INT95739

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Context Info
Confidence 0.42
First Reported 2001
Last Reported 2010
Negated 0
Speculated 1
Reported most in Abstract
Documents 11
Total Number 12
Disease Relevance 6.77
Pain Relevance 2.61

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
nerve 4
lung 2
PP2A 2
T cells 2
Mapk8 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
Pain 10 100.00 Very High Very High Very High
Neuropathic pain 4 100.00 Very High Very High Very High
cva 13 98.08 Very High Very High Very High
antidepressant 2 91.96 High High
Central nervous system 9 91.20 High High
Hippocampus 12 90.08 High High
anesthesia 5 90.00 High High
metalloproteinase 33 87.60 High High
tolerance 13 84.72 Quite High
cytokine 25 84.24 Quite High
Disease Link Frequency Relevance Heat
Diabetes Mellitus 84 100.00 Very High Very High Very High
Neuropathic Pain 5 100.00 Very High Very High Very High
Hemorrhage 13 98.08 Very High Very High Very High
Injury 25 97.44 Very High Very High Very High
Hypoxia 51 97.16 Very High Very High Very High
Increased Venous Pressure Under Development 3 94.88 High High
Obesity 20 94.28 High High
Adhesions 10 92.68 High High
Multiple Sclerosis 5 92.32 High High
Death 14 92.12 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Phosphorylation of c-Jun N-terminal kinase (JNK) in sensory neurones of diabetic rats, with possible effects on nerve conduction and neuropathic pain: prevention with an aldose reductase inhibitor.
Negative_regulation (prevention) of Phosphorylation (Phosphorylation) of JNK in nerve associated with pain, diabetes mellitus and neuropathic pain
1) Confidence 0.42 Published 2006 Journal Diabetologia Section Title Doc Link 16456679 Disease Relevance 0.30 Pain Relevance 0.30
Protein was isolated from tissues for determination of p44/42 and SAPK/JNK phosphorylation by Western blot analysis.
Negative_regulation (determination) of Phosphorylation (phosphorylation) of JNK
2) Confidence 0.41 Published 2002 Journal Shock Section Abstract Doc Link 12166775 Disease Relevance 1.03 Pain Relevance 0.72
Additionally, KA increased the phosphorylation of JNK, especially JNK1, which was attenuated by CHX.
Negative_regulation (attenuated) of Phosphorylation (phosphorylation) of JNK
3) Confidence 0.39 Published 2001 Journal Mol. Cells Section Abstract Doc Link 11355693 Disease Relevance 0 Pain Relevance 0.27
Phosphorylation of c-Jun N-terminal kinase (JNK) in sensory neurones of diabetic rats, with possible effects on nerve conduction and neuropathic pain: prevention with an aldose reductase inhibitor.
Negative_regulation (prevention) of Phosphorylation (Phosphorylation) of c-Jun N-terminal kinase in nerve associated with pain, diabetes mellitus and neuropathic pain
4) Confidence 0.36 Published 2006 Journal Diabetologia Section Title Doc Link 16456679 Disease Relevance 0.30 Pain Relevance 0.30
JNK activation was determined by monitoring phosphorylation of JNK (Thr183 and Tyr185) and c-Jun (Ser63), which is a substrate of JNK.
Negative_regulation (monitoring) of Phosphorylation (phosphorylation) of JNK
5) Confidence 0.30 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2997789 Disease Relevance 0.83 Pain Relevance 0.12
In addition, phosphorylation of JNK and ERK was also determined at 2, 4, 14 or 24 hours after LPS treatment to determine the kinetics of the kinase activation in lung tissue.


Spec (determined) Negative_regulation (determined) of Phosphorylation (phosphorylation) of JNK in lung
6) Confidence 0.28 Published 2004 Journal Respir Res Section Body Doc Link PMC538282 Disease Relevance 0.05 Pain Relevance 0.25
The Rho-kinase inhibitors attenuated the TNF-alpha-induced phosphorylation of both p38 MAP kinase and SAPK/JNK.
Negative_regulation (attenuated) of Phosphorylation (phosphorylation) of JNK
7) Confidence 0.27 Published 2009 Journal Neurochem. Int. Section Abstract Doc Link 19427347 Disease Relevance 0.94 Pain Relevance 0.29
Furthermore, the increased PP2A concentration may intensify GR action not only by inhibition of JNK and p38 phosphorylation, but also by a direct influence on the process of GR translocation.
Negative_regulation (inhibition) of Phosphorylation (phosphorylation) of JNK in PP2A
8) Confidence 0.27 Published 2010 Journal J. Physiol. Pharmacol. Section Abstract Doc Link 20436222 Disease Relevance 0.40 Pain Relevance 0.21
Agmatine reduced phosphorylation of JNK and NF-?
Negative_regulation (reduced) of Phosphorylation (phosphorylation) of JNK
9) Confidence 0.23 Published 2007 Journal BMC Neurosci Section Abstract Doc Link PMC2089075 Disease Relevance 1.33 Pain Relevance 0
and reduces the activation of JNK phosphorylation, with subsequent dose-related
Negative_regulation (reduces) of Phosphorylation (phosphorylation) of JNK
10) Confidence 0.15 Published 2008 Journal Experimental Diabetes Research Section Body Doc Link PMC2323445 Disease Relevance 0.54 Pain Relevance 0.05
Ser-447 phosphorylation by JNK appears to be correlated with ?
Negative_regulation (correlated) of Phosphorylation (phosphorylation) of JNK
11) Confidence 0.12 Published 2009 Journal Molecular & Cellular Proteomics : MCP Section Abstract Doc Link PMC2667352 Disease Relevance 0.09 Pain Relevance 0
On the other hand, when murine T cell is stimulated with mitogen, IL-2 was decreased by andrographolide [66] possibly via reducing nuclear factor of activated T cells (NFAT) activities and increasing JNK phosphorylation [67].
Negative_regulation (reducing) of Phosphorylation (phosphorylation) of JNK in T cells
12) Confidence 0.03 Published 2010 Journal Chin Med Section Body Doc Link PMC2881933 Disease Relevance 0.96 Pain Relevance 0.09

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