INT258166

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Context Info
Confidence 0.10
First Reported 2009
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 7
Disease Relevance 0.97
Pain Relevance 2.10

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

signal transduction (Ppap2a) plasma membrane (Ppap2a)
Ppap2a (Mus musculus)
Pain Link Frequency Relevance Heat
Antinociceptive 154 98.92 Very High Very High Very High
addiction 7 94.28 High High
adenocard 168 91.68 High High
IPN 42 87.28 High High
antinociception 70 80.12 Quite High
Antihyperalgesic 63 78.72 Quite High
antiallodynic 56 77.04 Quite High
Spinal cord 28 64.96 Quite High
antagonist 14 64.80 Quite High
Lasting pain 35 59.44 Quite High
Disease Link Frequency Relevance Heat
Inflammatory Pain 42 87.28 High High
Nociception 56 82.60 Quite High
Pain 56 59.44 Quite High
Neuropathic Pain 14 58.00 Quite High
Infection 7 57.12 Quite High
Targeted Disruption 7 53.64 Quite High
INFLAMMATION 42 33.20 Quite Low
Acidosis 28 31.12 Quite Low
Paralysis 28 5.00 Very Low Very Low Very Low
Sleep Disorders 14 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
In contrast, mPAP dephosphorylated all purine nucleotides (AMP, ADP, ATP) at an acidic pH (pH 5.6).
Phosphorylation (dephosphorylated) of mPAP
1) Confidence 0.10 Published 2009 Journal PLoS ONE Section Abstract Doc Link PMC2617779 Disease Relevance 0.15 Pain Relevance 0.59
We found that mPAP dephosphorylated AMP, and to a much lesser extent, ADP at neutral pH (pH 7.0).
Phosphorylation (dephosphorylated) of mPAP
2) Confidence 0.10 Published 2009 Journal PLoS ONE Section Abstract Doc Link PMC2617779 Disease Relevance 0.15 Pain Relevance 0.49
Recombinant mPAP dephosphorylates purine nucleotides in a pH-dependent manner
Phosphorylation (dephosphorylates) of mPAP
3) Confidence 0.10 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2617779 Disease Relevance 0.06 Pain Relevance 0.08
In addition, we found that mPAP could dephosphorylate all purine nucleotides (AMP, ADP, ATP) under acidic pH conditions.
Phosphorylation (dephosphorylate) of mPAP
4) Confidence 0.10 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2617779 Disease Relevance 0.31 Pain Relevance 0.37
At neutral pH, mPAP primarily dephosphorylated AMP.
Phosphorylation (dephosphorylated) of mPAP
5) Confidence 0.10 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2617779 Disease Relevance 0.31 Pain Relevance 0.39
We found that mPAP dephosphorylated AMP and, to a lesser extent, ADP at neutral pH (Fig. 3A), consistent with our previous findings using hPAP [3].
Phosphorylation (dephosphorylated) of mPAP
6) Confidence 0.07 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2617779 Disease Relevance 0 Pain Relevance 0.09
At pH 5.6, mPAP dephosphorylated AMP and ADP, and to a lesser extent, ATP (Fig. 3B).
Phosphorylation (dephosphorylated) of mPAP
7) Confidence 0.07 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2617779 Disease Relevance 0 Pain Relevance 0.09

General Comments

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