INT129988

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Context Info
Confidence 0.28
First Reported 2005
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 3
Total Number 3
Disease Relevance 1.94
Pain Relevance 1.25

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

cytosol (Gria1) transport (Gria1) endoplasmic reticulum (Gria1)
plasma membrane (Gria1) protein complex (Gria1)
Anatomy Link Frequency
spinal 2
Gria1 (Mus musculus)
Pain Link Frequency Relevance Heat
Spinal sensitization 4 99.20 Very High Very High Very High
Pain 15 97.88 Very High Very High Very High
Dorsal horn neuron 6 93.96 High High
Inflammation 9 90.76 High High
nMDA receptor antagonist 2 89.96 High High
Hyperalgesia 4 88.88 High High
antagonist 2 87.44 High High
Hippocampus 19 86.60 High High
IPN 9 70.84 Quite High
allodynia 5 69.56 Quite High
Disease Link Frequency Relevance Heat
Pain 12 97.88 Very High Very High Very High
Targeted Disruption 91 91.72 High High
INFLAMMATION 9 90.76 High High
Hyperalgesia 5 88.88 High High
Nociception 29 86.36 High High
Inflammatory Pain 9 70.84 Quite High
Neuropathic Pain 9 69.56 Quite High
Injury 3 62.16 Quite High
Irritable Bowel Syndrome /

Irritable Bowel Syndrome Super / Visceral Pain

1 60.96 Quite High
Anxiety Disorder 28 50.00 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Phosphorylation and dephosphorylation of GluR1 play a critical role for AMPA receptor insertion and internalization [9], [12], thereby affecting AMPA receptor-mediated synaptic responses.
Regulation (affecting) of Phosphorylation (Phosphorylation) of GluR1
1) Confidence 0.28 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2169299 Disease Relevance 0.44 Pain Relevance 0.10
The rapid alterations in the composition of synaptic AMPA receptors induced by physiologic activity or noxious stimuli can be achieved by modulating the phosphorylation status of GluR1 and GluR2 subunits and their binding to PDZ domain-containing synaptic scaffolding proteins.
Regulation (modulating) of Phosphorylation (phosphorylation) of GluR1
2) Confidence 0.16 Published 2010 Journal Mol Pain Section Body Doc Link PMC2823608 Disease Relevance 1.08 Pain Relevance 0.66
These findings indicate that spinal sensitization in the thermal stimulus model does not involve CaMKIIalpha activation or AMPA GLUR1 receptor phosphorylation, and differs from that occurring in NMDAr-dependent pain states.
Neg (not) Regulation (involve) of Phosphorylation (phosphorylation) of GLUR1 in spinal associated with pain and spinal sensitization
3) Confidence 0.08 Published 2005 Journal Pain Section Abstract Doc Link 16150547 Disease Relevance 0.36 Pain Relevance 0.50

General Comments

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