INT95734

From wiki-pain
Jump to: navigation, search
Context Info
Confidence 0.82
First Reported 2001
Last Reported 2011
Negated 2
Speculated 4
Reported most in Abstract
Documents 108
Total Number 113
Disease Relevance 49.92
Pain Relevance 33.52

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
neurons 9
nerve 5
spinal cord 4
astrocytes 4
brain 3
Mapk8 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
Pain 80 100.00 Very High Very High Very High
nociceptor 10 100.00 Very High Very High Very High
Paracetamol 23 99.82 Very High Very High Very High
noradrenaline 22 99.82 Very High Very High Very High
cva 56 99.80 Very High Very High Very High
Spinal cord 102 99.68 Very High Very High Very High
tolerance 81 99.66 Very High Very High Very High
agonist 215 99.60 Very High Very High Very High
Thermal hyperalgesia 17 99.52 Very High Very High Very High
Nerve growth factor 10 99.52 Very High Very High Very High
Disease Link Frequency Relevance Heat
Stress 752 100.00 Very High Very High Very High
Insulin Resistance 123 100.00 Very High Very High Very High
Hemorrhage 42 99.80 Very High Very High Very High
Nervous System Injury 20 99.64 Very High Very High Very High
Injury 272 99.58 Very High Very High Very High
Hyperalgesia 38 99.52 Very High Very High Very High
Poisoning 38 99.38 Very High Very High Very High
Ganglion Cysts 73 99.32 Very High Very High Very High
Obesity 123 99.12 Very High Very High Very High
Diabetes Mellitus 113 99.10 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Phosphorylation of c-Jun N-terminal kinase isoforms and their different roles in spinal cord dorsal horn and primary somatosensory cortex.
Phosphorylation (Phosphorylation) of c-Jun N-terminal kinase in spinal cord dorsal horn associated with primary somatosensory cortex, nociceptor, dorsal horn and spinal cord
1) Confidence 0.82 Published 2007 Journal Neurosci. Lett. Section Title Doc Link 17923323 Disease Relevance 0.21 Pain Relevance 1.00
Subcutaneous bee venom (BV)-induced persistent pain stimulation resulted in a significant increase in the phosphorylation of both JNK isoforms in each area for a long period (lasting at least 48 h).
Phosphorylation (osphorylation o) of JNK associated with pain and lasting pain
2) Confidence 0.82 Published 2007 Journal Neurosci. Lett. Section Abstract Doc Link 17923323 Disease Relevance 0.30 Pain Relevance 0.54
An i.pl. injection of nerve growth factor (NGF) also induced the phosphorylation of JNK as well as thermal hyperalgesia, and SP600125 improved hyperalgesia.
Phosphorylation (phosphorylation) of JNK in nerve associated with hyperalgesia, nerve growth factor and thermal hyperalgesia
3) Confidence 0.82 Published 2005 Journal Biochem. Biophys. Res. Commun. Section Abstract Doc Link 16055088 Disease Relevance 1.30 Pain Relevance 1.02
The phosphorylation of c-Jun NH (2)-terminal protein kinase (JNK), one of the mitogen-activated protein kinases, was analyzed in the sciatic nerves of Lewis rats with experimental autoimmune neuritis (EAN).
Spec (analyzed) Phosphorylation (phosphorylation) of JNK in sciatic nerves associated with experimental autoimmune neuritis, sciatic nerve and neuritis
4) Confidence 0.82 Published 2006 Journal J. Vet. Sci. Section Abstract Doc Link 16434843 Disease Relevance 0.65 Pain Relevance 0.58
These findings suggest that JNK phosphorylation is closely associated with the clearance of inflammatory cells as well as the activation of Schwann cells in the EAN affected sciatic nerves.
Phosphorylation (phosphorylation) of JNK in sciatic nerves associated with inflammation, sciatic nerve and neuritis
5) Confidence 0.82 Published 2006 Journal J. Vet. Sci. Section Abstract Doc Link 16434843 Disease Relevance 1.25 Pain Relevance 0.99
However, phosphorylated JNK 46 kDa was normally expressed in the S1 area, but not in the spinal cord, while neither of the two structures contained phosphorylated JNK 54 kDa.
Neg (neither) Phosphorylation (phosphorylated) of JNK in spinal cord associated with spinal cord
6) Confidence 0.81 Published 2007 Journal Neurosci. Lett. Section Abstract Doc Link 17923323 Disease Relevance 0.24 Pain Relevance 0.54
However, phosphorylated JNK 46 kDa was normally expressed in the S1 area, but not in the spinal cord, while neither of the two structures contained phosphorylated JNK 54 kDa.
Phosphorylation (phosphorylated) of JNK in spinal cord associated with spinal cord
