INT108334

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Context Info
Confidence 0.57
First Reported 2003
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 4
Total Number 16
Disease Relevance 2.27
Pain Relevance 1.16

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 (EPHB2)
Anatomy Link Frequency
HeLa 2
L929 2
colon 2
EPHB2 (Homo sapiens)
Pain Link Frequency Relevance Heat
cINOD 2 99.74 Very High Very High Very High
opioid receptor 3 99.72 Very High Very High Very High
Morphine 5 98.32 Very High Very High Very High
Immobilon 16 88.52 High High
Delta opioid receptors 4 85.08 High High
addiction 4 84.64 Quite High
Glutamate 1 84.24 Quite High
agonist 1 75.04 Quite High
opiate 1 74.68 Quite High
Kinase C 79 66.32 Quite High
Disease Link Frequency Relevance Heat
INFLAMMATION 3 99.62 Very High Very High Very High
Colon Cancer 7 99.60 Very High Very High Very High
Apoptosis 34 96.72 Very High Very High Very High
Cancer 188 95.92 Very High Very High Very High
Death 2 84.72 Quite High
Rectal Cancer 1 82.80 Quite High
Epilepsy 27 78.12 Quite High
Pancreatic Cancer 44 71.84 Quite High
Metastasis 15 47.68 Quite Low
Non-small-cell Lung Cancer 1 38.88 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
After 6 and 24 h, the degree of Erk1/2 phosphorylation decreased further.
Negative_regulation (decreased) of Phosphorylation (phosphorylation) of Erk1
1) Confidence 0.57 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
When ERK/MAP kinase phosphorylation was blocked by 2'-Amino-3'-methoxyflavone (PD98059), morphine gained the ability to strongly induce DOR endocytosis.
Negative_regulation (blocked) of Phosphorylation (phosphorylation) of ERK associated with morphine
2) Confidence 0.57 Published 2004 Journal J. Pharmacol. Exp. Ther. Section Abstract Doc Link 14742744 Disease Relevance 0 Pain Relevance 0.94
Erk1/2 phosphorylation was significantly decreased in CSML0 and L929, significantly increased in CSML100, BT4Cn and N2a, and not significantly affected in BT4C, U87MG, PC12-E2, HeLa and Swiss 3T3.
Neg (not) Negative_regulation (decreased) of Phosphorylation (phosphorylation) of Erk1 in HeLa
3) Confidence 0.57 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
In L929 cells, VPA inhibits the degree of Erk1/2 phosphorylation (Figure 1) and cell speed [21].
Negative_regulation (inhibits) of Phosphorylation (phosphorylation) of Erk1 in L929
4) Confidence 0.57 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
However, VPA caused equally strong inhibition of Erk1/2 phosphorylation in control- and caRas-transfected cells (Figure 5b, lanes 3 and 4).
Negative_regulation (inhibition) of Phosphorylation (phosphorylation) of Erk1
5) Confidence 0.42 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
Moreover, cell growth, motility and the degree of Erk1/2 phosphorylation were inhibited, activated, or unaffected by VPA in a cell type-specific manner.
Negative_regulation (inhibited) of Phosphorylation (phosphorylation) of Erk1
6) Confidence 0.42 Published 2010 Journal BMC Cancer Section Abstract Doc Link PMC2918577 Disease Relevance 0.23 Pain Relevance 0
A 1 h exposure to 3 mM VPA significantly decreased the degree of Erk1/2 phosphorylation.
Negative_regulation (decreased) of Phosphorylation (phosphorylation) of Erk1
7) Confidence 0.42 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
At a pre-clinical level, one of the studies mentioned earlier demonstrated reduction in phosphorylation of ERK1/2 (extracellular-regulated kinase), part of the ras-Raf transduction effector cascade, in one of the xenograft models with no effect on phospho-PKB (protein kinase B), part of the PI3-kinase/Akt pathway, in either pancreatic xenograft (Ng et al 2002).
Negative_regulation (reduction) of Phosphorylation (phosphorylation) of ERK1
8) Confidence 0.42 Published 2006 Journal Therapeutics and Clinical Risk Management Section Body Doc Link PMC1936363 Disease Relevance 0.47 Pain Relevance 0.04
VPA dose-dependently inhibited the degree of Erk1/2 phosphorylation, with estimated IC25 and IC50 values of ~0.24 and 0.58 mM, respectively.
Negative_regulation (inhibited) of Phosphorylation (phosphorylation) of Erk1
9) Confidence 0.42 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
Furthermore, the effects of VPA on the degree of Erk1/2 phosphorylation and HDAC inhibition were not related to the degree of Erk1/2 phosphorylation and acetylation in the absence of the drug.
Negative_regulation (degree) of Phosphorylation (phosphorylation) of Erk1
10) Confidence 0.41 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
In conclusion, VPA has highly cell type-specific effects on the degree of HDAC inhibition and on changes in the degree of Erk1/2 phosphorylation.
Negative_regulation (degree) of Phosphorylation (phosphorylation) of Erk1
11) Confidence 0.41 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
Sulindac metabolites and other nonsteroidal anti-inflammatory drugs selectively inhibit ERK1/2 phosphorylation in human colon cancer cells.
Negative_regulation (inhibit) of Phosphorylation (phosphorylation) of ERK in colon associated with inflammation, colon cancer and cinod
12) Confidence 0.41 Published 2003 Journal Cancer Res. Section Abstract Doc Link 12566304 Disease Relevance 1.43 Pain Relevance 0.17
Finally, no relationship was found between the effects of VPA on HDAC inhibition and the degree of Erk1/2 phosphorylation.
Negative_regulation (degree) of Phosphorylation (phosphorylation) of Erk1
13) Confidence 0.41 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
Figure 1b and 1c show the relative changes in the degree of Erk1/2 phosphorylation in the respective cell lines in response to VPA (3 mM, 48 h).
Negative_regulation (degree) of Phosphorylation (phosphorylation) of Erk1
14) Confidence 0.41 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
Therefore, effects of VPA on the degree of Erk1/2 phosphorylation and HDAC inhibition seem to be independent responses that, subsequently, may modulate biological processes such as cell growth or motility through independent mechanisms.
Negative_regulation (inhibition) of Phosphorylation (phosphorylation) of Erk1
15) Confidence 0.41 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0.13 Pain Relevance 0
Furthermore, the effects of VPA on the degree of Erk1/2 phosphorylation and HDAC inhibition were not related to the degree of Erk1/2 phosphorylation and acetylation in the absence of the drug.
Negative_regulation (inhibition) of Phosphorylation (phosphorylation) of Erk1
16) Confidence 0.41 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0

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