INT95735

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Context Info
Confidence 0.50
First Reported 2001
Last Reported 2009
Negated 5
Speculated 3
Reported most in Abstract
Documents 7
Total Number 10
Disease Relevance 1.88
Pain Relevance 2.69

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

cytosol (Mapk8) signal transduction (Mapk8) mitochondrion (Mapk8)
nucleus (Mapk8) kinase activity (Mapk8) cytoplasm (Mapk8)
Anatomy Link Frequency
spinal 4
brain 4
neuronal 2
nociceptors 2
hippocampus 2
Mapk8 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
noradrenaline 22 100.00 Very High Very High Very High
Spinal cord 12 97.20 Very High Very High Very High
Hippocampus 27 95.68 Very High Very High Very High
intrathecal 6 92.32 High High
Dorsal horn 2 88.72 High High
Glutamate 4 87.16 High High
ischemia 16 87.12 High High
Thermal hyperalgesia 8 85.96 High High
withdrawal 3 83.44 Quite High
Neuropathic pain 2 75.00 Quite High
Disease Link Frequency Relevance Heat
Thyroid Disease 2 92.96 High High
Stress 67 92.28 High High
Diabetes Mellitus 4 89.08 High High
Cv Unclassified Under Development 7 87.12 High High
Hyperalgesia 8 85.96 High High
Nociception 6 82.64 Quite High
Middle Cerebral Artery Infarction 27 81.88 Quite High
Apoptosis 2 81.84 Quite High
Neuropathic Pain 2 75.00 Quite High
Cretinism 2 75.00 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
To elucidate the involvement of the noradrenergic system in the regulation of spinal microglial activity, we examined the effects of noradrenaline (NA) on the phosphorylation of three MAP kinases (extracellular signal-regulated kinase (ERK), p38, or c-Jun N-terminal kinase (JNK)) stimulated by ATP in rat cultured spinal microglia using Western blotting.
Spec (examined) Regulation (effects) of Phosphorylation (phosphorylation) of JNK in spinal associated with noradrenaline
1) Confidence 0.50 Published 2009 Journal Neurochem. Int. Section Abstract Doc Link 19524113 Disease Relevance 0 Pain Relevance 0.27
We also sought to determine which neuronal phenotypes are affected and to examine the effect of aldose reductase inhibition on JNK and c-Jun phosphorylation.
Spec (examine) Regulation (effect) of Phosphorylation (phosphorylation) of JNK in neuronal
2) Confidence 0.44 Published 2006 Journal Diabetologia Section Abstract Doc Link 16456679 Disease Relevance 0.24 Pain Relevance 0.07
Our results suggest that the phosphorylation of JNK is involved in the up-regulation of the proenkephalin gene expression via c-Fos and c-Jun that is induced by KA in rat hippocampus.
Regulation (involved) of Phosphorylation (phosphorylation) of JNK in hippocampus associated with hippocampus
3) Confidence 0.42 Published 2001 Journal Mol. Cells Section Abstract Doc Link 11355693 Disease Relevance 0 Pain Relevance 0.26
To elucidate the involvement of the noradrenergic system in the regulation of spinal microglial activity, we examined the effects of noradrenaline (NA) on the phosphorylation of three MAP kinases (extracellular signal-regulated kinase (ERK), p38, or c-Jun N-terminal kinase (JNK)) stimulated by ATP in rat cultured spinal microglia using Western blotting.
Spec (examined) Regulation (effects) of Phosphorylation (phosphorylation) of c-Jun N-terminal kinase in spinal associated with noradrenaline
4) Confidence 0.37 Published 2009 Journal Neurochem. Int. Section Abstract Doc Link 19524113 Disease Relevance 0 Pain Relevance 0.27
However, neither the phosphorylated extracellular signal-regulated kinase (p-ERK) nor phosphorylated c-Jun NH2-terminal kinase (p-JNK) was affected.
Neg (neither) Regulation (affected) of Phosphorylation (phosphorylated) of JNK
5) Confidence 0.27 Published 2005 Journal J. Neurochem. Section Abstract Doc Link 16033422 Disease Relevance 0.45 Pain Relevance 0.71
However, neither the phosphorylated extracellular signal-regulated kinase (p-ERK) nor phosphorylated c-Jun NH2-terminal kinase (p-JNK) was affected.
Neg (neither) Regulation (affected) of Phosphorylation (phosphorylated) of JNK
6) Confidence 0.27 Published 2005 Journal J. Neurochem. Section Abstract Doc Link 16033422 Disease Relevance 0.44 Pain Relevance 0.69
CONCLUSIONS/INTERPRETATION: Fidarestat-sensitive phosphorylation of JNK and c-Jun occurs in fast-conduction mechanoceptors-the same class of neurones that registers the changes in sensory nerve conduction velocity-and in nociceptors.
Regulation (sensitive) of Phosphorylation (phosphorylation) of JNK in nociceptors
7) Confidence 0.26 Published 2006 Journal Diabetologia Section Body Doc Link 16456679 Disease Relevance 0 Pain Relevance 0
Additionally, we demonstrated increased extracellular signal-regulated kinase 1/2 (ERK1/2) phosphorylation without altering Jun N-terminal kinase (JNK) and p38(MAPK) phosphorylation.
Neg (without) Regulation (altering) of Phosphorylation (phosphorylation) of JNK
8) Confidence 0.21 Published 2008 Journal Neurotoxicology Section Abstract Doc Link 18845185 Disease Relevance 0.27 Pain Relevance 0.27
Curiously, phosphorylation of their cognate substrates (Erk and JNK) was increased to a much more modest extent, and in some brain regions was not altered.
Neg (not) Regulation (altered) of Phosphorylation (phosphorylation) of JNK in brain
9) Confidence 0.11 Published 2004 Journal BMC Neurosci Section Abstract Doc Link PMC526203 Disease Relevance 0.22 Pain Relevance 0.07
It is intriguing that U0126 does not affect phosphorylation of p38 or JNK in cultured neurons [18], in vivo in brain tissue [13] or in cerebrovascular smooth muscle cells [14].
Neg (not) Regulation (affect) of Phosphorylation (phosphorylation) of JNK in brain
10) Confidence 0.06 Published 2008 Journal BMC Neurosci Section Body Doc Link PMC2553085 Disease Relevance 0.25 Pain Relevance 0.08

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