INT117713

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Context Info
Confidence 0.82
First Reported 2004
Last Reported 2010
Negated 1
Speculated 2
Reported most in Body
Documents 275
Total Number 283
Disease Relevance 95.82
Pain Relevance 54.34

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

nucleoplasm (Akt1) transport (Akt1) aging (Akt1)
enzyme binding (Akt1) carbohydrate metabolic process (Akt1) cytoplasm (Akt1)
Anatomy Link Frequency
hearts 15
muscle 14
kidney cortex 7
myocardium 5
liver 4
Akt1 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
opioid receptor 3682 100.00 Very High Very High Very High
Morphine 163 99.98 Very High Very High Very High
antagonist 1246 99.80 Very High Very High Very High
qutenza 27 99.68 Very High Very High Very High
Pyramidal cell 14 99.68 Very High Very High Very High
Paracetamol 2344 99.56 Very High Very High Very High
Dopamine 693 99.54 Very High Very High Very High
dorsal root ganglion 16 99.52 Very High Very High Very High
Nucleus accumbens 21 99.40 Very High Very High Very High
fibrosis 255 99.36 Very High Very High Very High
Disease Link Frequency Relevance Heat
Reperfusion Injury 101 100.00 Very High Very High Very High
Aging 1514 99.92 Very High Very High Very High
Bordatella Infection 7 99.92 Very High Very High Very High
Diabetes Mellitus 3037 99.82 Very High Very High Very High
Hyperglycemia 496 99.76 Very High Very High Very High
Stroke 145 99.72 Very High Very High Very High
Apoptosis 1728 99.64 Very High Very High Very High
Myocardial Infarction 1611 99.64 Very High Very High Very High
Ganglion Cysts 20 99.52 Very High Very High Very High
Fibrosis 225 99.36 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Moreover, an inhibitor of glycogen synthase kinase-3beta (GSK3beta), a kinase whose activity is blocked by Akt-mediated phosphorylation, promoted mitochondrial movement.
Phosphorylation (phosphorylation) of Akt
1) Confidence 0.82 Published 2007 Journal Mol. Cell. Neurosci. Section Abstract Doc Link 17904380 Disease Relevance 0 Pain Relevance 0.25
Phosphorylated Akt levels in the nucleus accumbens were significantly increased after a single morphine injection.
Phosphorylation (Phosphorylated) of Akt in nucleus accumbens associated with nucleus accumbens and morphine
2) Confidence 0.81 Published 2004 Journal J. Pharmacol. Exp. Ther. Section Abstract Doc Link 15056728 Disease Relevance 0 Pain Relevance 1.09
In vivo regulation of extracellular signal-regulated protein kinase (ERK) and protein kinase B (Akt) phosphorylation by acute and chronic morphine.
Phosphorylation (phosphorylation) of Akt associated with morphine
3) Confidence 0.81 Published 2004 Journal J. Pharmacol. Exp. Ther. Section Title Doc Link 15056728 Disease Relevance 0 Pain Relevance 0.72
In vivo regulation of extracellular signal-regulated protein kinase (ERK) and protein kinase B (Akt) phosphorylation by acute and chronic morphine.
Phosphorylation (phosphorylation) of protein kinase B associated with morphine
4) Confidence 0.81 Published 2004 Journal J. Pharmacol. Exp. Ther. Section Title Doc Link 15056728 Disease Relevance 0 Pain Relevance 0.72
Cultured DRG neurons confirmed that phosphorylation of Akt in different cellular compartments is triggered by depolarization or receptor activation, and suggested that this effect is mediated in part by phosphatidylinositol 3-kinase.
Phosphorylation (phosphorylation) of Akt in neurons associated with dorsal root ganglion
5) Confidence 0.81 Published 2005 Journal Eur. J. Neurosci. Section Abstract Doc Link 15869474 Disease Relevance 0.48 Pain Relevance 0.67
Activity-dependent phosphorylation of Akt/PKB in adult DRG neurons.
Phosphorylation (phosphorylation) of Akt in neurons associated with qutenza
6) Confidence 0.81 Published 2005 Journal Eur. J. Neurosci. Section Title Doc Link 15869474 Disease Relevance 0.47 Pain Relevance 0.58
ERK and Akt are activated by phosphorylation, hence the levels of phosphorylated ERK (pERK) and Akt (pAkt) as well as total levels of ERK and Akt protein were measured by Western blot analysis.
Phosphorylation (phosphorylated) of Akt
7) Confidence 0.81 Published 2004 Journal J. Pharmacol. Exp. Ther. Section Abstract Doc Link 15056728 Disease Relevance 0 Pain Relevance 0.71
In contrast, AMPH activates phosphoinositide-3 kinase substrates, like protein kinase B/Akt, only in the nuclei of striatal cells but this transient increase induced by AMPH is followed by a delayed decrease in protein kinase B/Akt phosphorylation whether or not the rats have a drug history, suggesting that the phosphoinositide-3 kinase pathway is not essential for AMPH-induced behavioral sensitization.
Neg (not) Spec (whether) Phosphorylation (phosphorylation) of Akt
8) Confidence 0.80 Published 2008 Journal J. Neurochem. Section Abstract Doc Link 18221378 Disease Relevance 0 Pain Relevance 0.28
Phosphorylated p38 mitogen-activated protein kinase, c-jun N-terminal protein kinases, extracellular signal-regulated kinases and Akt at 45 min of reperfusion were similar between groups.
Phosphorylation (Phosphorylated) of Akt
9) Confidence 0.80 Published 2009 Journal Eur J Anaesthesiol Section Body Doc Link 19359990 Disease Relevance 0.11 Pain Relevance 0
Paradoxically, these increases in Akt phosphorylation were associated with diminished mammalian target of rapamycin (mTOR) phosphorylation, along with decreased levels of insulin receptor beta (IR-?)
Phosphorylation (phosphorylation) of Akt
10) Confidence 0.79 Published 2009 Journal PLoS ONE Section Abstract Doc Link PMC2712760 Disease Relevance 0.24 Pain Relevance 0.17
Taken together, these two different sets of experiments both suggest that aging in the F344BN soleus is associated with a mismatch between Akt phosphorylation and Akt kinase activity.
Phosphorylation (phosphorylation) of Akt kinase in soleus associated with aging
11) Confidence 0.79 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2712760 Disease Relevance 0.30 Pain Relevance 0.09
were similar after insulin incubation between age-matched control and acetaminophen-treated rats, while there was higher phosphorylation of Akt Ser473 and Thr308 in the age-matched controls compared to that from acetaminophen-treated rats (Figure 4B).