7) Confidence 0.81 Published 2007 Journal Neurosci. Lett. Section Abstract Doc Link 17923323 Disease Relevance 0.18 Pain Relevance 0.47
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.
Phosphorylation (Phosphorylation) of JNK in nerve associated with pain, diabetes mellitus and neuropathic pain
8) Confidence 0.80 Published 2006 Journal Diabetologia Section Title Doc Link 16456679 Disease Relevance 0.29 Pain Relevance 0.30
AIMS/HYPOTHESIS: This study was designed to determine whether diabetes in rats is associated with phosphorylation of c-Jun N-terminal kinase (JNK) and one of its transcription factors, c-Jun, in sensory neurones innervating the lower limb.
Phosphorylation (phosphorylation) of JNK in lower limb associated with diabetes mellitus
9) Confidence 0.80 Published 2006 Journal Diabetologia Section Abstract Doc Link 16456679 Disease Relevance 0.25 Pain Relevance 0.07
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.
Phosphorylation (phosphorylation) of JNK in nociceptors
10) Confidence 0.80 Published 2006 Journal Diabetologia Section Body Doc Link 16456679 Disease Relevance 0 Pain Relevance 0
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.
Phosphorylation (phosphorylation) of JNK in neuronal
11) Confidence 0.80 Published 2006 Journal Diabetologia Section Abstract Doc Link 16456679 Disease Relevance 0.24 Pain Relevance 0.07
Phosphorylation of JNK and c-Jun in lumbar dorsal root ganglia was determined by binding of phospho-specific antibodies using western blots and immunocytochemistry.
Phosphorylation (Phosphorylation) of JNK in dorsal root ganglia
12) Confidence 0.80 Published 2006 Journal Diabetologia Section Body Doc Link 16456679 Disease Relevance 0 Pain Relevance 0
Phosphorylation of p44/42 and SAPK/JNK was detected in all tissues following both sham and SLH, and this effect was significantly more pronounced following SLH (P < 0.05).
Phosphorylation (Phosphorylation) of JNK associated with cva
13) Confidence 0.80 Published 2002 Journal Shock Section Abstract Doc Link 12166775 Disease Relevance 1.04 Pain Relevance 0.72
Protein was isolated from tissues for determination of p44/42 and SAPK/JNK phosphorylation by Western blot analysis.
Phosphorylation (phosphorylation) of JNK
14) Confidence 0.80 Published 2002 Journal Shock Section Abstract Doc Link 12166775 Disease Relevance 1.02 Pain Relevance 0.71
The induction of tolerance by SLH leads to phosphorylation of both p44/42 and SAPK/JNK MAP-kinases.
Phosphorylation (phosphorylation) of JNK associated with tolerance and cva
15) Confidence 0.80 Published 2002 Journal Shock Section Abstract Doc Link 12166775 Disease Relevance 0.85 Pain Relevance 0.64
The sciatic nerve and the lumbar tract of the spinal cord were processed to evaluate the levels of the phosphorylated form of PKCgamma, ERK 1,2, SAP/JNK, p-38 and c-Jun; furthermore, the mRNA expression of the early genes c-Jun and c-Fos has been investigated.
Phosphorylation (phosphorylated) of JNK in spinal cord associated with sciatic nerve and spinal cord
16) Confidence 0.80 Published 2010 Journal Neuroscience Section Abstract Doc Link 19925851 Disease Relevance 0.57 Pain Relevance 0.57
G. elata resulted in phosphorylation and dephosphorylation of ERK1/2 and JNK1/2-p38 MAPKs (members of the serine/threonine kinase family), respectively, as revealed by Western blot analysis.
Phosphorylation (phosphorylation) of JNK
17) Confidence 0.80 Published 2004 Journal Life Sci. Section Abstract Doc Link 15261768 Disease Relevance 0.76 Pain Relevance 0.09
G. elata resulted in phosphorylation and dephosphorylation of ERK1/2 and JNK1/2-p38 MAPKs (members of the serine/threonine kinase family), respectively, as revealed by Western blot analysis.
Phosphorylation (dephosphorylation) of JNK
18) Confidence 0.79 Published 2004 Journal Life Sci. Section Abstract Doc Link 15261768 Disease Relevance 0.76 Pain Relevance 0.09
Additionally, KA increased the phosphorylation of JNK, especially JNK1, which was attenuated by CHX.
Phosphorylation (phosphorylation) of JNK
19) Confidence 0.76 Published 2001 Journal Mol. Cells Section Abstract Doc Link 11355693 Disease Relevance 0 Pain Relevance 0.27
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.
Phosphorylation (phosphorylation) of JNK in hippocampus associated with hippocampus
20) Confidence 0.76 Published 2001 Journal Mol. Cells Section Abstract Doc Link 11355693 Disease Relevance 0 Pain Relevance 0.26

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox