INT243980

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Context Info
Confidence 0.23
First Reported 2008
Last Reported 2009
Negated 2
Speculated 0
Reported most in Body
Documents 4
Total Number 4
Disease Relevance 0.19
Pain Relevance 0.31

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 (Camk2a) kinase activity (Camk2a) cytoplasm (Camk2a)
Camk2a (Mus musculus)
Pain Link Frequency Relevance Heat
nMDA receptor 60 98.92 Very High Very High Very High
Spinal cord 61 87.44 High High
Hippocampus 16 77.72 Quite High
GABAergic 30 50.00 Quite Low
Inflammation 18 50.00 Quite Low
Dorsal horn 22 13.28 Low Low
imagery 7 12.96 Low Low
gABA 39 5.00 Very Low Very Low Very Low
intrathecal 32 5.00 Very Low Very Low Very Low
Thermal hyperalgesia 26 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Nociception 28 95.20 Very High Very High Very High
INFLAMMATION 18 50.00 Quite Low
Bardet-biedl Syndrome 1 15.96 Low Low
Hyperalgesia 50 5.00 Very Low Very Low Very Low
Neuropathic Pain 36 5.00 Very Low Very Low Very Low
Pain 27 5.00 Very Low Very Low Very Low
Depression 17 5.00 Very Low Very Low Very Low
Inflammatory Pain 14 5.00 Very Low Very Low Very Low
Targeted Disruption 11 5.00 Very Low Very Low Very Low
Injury 10 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
As the amount of active CaMKII increased, active PP-1 decreased in a manner depending on PDE1 phosphorylation by CaMKII (Figure 5F).
Regulation (depending) of Phosphorylation (phosphorylation) of CaMKII
1) Confidence 0.23 Published 2009 Journal Mol Syst Biol Section Body Doc Link PMC2710870 Disease Relevance 0 Pain Relevance 0
The group of Hirano suggests, that PP-1 reduces GABAA receptor function by controlling the autophosphorylation of CaMKII (Sugiyama et al., 2008).
Regulation (controlling) of Phosphorylation (autophosphorylation) of CaMKII
2) Confidence 0.17 Published 2008 Journal Frontiers in Molecular Neuroscience Section Body Doc Link PMC2526003 Disease Relevance 0 Pain Relevance 0
This therefore suggests that neither CaMKII nor modulation of Ser1303 phosphorylation is involved in ephrinB2 modulation of NMDA receptor activity.


Neg (neither) Regulation (involved) of Phosphorylation (phosphorylation) of CaMKII associated with nmda receptor
3) Confidence 0.05 Published 2008 Journal Neuroscience Section Body Doc Link PMC2568875 Disease Relevance 0.10 Pain Relevance 0.16
This therefore suggests that neither CaMKII nor modulation of Ser1303 phosphorylation is involved in ephrinB2 modulation of NMDA receptor activity.


Neg (neither) Regulation (modulation) of Phosphorylation (phosphorylation) of CaMKII associated with nmda receptor
4) Confidence 0.05 Published 2008 Journal Neuroscience Section Body Doc Link PMC2568875 Disease Relevance 0.09 Pain Relevance 0.16

General Comments

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