INT259167

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Context Info
Confidence 0.34
First Reported 2008
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 2
Total Number 9
Disease Relevance 5.24
Pain Relevance 5.13

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

endoplasmic reticulum (Gria2) plasma membrane (Gria2) protein complex (Gria2)
Anatomy Link Frequency
amygdala 14
neurons 2
Gria2 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
Kinase C 1 99.98 Very High Very High Very High
amygdala 192 99.44 Very High Very High Very High
Hippocampus 384 99.16 Very High Very High Very High
Inflammation 26 98.80 Very High Very High Very High
long-term potentiation 137 94.24 High High
Spinal cord 21 86.08 High High
depression 32 85.76 High High
Eae 29 83.08 Quite High
Dorsal horn neuron 13 80.64 Quite High
central sensitization 4 70.72 Quite High
Disease Link Frequency Relevance Heat
Stress 600 99.98 Very High Very High Very High
INFLAMMATION 26 98.80 Very High Very High Very High
Depression 32 85.76 High High
Inflammatory Pain 28 83.08 Quite High
Cognitive Disorder 24 60.48 Quite High
Hypersensitivity 16 55.36 Quite High
Syndrome 1 43.92 Quite Low
Decapitation 17 5.00 Very Low Very Low Very Low
Affective Disorder 16 5.00 Very Low Very Low Very Low
Nociception 10 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Similarly, Protein kinase C phosphorylation of GluR2 at Ser880 disrupts GluR2 binding to its synaptic anchoring protein ABP/GRIP and promotes GluR2 internalization in cultured hippocampal neurons [36,37].
Negative_regulation (disrupts) of Phosphorylation (phosphorylation) of GluR2 in neurons associated with kinase c
1) Confidence 0.34 Published 2008 Journal Mol Pain Section Body Doc Link PMC2628655 Disease Relevance 0.39 Pain Relevance 0.47
Thirty minutes after the end of stress, changes in the phosphorylation sites of both GluA1 and GluA2 were found, with a decreased phosphorylation level at the Tyr876-GluA2 and Ser880-GluA2 sites in the amygdala (t (23)?
Negative_regulation (level) of Phosphorylation (phosphorylation) of GluA2 in amygdala associated with stress and amygdala
2) Confidence 0.22 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2999558 Disease Relevance 0.46 Pain Relevance 0.48
Phosphorylation of the Tyr876-GluA2 residue is known to control the surface expression and the synaptic targeting of the GluA2 subunit by causing its internalization [28], whereas Ser880-GluA2 phosphorylation decreases the affinity of GluA2 for GRIP and then triggers its internalization [29].
Negative_regulation (decreases) of Phosphorylation (phosphorylation) of GluA2
3) Confidence 0.19 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2999558 Disease Relevance 0.59 Pain Relevance 0.52
Exposure to stress decreased phosphorylation at both the Tyr876-GluA2 and Ser880-GluA2 sites in the amygdala, and at the Ser880-GluA2 site in the VH.
Negative_regulation (decreased) of Phosphorylation (phosphorylation) of GluA2 in amygdala associated with stress, hippocampus and amygdala
4) Confidence 0.19 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2999558 Disease Relevance 0.62 Pain Relevance 0.64
Thirty minutes after the end of stress, changes in the phosphorylation sites of both GluA1 and GluA2 were found, with a decreased phosphorylation level at the Tyr876-GluA2 and Ser880-GluA2 sites in the amygdala (t (23)?
Negative_regulation (level) of Phosphorylation (phosphorylation) of GluA2 in amygdala associated with stress and amygdala
5) Confidence 0.19 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2999558 Disease Relevance 0.51 Pain Relevance 0.48
Stress also modulated the GluA2 subunit with a decrease in the phosphorylation of both Tyr876-GluA2 and Ser880-GluA2 residues in the amygdala, and an increase in the phosphorylation of Ser880-GluA2 in the mPFC.
Negative_regulation (decrease) of Phosphorylation (phosphorylation) of GluA2 in amygdala associated with stress and amygdala
6) Confidence 0.19 Published 2010 Journal PLoS ONE Section Abstract Doc Link PMC2999558 Disease Relevance 0.77 Pain Relevance 0.71
Exposure to stress decreased phosphorylation at both the Tyr876-GluA2 and Ser880-GluA2 sites in the amygdala, and at the Ser880-GluA2 site in the VH.
Negative_regulation (decreased) of Phosphorylation (phosphorylation) of GluA2 in amygdala associated with stress, hippocampus and amygdala
7) Confidence 0.19 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2999558 Disease Relevance 0.63 Pain Relevance 0.64
Stress also modulated the GluA2 subunit with a decrease in the phosphorylation of both Tyr876-GluA2 and Ser880-GluA2 residues in the amygdala, and an increase in the phosphorylation of Ser880-GluA2 in the mPFC.
Negative_regulation (decrease) of Phosphorylation (phosphorylation) of GluA2 in amygdala associated with stress and amygdala
8) Confidence 0.19 Published 2010 Journal PLoS ONE Section Abstract Doc Link PMC2999558 Disease Relevance 0.76 Pain Relevance 0.71
Thirty minutes after the end of stress, changes in the phosphorylation sites of both GluA1 and GluA2 were found, with a decreased phosphorylation level at the Tyr876-GluA2 and Ser880-GluA2 sites in the amygdala (t (23)?
Negative_regulation (level) of Phosphorylation (phosphorylation) of GluA2 in amygdala associated with stress and amygdala
9) Confidence 0.19 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2999558 Disease Relevance 0.51 Pain Relevance 0.48

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