INT110181

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Context Info
Confidence 0.57
First Reported 2003
Last Reported 2011
Negated 0
Speculated 0
Reported most in Body
Documents 20
Total Number 20
Disease Relevance 9.43
Pain Relevance 4.06

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) nucleoplasm (MAPK8) mitochondrion (MAPK8)
nucleus (MAPK8) response to stress (MAPK8) cytoplasm (MAPK8)
Anatomy Link Frequency
vessels 2
MAPK8 (Homo sapiens)
Pain Link Frequency Relevance Heat
Inflammation 127 100.00 Very High Very High Very High
Paracetamol 8 100.00 Very High Very High Very High
Leflunomide 8 99.74 Very High Very High Very High
Nicotine 192 99.72 Very High Very High Very High
Morphine 10 99.52 Very High Very High Very High
cytokine 36 98.44 Very High Very High Very High
Inflammatory mediators 9 91.88 High High
metalloproteinase 12 90.88 High High
Kinase C 5 89.80 High High
Cannabinoid 1 86.44 High High
Disease Link Frequency Relevance Heat
INFLAMMATION 155 100.00 Very High Very High Very High
Apoptosis 111 98.04 Very High Very High Very High
Hypersensitivity 7 96.88 Very High Very High Very High
Stress 48 94.80 High High
Increased Venous Pressure Under Development 6 94.48 High High
Injury 13 94.32 High High
Shock 8 91.52 High High
Cancer 463 91.48 High High
Asthma 30 91.40 High High
Sepsis 1 90.92 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
ROS in turn exerted feedback regulation on JNK activation, as shown by the observations that cyclosporin A and the antioxidant N-acetylcysteine significantly inhibited the phosphorylation of JNK induced by morphine.
Negative_regulation (inhibited) of Phosphorylation (phosphorylation) of JNK associated with morphine
1) Confidence 0.57 Published 2009 Journal FEBS J. Section Abstract Doc Link 19292871 Disease Relevance 0.38 Pain Relevance 0.69
A decreased level of phosphorylated JNK but not of total JNK was induced by siRNA-mediated podoplanin knockdown (Figures 6D and 7C), suggesting that podoplanin could induce JNK phosphorylation.
Negative_regulation (decreased) of Phosphorylation (phosphorylated) of JNK
2) Confidence 0.42 Published 2010 Journal Mol Cancer Section Body Doc Link PMC2987985 Disease Relevance 0.27 Pain Relevance 0.04
In addition, significant upregulation of VEGF-C mRNA (Figure 7B) and a decreased level of phosphorylated JNK (Figure 7C) were also induced in H157 cells treated with siRNA-podoplanin.
Negative_regulation (decreased) of Phosphorylation (phosphorylated) of JNK
3) Confidence 0.42 Published 2010 Journal Mol Cancer Section Body Doc Link PMC2987985 Disease Relevance 0.17 Pain Relevance 0
As a result, significant upregulation of VEGF-C mRNA (Figure 6C) and a decreased level of phosphorylated JNK (Figure 6D) were induced in EBC1-P4 cells treated with siRNA-podoplanin.
Negative_regulation (decreased) of Phosphorylation (phosphorylated) of JNK
4) Confidence 0.42 Published 2010 Journal Mol Cancer Section Body Doc Link PMC2987985 Disease Relevance 0.07 Pain Relevance 0
Instead, we demonstrate that leflunomide (20 microM) inhibited the APAP-induced early (3 h) activation (phosphorylation) of JNK1/2, thus inhibiting phosphorylation of the anti-apoptotic protein Bcl-2 and preventing P-Bcl-2-mediated induction of the mPT.
Negative_regulation (inhibited) of Phosphorylation (phosphorylation) of JNK associated with paracetamol, leflunomide and apoptosis
5) Confidence 0.42 Published 2006 Journal Toxicol. Appl. Pharmacol. Section Abstract Doc Link 16979204 Disease Relevance 0.75 Pain Relevance 0.97
It has been reported that JNK can phosphorylate the ?
Negative_regulation (reported) of Phosphorylation (phosphorylate) of JNK
6) Confidence 0.39 Published 2008 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2427353 Disease Relevance 0.08 Pain Relevance 0
AEA triggered phosphorylation of c-Jun NH(2)-terminal kinase (JNK) and p38 mitogen activated protein kinase.
Negative_regulation (triggered) of Phosphorylation (phosphorylation) of JNK
7) Confidence 0.34 Published 2003 Journal Thromb. Haemost. Section Abstract Doc Link 12719786 Disease Relevance 0.82 Pain Relevance 0.20
Furthermore, Trolox attenuated indomethacin-induced increased phosphorylation in ERK, p38 MAPK, JNK, and AKT.
Negative_regulation (attenuated) of Phosphorylation (phosphorylation) of JNK
8) Confidence 0.32 Published 2007 Journal Eur. J. Pharmacol. Section Abstract Doc Link 17341418 Disease Relevance 0.61 Pain Relevance 0.05
According to results in Figure 5A, phosphorylation of JNK was observed at 30 min after Pa-PDT treatment, where the native form of JNK was slightly decreased.
Negative_regulation (decreased) of Phosphorylation (form) of JNK
