 0 Pain Relevance 0
The binding of ATP to the P2X receptor results in conformational changes that lead to the opening of the channel pore (gating of the channel).
P2X Binding (binding) of in pore
10) Confidence 0.17 Published 2010 Journal British Journal of Pharmacology Section Body Doc Link PMC2972645 Disease Relevance 0 Pain Relevance 0.24
Mutants generated on P2X1 and P2X2 receptor backgrounds showed that residues Lys68, Lys70, Arg292 and Lys309 contribute to ATP potency (P2X1 receptor numbering)(Ennion et al., 2000; Jiang et al., 2000); with the greatest, >1000-fold, decreases in ATP sensitivity for Lys68Ala and Lys309Ala mutants at the P2X1 receptor (Ennion et al., 2000).
P2X2 Binding (backgrounds) of associated with potency
11) Confidence 0.17 Published 2010 Journal British Journal of Pharmacology Section Body Doc Link PMC2972645 Disease Relevance 0 Pain Relevance 0.11
Structural interpretation of P2X receptor mutagenesis studies on drug action

P2X receptors for ATP are ligand gated cation channels that form from the trimeric assembly of subunits with two transmembrane segments, a large extracellular ligand binding loop, and intracellular amino and carboxy termini.

P2X Binding (interpretation) of
12) Confidence 0.17 Published 2010 Journal British Journal of Pharmacology Section Title Doc Link PMC2972645 Disease Relevance 0.17 Pain Relevance 0.08
Unlike other ionotropic purinoceptors, including P2X2, which bind directly to phosphoinositides, our findings suggest that P2X3 is modulated by PIP2 indirectly.
P2X2 Binding (bind) of
13) Confidence 0.16 Published 2009 Journal Mol Pain Section Body Doc Link PMC2734547 Disease Relevance 0.52 Pain Relevance 0.45
Structural interpretation of P2X receptor mutagenesis studies on drug action

P2X receptors for ATP are ligand gated cation channels that form from the trimeric assembly of subunits with two transmembrane segments, a large extracellular ligand binding loop, and intracellular amino and carboxy termini.

P2X Binding (interpretation) of
14) Confidence 0.15 Published 2010 Journal British Journal of Pharmacology Section Title Doc Link PMC2972645 Disease Relevance 0.17 Pain Relevance 0.08
The present study examined interactions between alphabeta-methylene-ATP (a P2X(3) receptor ligand) and 5-hydroxytryptamine (5-HT), noradrenaline (NA) and histamine, following local administration into the hindpaw, on spontaneous pain behaviors and thermal hyperalgesia in Sprague-Dawley rats.
P2X Spec (examined) Binding (interactions) of associated with pain, thermal hyperalgesia, spontaneous pain and noradrenaline
15) Confidence 0.13 Published 2004 Journal Pain Section Abstract Doc Link 15275755 Disease Relevance 0.43 Pain Relevance 0.42
Peripheral P2X receptors and nociception: interactions with biogenic amine systems.
P2X Binding (interactions) of associated with nociception and nociceptor
16) Confidence 0.13 Published 2004 Journal Pain Section Title Doc Link 15275755 Disease Relevance 0.61 Pain Relevance 0.93
However, taking into consideration lipid binding to recombinant C-terminal P2X2 channel constructs, they proposed that PI(3)P and PI(3,5)P2, rather than PIP2 or PIP3, are the main regulators of homomeric P2X2 function.
P2X2 Binding (binding) of
17) Confidence 0.12 Published 2009 Journal Mol Pain Section Body Doc Link PMC2734547 Disease Relevance 0.22 Pain Relevance 0.08
Functional interaction between A1Rs and P2X receptors
P2X Binding (interaction) of
18) Confidence 0.12 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072922 Disease Relevance 0.44 Pain Relevance 0.29
The P2X2 peptide showed direct binding to all phosphatidylinositol phosphates: PI(3)P, PI(4)P, PI(5)P, PI(3,4)P2, PI(3,5)P2, PI(4,5)P2, PI(3,4,5)P3.
P2X2 Binding (binding) of
19) Confidence 0.11 Published 2009 Journal Mol Pain Section Body Doc Link PMC2734547 Disease Relevance 0 Pain Relevance 0
Phosphoinositides are negatively charged lipids, therefore we investigated potential interactions with basic residues on the intracellular domain of the P2X3 channel subunit and confirmed P2X2 subunit binding using a lipid strip assay.
P2X2 Binding (binding) of
20) Confidence 0.10 Published 2009 Journal Mol Pain Section Body Doc Link PMC2734547 Disease Relevance 0 Pain Relevance 0

General Comments

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