INT108338

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Context Info
Confidence 0.67
First Reported 2003
Last Reported 2010
Negated 2
Speculated 0
Reported most in Body
Documents 13
Total Number 17
Disease Relevance 5.42
Pain Relevance 2.92

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
monocytes 2
L929 2
HeLa 2
EPHB2 (Homo sapiens)
Pain Link Frequency Relevance Heat
Kinase C 55 100.00 Very High Very High Very High
Morphine 5 99.98 Very High Very High Very High
opioid receptor 3 97.76 Very High Very High Very High
bradykinin 24 96.84 Very High Very High Very High
b2 receptor 6 95.00 High High
cINOD 9 93.60 High High
Immobilon 8 93.28 High High
Calcium channel 8 92.16 High High
Delta opioid receptors 4 89.84 High High
endometriosis 2 87.76 High High
Disease Link Frequency Relevance Heat
Cancer 141 99.12 Very High Very High Very High
Apoptosis 30 98.48 Very High Very High Very High
Immunization 30 97.72 Very High Very High Very High
Glioma 32 97.48 Very High Very High Very High
Endometriosis (extended) 12 97.20 Very High Very High Very High
INFLAMMATION 15 92.16 High High
Death 3 91.76 High High
Rectal Cancer 1 89.84 High High
Colon Cancer 10 88.96 High High
Reprotox - General 1 5 88.28 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
We have shown activation of the EP2 and FP receptors can lead to phosphorylation of ERK1/2 via the activation of c-Src and transphosphorylation of the epidermal growth factor receptor (EGFR) in Ishikawa cells and endometrial adenocarcinoma explants ex vivo [7,18].
Positive_regulation (lead) of Phosphorylation (phosphorylation) of ERK1 associated with endometriosis (extended)
1) Confidence 0.67 Published 2010 Journal Cell Signal Section Body Doc Link PMC2791881 Disease Relevance 0.45 Pain Relevance 0.13
1A-AR-antibodies result in protein kinase C alpha activation and transient extracellular-related kinase (ERK1/2) phosphorylation.
Positive_regulation (result) of Phosphorylation (phosphorylation) of ERK1 associated with kinase c
2) Confidence 0.67 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2827566 Disease Relevance 0.46 Pain Relevance 0.10
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) Positive_regulation (increased) of Phosphorylation (phosphorylation) of Erk1 in HeLa
3) Confidence 0.49 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
For the ERK1/2 phosphorylation experiments, 50 µg of IgG purified from sera of rats 3 months after immunization and controls were added to the CHO/?
Positive_regulation (experiments) of Phosphorylation (phosphorylation) of ERK1 associated with immunization
4) Confidence 0.49 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2827566 Disease Relevance 0.32 Pain Relevance 0.20
Phosphorylation of Ser112 by ERK1/2 inactivates Bad and protects the tumor cell from apoptosis.
Positive_regulation (inactivates) of Phosphorylation (Phosphorylation) of ERK associated with cancer and apoptosis
5) Confidence 0.49 Published 2003 Journal Cancer Res. Section Abstract Doc Link 12566304 Disease Relevance 1.48 Pain Relevance 0.18
We have shown activation of the EP2 and FP receptors can lead to phosphorylation of ERK1/2 via the activation of c-Src and transphosphorylation of the epidermal growth factor receptor (EGFR) in Ishikawa cells and endometrial adenocarcinoma explants ex vivo [7,18].
Positive_regulation (activation) of Phosphorylation (transphosphorylation) of ERK1 associated with endometriosis (extended)
6) Confidence 0.49 Published 2010 Journal Cell Signal Section Body Doc Link PMC2791881 Disease Relevance 0.45 Pain Relevance 0.13
The immunoblot presented in Figure 5b shows that L929 cells expressing caRas exhibited higher degrees of Erk1/2 phosphorylation than control-transfected cells when grown in the absence of VPA (Figure 5b, lanes 2 and 1).
Positive_regulation (degrees) of Phosphorylation (phosphorylation) of Erk1 in L929
7) Confidence 0.49 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