Phosphorylation (phosphorylation) of Akt Ser473 associated with paracetamol
12) Confidence 0.79 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2712760 Disease Relevance 0.08 Pain Relevance 0.59
This increase in PTEN protein appeared to parallel decreases in the amount of Akt-Thr308 phosphorylation which support the notion that a loss of PTEN protein with aging may contribute to the hyper-phosphorylation of Akt, and that acetaminophen intervention may function in reducing Akt phosphorylation by increasing PTEN levels.
Phosphorylation (phosphorylation) of Akt associated with paracetamol and aging
13) Confidence 0.79 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2712760 Disease Relevance 0.49 Pain Relevance 0.40
Taken together, these two different sets of experiments both suggest that aging in the F344BN soleus is associated with a mismatch between Akt phosphorylation and Akt kinase activity.
Phosphorylation (phosphorylation) of Akt in soleus associated with aging
14) Confidence 0.79 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2712760 Disease Relevance 0.30 Pain Relevance 0.09
Interestingly, this decrease in activity occurs even though the amount of Akt phosphorylation (Ser473 and Thr308) is actually increased in the aged muscle.
Phosphorylation (phosphorylation) of Akt in muscle
15) Confidence 0.79 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2712760 Disease Relevance 0.22 Pain Relevance 0.08
This increase in PTEN protein appeared to parallel decreases in the amount of Akt-Thr308 phosphorylation which support the notion that a loss of PTEN protein with aging may contribute to the hyper-phosphorylation of Akt, and that acetaminophen intervention may function in reducing Akt phosphorylation by increasing PTEN levels.
Phosphorylation (phosphorylation) of Akt associated with paracetamol and aging
16) Confidence 0.79 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2712760 Disease Relevance 0.50 Pain Relevance 0.40
It has been reported that the phosphorylation of Thr308 of Akt, but not Ser473, is regulated by PTEN in adipocytes [13].
Phosphorylation (phosphorylation) of Akt in adipocytes associated with obesity
17) Confidence 0.79 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2712760 Disease Relevance 0.24 Pain Relevance 0.35
These results indicate that hyper-phosphorylation of Akt in aged muscle may be not directly related to the levels or phosphorylation of its putative upstream regulators.
Phosphorylation (-) of Akt in muscle
18) Confidence 0.79 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2712760 Disease Relevance 0.25 Pain Relevance 0.05
As expected, this decrease in S-nitrosylated Akt was found to parallel the normalization of Akt phosphorylation and increases in Akt kinase activity.
Phosphorylation (phosphorylation) of Akt
19) Confidence 0.79 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2712760 Disease Relevance 0.25 Pain Relevance 0.47
Using an ex vivo approach resulted in a similar conclusion as the aged control muscles required higher levels of Akt phosphorylation (both Ser474 and Thr308) to phosphorylate similar amounts of GSK3?
Phosphorylation (phosphorylation) of Akt in muscles
20) Confidence 0.79 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2712760 Disease Relevance 0.17 Pain Relevance 0.09

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