9) Confidence 0.27 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2731730 Disease Relevance 0.66 Pain Relevance 0
Our initial studies indicated that DAG-dependent PKC isoforms are involved in the response since PMA was able to mimic the effect of PAR2 activation, abolishing both JNK activity and phosphorylation.
Negative_regulation (abolishing) of Phosphorylation (phosphorylation) of JNK
10) Confidence 0.21 Published 2010 Journal Cellular Signalling Section Body Doc Link PMC2806525 Disease Relevance 0 Pain Relevance 0.12
Therefore, we tested the effect of the PKC inhibitor GF109203X on PAR2 mediated inhibition of JNK activity and phosphorylation.
Negative_regulation (inhibition) of Phosphorylation (phosphorylation) of JNK
11) Confidence 0.21 Published 2010 Journal Cellular Signalling Section Body Doc Link PMC2806525 Disease Relevance 0 Pain Relevance 0.07
We found increased phosphorylation of JNK and p38 in samples stimulated with IL-1?
Negative_regulation (found) of Phosphorylation (phosphorylation) of JNK
12) Confidence 0.21 Published 2007 Journal Arthritis Res Ther Section Body Doc Link PMC2212570 Disease Relevance 0.38 Pain Relevance 0.19
There is also evidence suggesting that nicotine can directly interfere with the phosphorylation of intracellular inflammatory signal molecules such as c-Jun N-terminal kinase (JNK) and ERK1/2, without involvement of the nicotinic receptors [13].
Negative_regulation (interfere) of Phosphorylation (phosphorylation) of c-Jun N-terminal kinase associated with inflammation and nicotine
13) Confidence 0.20 Published 2010 Journal Respir Res Section Body Doc Link PMC2845563 Disease Relevance 0.69 Pain Relevance 0.53
M, SP600125 selectively inhibits the phosphorylation of JNK, but not ERK1/2 or p38 in vessels [39].
Negative_regulation (inhibits) of Phosphorylation (phosphorylation) of JNK in vessels
14) Confidence 0.19 Published 2010 Journal Respir Res Section Body Doc Link PMC2845563 Disease Relevance 0.16 Pain Relevance 0.32
Opposite the p38 MAPK inhibitors, JNK-MAPK pathway inhibitor SP600125 showed no effect on SRP72 phosphorylation in rhIL-1?
Negative_regulation (Opposite) of Phosphorylation (phosphorylation) of JNK
15) Confidence 0.19 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0.08 Pain Relevance 0
The observed increase in phosphorylation of p38 MAPKs and c-Jun N-terminal kinase 1/2 (JNK1/2) was inhibited by the use of the singlet oxygen scavenger L-histidine, showing that MAPKs pathways are activated via the induction of oxidative stress in HK-1 cells, whereas blocking the expression p38a MAPK (p38a) and p38b MAPK (p38b) isoforms of the MAPKs enhanced the HY-PDT-induced apoptosis of HK-1.
Negative_regulation (inhibited) of Phosphorylation (phosphorylation) of JNK1 associated with stress, cancer and apoptosis
16) Confidence 0.10 Published 2010 Journal International Journal of Molecular Sciences Section Body Doc Link PMC2852855 Disease Relevance 1.57 Pain Relevance 0.11
SP600125 is a reversible ATP-competitive inhibitor of JNK that prevents the phosphorylation of JNK substrates.
Negative_regulation (prevents) of Phosphorylation (phosphorylation) of JNK
17) Confidence 0.09 Published 2010 Journal BMC Microbiol Section Body Doc Link PMC3022711 Disease Relevance 0.09 Pain Relevance 0
Semapimod® is a synthetic guanylhydrazone that inhibits 1) signal transduction pathways by preventing phosphorylation of p38 MAP kinase and JNK; 2) production of the proinflammatory cytokines TNF-alpha, IL-1, IL-6.
Negative_regulation (preventing) of Phosphorylation (phosphorylation) of JNK associated with cytokine
18) Confidence 0.06 Published 2008 Journal International Journal of Nanomedicine Section Body Doc Link PMC2626933 Disease Relevance 0.64 Pain Relevance 0.20
Sal-B treatment effectively inhibits MMP-2 and MMP-9 activitation and expression both cell culture and animal models, and it also, downregulates JNK and ERK phosphorylation [36, 37].
Negative_regulation (downregulates) of Phosphorylation (phosphorylation) of JNK
19) Confidence 0.05 Published 2011 Journal Journal of Oncology Section Body Doc Link PMC3010684 Disease Relevance 0.89 Pain Relevance 0.26
Sal-B has been reported to attenuate significantly COX-2 expression and PGE2 production with or without lipopolysaccharide (LPS)-induced both in vitro and in vivo [24, 25, 29], and which may be attributed to the downregulation of JNK and ERK phosphorylation and blockage of MAPKs phosphorylation [29].

3.2.

Negative_regulation (downregulation) of Phosphorylation (phosphorylation) of JNK
20) Confidence 0.05 Published 2011 Journal Journal of Oncology Section Body Doc Link PMC3010684 Disease Relevance 1.14 Pain Relevance 0.28

General Comments

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