INT259165

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Context Info
Confidence 0.65
First Reported 2008
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 4
Total Number 22
Disease Relevance 11.65
Pain Relevance 11.07

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 13
neurons 2
plasma 1
Gria2 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
Kinase C 3 99.98 Very High Very High Very High
Hippocampus 912 99.92 Very High Very High Very High
Spinal cord 63 99.78 Very High Very High Very High
amygdala 456 99.52 Very High Very High Very High
Inflammation 78 99.38 Very High Very High Very High
Eae 87 98.28 Very High Very High Very High
Dorsal horn neuron 39 97.06 Very High Very High Very High
long-term potentiation 326 94.24 High High
depression 76 91.28 High High
Glutamate receptor 47 73.76 Quite High
Disease Link Frequency Relevance Heat
Stress 1425 99.78 Very High Very High Very High
INFLAMMATION 78 99.38 Very High Very High Very High
Inflammatory Pain 84 98.28 Very High Very High Very High
Depression 76 91.28 High High
Cognitive Disorder 57 73.84 Quite High
Syndrome 3 57.40 Quite High
Hypersensitivity 48 55.84 Quite High
Overactive Bladder 19 24.24 Low Low
Decapitation 41 23.84 Low Low
Affective Disorder 38 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].
Phosphorylation (phosphorylation) of GluR2 in neurons associated with kinase c
1) Confidence 0.65 Published 2008 Journal Mol Pain Section Body Doc Link PMC2628655 Disease Relevance 0.39 Pain Relevance 0.47
The molecular mechanisms by which GluR1 is inserted into plasma membrane and GluR2 is internalized into cytoplasm in dorsal horn neurons during the maintenance phase of persistent inflammatory pain are unclear, but they might be related to inflammation-induced spinal cord GluR1 and GluR2 phosphorylation.
Phosphorylation (phosphorylation) of GluR2 in plasma associated with inflammation, eae, dorsal horn neuron and spinal cord
2) Confidence 0.57 Published 2008 Journal Mol Pain Section Body Doc Link PMC2628655 Disease Relevance 0.39 Pain Relevance 0.49
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].
Phosphorylation (phosphorylation) of GluR2 in neurons associated with kinase c
3) Confidence 0.50 Published 2008 Journal Mol Pain Section Body Doc Link PMC2628655 Disease Relevance 0.44 Pain Relevance 0.50
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)?
Phosphorylation (phosphorylation) of GluA2 in amygdala associated with stress and amygdala
4) Confidence 0.43 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2999558 Disease Relevance 0.46 Pain Relevance 0.48
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)?
Phosphorylation (phosphorylation) of GluA2 in amygdala associated with stress and amygdala
5) Confidence 0.43 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2999558 Disease Relevance 0.46 Pain Relevance 0.48
In contrast, the increased phosphorylation of the Ser880-GluA2 residue in the mPFC that we observed suggests acute stress increases AMPAR internalization and facilitates the generation of LTD in that region.
Phosphorylation (phosphorylation) of GluA2 associated with stress
6) Confidence 0.37 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2999558 Disease Relevance 0.62 Pain Relevance 0.37
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].
Phosphorylation (phosphorylation) of GluA2
7) Confidence 0.37 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2999558 Disease Relevance 0.59 Pain Relevance 0.52
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.
Phosphorylation (phosphorylation) of GluA2 in amygdala associated with stress and amygdala
8) Confidence 0.37 Published 2010 Journal PLoS ONE Section Abstract Doc Link PMC2999558 Disease Relevance 0.77 Pain Relevance 0.70
In addition to affecting GluA1 subunits, we observed that acute stress modulates the phosphorylation state of the GluA2 subunit in amygdala, mPFC and VH.
Phosphorylation (phosphorylation) of GluA2 in amygdala associated with stress, hippocampus and amygdala
9) Confidence 0.37 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2999558 Disease Relevance 0.57 Pain Relevance 0.59
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.
Phosphorylation (phosphorylation) of GluA2 in amygdala associated with stress, hippocampus and amygdala
10) Confidence 0.37 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2999558 Disease Relevance 0.63 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)?
Phosphorylation (phosphorylation) of GluA2 in amygdala associated with stress and amygdala
11) Confidence 0.37 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.
Phosphorylation (phosphorylation) of GluA2 in amygdala associated with stress and amygdala
12) Confidence 0.37 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)?
Phosphorylation (phosphorylation) of GluA2 in amygdala associated with stress and amygdala
13) Confidence 0.37 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2999558 Disease Relevance 0.52 Pain Relevance 0.49
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)?
Phosphorylation (phosphorylation) of GluA2 in amygdala associated with stress and amygdala
14) Confidence 0.37 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2999558 Disease Relevance 0.51 Pain Relevance 0.48
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)?
Phosphorylation (phosphorylation) of GluA2 in amygdala associated with stress and amygdala
15) Confidence 0.37 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2999558 Disease Relevance 0.52 Pain Relevance 0.49
Immunoblotting was also carried out on the same stripped membranes with antibodies that were not phosphorylation-state-specific against total GluA1, GluA2 (Millipore, Molsheim, France) in blocking buffer.
Phosphorylation (phosphorylation) of GluA2
16) Confidence 0.37 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2999558 Disease Relevance 0 Pain Relevance 0
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.
Phosphorylation (phosphorylation) of GluA2 in amygdala associated with stress, hippocampus and amygdala
17) Confidence 0.37 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2999558 Disease Relevance 0.62 Pain Relevance 0.63
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.
Phosphorylation (phosphorylation) of GluA2 in amygdala associated with stress and amygdala
18) Confidence 0.37 Published 2010 Journal PLoS ONE Section Abstract Doc Link PMC2999558 Disease Relevance 0.76 Pain Relevance 0.71
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].
Phosphorylation (phosphorylation) of GluA2
19) Confidence 0.33 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2999558 Disease Relevance 0.55 Pain Relevance 0.53
Specifically, we examined the phosphorylation of GluA1 at the CaMKII and PKA sites (Ser831-GluA1 and Ser845-GluA1) and the phosphorylation of GluA2 at the tyrosine kinase and PKC sites (Tyr876-GluA2 and Ser880-GluA2) after acute platform stress.
Phosphorylation (phosphorylation) of GluA2 associated with stress
20) Confidence 0.33 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2999558 Disease Relevance 0.59 Pain Relevance 0.39

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