Treatment with NIM811 significantly enhanced the phosphorylation of JNK and p38 MAPK in a concentration-dependent manner, but did not enhance the phosphorylation of ERK1/2 (Fig. 5A–C).
Neg (not) Positive_regulation (enhance) of Phosphorylation (phosphorylation) of ERK1
8) Confidence 0.49 Published 2007 Journal Liver International Section Body Doc Link PMC2156109 Disease Relevance 0.32 Pain Relevance 0
Intracellular effects of B2 stimulation were the following: (a) the increase of free intracellular Ca(2+) concentration by a mechanism dependent upon the phospholipase C (PLC) activity; (b) the cytosol-to-membrane translocation of conventional (PKC)-alpha and -beta isozymes, novel PKC-delta, -epsilon, and -eta isozymes; (c) the phosphorylation of the extracellular-regulated kinase 1 and 2 (ERK1/2); and (d) the stimulation of the expression of c-Fos protein.
Positive_regulation (upon) of Phosphorylation (phosphorylation) of ERK
9) Confidence 0.49 Published 2004 Journal J. Cell. Physiol. Section Abstract Doc Link 15281091 Disease Relevance 0.42 Pain Relevance 0.52
Intracellular effects of B2 stimulation were the following: (a) the increase of free intracellular Ca(2+) concentration by a mechanism dependent upon the phospholipase C (PLC) activity; (b) the cytosol-to-membrane translocation of conventional (PKC)-alpha and -beta isozymes, novel PKC-delta, -epsilon, and -eta isozymes; (c) the phosphorylation of the extracellular-regulated kinase 1 and 2 (ERK1/2); and (d) the stimulation of the expression of c-Fos protein.
Positive_regulation (increase) of Phosphorylation (phosphorylation) of ERK
10) Confidence 0.49 Published 2004 Journal J. Cell. Physiol. Section Abstract Doc Link 15281091 Disease Relevance 0.44 Pain Relevance 0.53
In contrast, prolonged exposure of HEK293 cells to morphine excited persistent phosphorylation of ERK/MAP kinases, and those cells failed to internalize the opioid receptor.
Positive_regulation (excited) of Phosphorylation (phosphorylation) of ERK associated with opioid receptor and morphine
11) Confidence 0.49 Published 2004 Journal J. Pharmacol. Exp. Ther. Section Abstract Doc Link 14742744 Disease Relevance 0 Pain Relevance 0.86
Stimulation of hRPE cells by monocytes resulted in prominent increases in p38, ERK1/2 and JNK/SAPK phosphorolation, IkappaBalpha degradation, and NF-kappaB nuclear translocation.
Positive_regulation (increases) of Phosphorylation (phosphorolation) of ERK in monocytes
12) Confidence 0.49 Published 2003 Journal Exp. Eye Res. Section Abstract Doc Link 12697421 Disease Relevance 0.14 Pain Relevance 0.24
For example, VPA increased the degree of Erk1/2 phosphorylation in BT4Cn and N2a cells.
Positive_regulation (increased) of Phosphorylation (phosphorylation) of Erk1
13) Confidence 0.45 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
In conclusion, we demonstrate that VPA exposure induced considerable cell type-specific effects on HDAC inhibition, Erk1/2 phosphorylation, cell growth and motility.
Positive_regulation (induced) of Phosphorylation (phosphorylation) of Erk1
14) Confidence 0.45 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0.50 Pain Relevance 0
As expected, VPA increased the degree of Erk1/2 phosphorylation compared with untreated cells (Figure 5g, lanes 1 and 3).
Positive_regulation (increased) of Phosphorylation (phosphorylation) of Erk1
15) Confidence 0.45 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
In the presence of minimal amounts EPO, we also found increased Erk1/2 phosphorylation, which suggests greatly augmented activity of the receptor (Figure 6B).
Positive_regulation (increased) of Phosphorylation (phosphorylation) of Erk1
16) Confidence 0.45 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2916842 Disease Relevance 0.06 Pain Relevance 0.04
induced ERK1/2 phosphorylation by
Positive_regulation (induced) of Phosphorylation (phosphorylation) of ERK1
17) Confidence 0.45 Published 2008 Journal PPAR Research Section Body Doc Link PMC2440494 Disease Relevance 0.40 Pain Relevance 0

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