INT120732

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Context Info
Confidence 0.48
First Reported 2004
Last Reported 2005
Negated 0
Speculated 0
Reported most in Body
Documents 2
Total Number 2
Disease Relevance 1.04
Pain Relevance 1.81

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 (Prkcg, Grin1) cytoplasm (Prkcg, Grin1) cytosol (Prkcg)
nucleus (Prkcg) intracellular (Prkcg) enzyme binding (Grin1)
Prkcg (Rattus norvegicus)
Grin1 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
Kinase C 12 100.00 Very High Very High Very High
qutenza 8 98.76 Very High Very High Very High
Dorsal horn neuron 5 96.92 Very High Very High Very High
spinothalamic tract 6 94.84 High High
allodynia 14 93.36 High High
Thermal hyperalgesia 8 90.80 High High
nMDA receptor 35 90.64 High High
Spinal cord 33 87.80 High High
antagonist 2 82.56 Quite High
intrathecal 2 81.88 Quite High
Disease Link Frequency Relevance Heat
Neuropathic Pain 14 93.36 High High
Hyperalgesia 13 90.80 High High
Injury 14 88.36 High High
Nociception 27 83.12 Quite High
Pain 14 61.32 Quite High
INFLAMMATION 21 5.00 Very Low Very Low Very Low
Frailty 4 5.00 Very Low Very Low Very Low
Disease 3 5.00 Very Low Very Low Very Low
Nervous System Injury 1 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
To see if protein kinase C (PKC) also participates in the phosphorylation of NR1, we used electron microscopic techniques to determine further where the phosphorylated NR1 subunits (pNR1) are expressed in the spinothalamic tract (STT) cells and immunohistochemistry to examine whether a PKC inhibitor, chelerythrine chloride, blocks the enhanced phosphorylation of NR1 on serine 896.
PKC Positive_regulation (participates) of Phosphorylation (phosphorylation) of NR1 associated with spinothalamic tract and kinase c
1) Confidence 0.48 Published 2004 Journal Brain Res. Section Abstract Doc Link 15312791 Disease Relevance 0 Pain Relevance 0.80
Zou et al. and Brenner et al. have demonstrated that NR1 phosphorylation is mediated by the serine/threonine kinases protein kinase C (PKC) and protein kinase A (PKA) [11,13,14].
PKC Positive_regulation (mediated) of Phosphorylation (phosphorylation) of NR1 associated with kinase c
2) Confidence 0.38 Published 2005 Journal Mol Pain Section Body Doc Link PMC1208948 Disease Relevance 1.04 Pain Relevance 1.00

General Comments

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