INT215166

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Context Info
Confidence 0.35
First Reported 2006
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 5
Total Number 8
Disease Relevance 0.41
Pain Relevance 1.97

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 (P2rx1) protein complex (P2rx1)
Anatomy Link Frequency
brain 1
P2rx1 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
Potency 194 100.00 Very High Very High Very High
Neurotransmitter 2 99.92 Very High Very High Very High
agonist 185 98.12 Very High Very High Very High
adenocard 14 92.60 High High
Inflammation 21 90.48 High High
antagonist 77 86.72 High High
Inflammatory response 2 72.96 Quite High
Glutamate 5 70.20 Quite High
Glutamate receptor 1 69.60 Quite High
cytokine 4 55.84 Quite High
Disease Link Frequency Relevance Heat
INFLAMMATION 23 90.48 High High
Chronic Disease 1 78.40 Quite High
Reprotox - General 1 4 62.88 Quite High
Ganglion Cysts 22 54.88 Quite High
Hyperalgesia 7 47.84 Quite Low
Neuropathic Pain 9 47.16 Quite Low
Nociception 9 5.00 Very Low Very Low Very Low
Pain 9 5.00 Very Low Very Low Very Low
Targeted Disruption 9 5.00 Very Low Very Low Very Low
Nervous System Injury 7 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
ATP acts as a fast synaptic neurotransmitter by binding to post-synaptic P2X receptors in a variety of neuronal cells, in keeping with their wide distribution predominantly on brain neurons [6].
P2X Binding (binding) of in brain associated with neurotransmitter
1) Confidence 0.35 Published 2006 Journal Purinergic Signal Section Body Doc Link PMC2096653 Disease Relevance 0.30 Pain Relevance 0.40
Phosphorylation of regulatory proteins associated with P2X1 or P2X7 receptor increased the activity of the P2X receptors [51,52].
P2X1 Binding (associated) of
2) Confidence 0.24 Published 2007 Journal Mol Pain Section Body Doc Link PMC2063498 Disease Relevance 0.05 Pain Relevance 0.19
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).
P2X1 Binding (backgrounds) of associated with potency
3) Confidence 0.17 Published 2010 Journal British Journal of Pharmacology Section Body Doc Link PMC2972645 Disease Relevance 0 Pain Relevance 0.11
Phe291 (P2X1 receptor numbering) was suggested to bind the adenine ring of ATP as mutation decreased agonist potency at P2X1, 2 and 4 receptors (Roberts and Evans, 2004; Roberts et al., 2008).
P2X1 Binding (bind) of associated with agonist and potency
4) Confidence 0.17 Published 2010 Journal British Journal of Pharmacology Section Body Doc Link PMC2972645 Disease Relevance 0 Pain Relevance 0.28
Binding of 2-azido ATP was reduced for cysteine mutants of Asn290, Phe291, Arg292 and Lys309 at the P2X1 receptor.
P2X1 Binding (Binding) of
5) Confidence 0.17 Published 2010 Journal British Journal of Pharmacology Section Body Doc Link PMC2972645 Disease Relevance 0.06 Pain Relevance 0.36
Cysteine reactive (2-aminoethyl) methanethiosulfonate hydrobromide-biotin was unable to bind to wild-type P2X1 receptors suggesting that no free cysteine residues were accessible (Ennion and Evans, 2002).
P2X1 Neg (unable) Binding (bind) of
6) Confidence 0.17 Published 2010 Journal British Journal of Pharmacology Section Body Doc Link PMC2972645 Disease Relevance 0 Pain Relevance 0.04
These results suggest that the effects of mutation of this conserved residue can be manifest as a principal effect on ATP binding at the P2X1 receptor (16) and an additional effect on gating at the P2X2 receptor (32).
P2X1 Binding (binding) of
7) Confidence 0.15 Published 2008 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2459275 Disease Relevance 0 Pain Relevance 0.21
Close to the FT motif is a nearby conserved lysine residue that has been shown to be involved in regulating ATP potency (Lys190 in P2X1 and Lys188 in P2X2 that when mutated to alanine resulted in ?
P2X1 Binding (potency) of associated with potency
8) Confidence 0.13 Published 2008 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2459275 Disease Relevance 0 Pain Relevance 0.39

General Comments

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