INT276173

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Context Info
Confidence 0.56
First Reported 2009
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 7
Total Number 7
Disease Relevance 1.79
Pain Relevance 0.15

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

cytosol (Foxo1) nucleus (Foxo1) DNA binding (Foxo1)
cytoplasm (Foxo1)
Anatomy Link Frequency
muscle 2
skeletal muscle 1
Foxo1 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
Paracetamol 120 73.16 Quite High
anesthesia 5 32.16 Quite Low
antagonist 10 5.00 Very Low Very Low Very Low
cytokine 8 5.00 Very Low Very Low Very Low
ischemia 8 5.00 Very Low Very Low Very Low
nalbuphine 2 5.00 Very Low Very Low Very Low
Central nervous system 2 5.00 Very Low Very Low Very Low
Spinal cord 2 5.00 Very Low Very Low Very Low
analgesia 2 5.00 Very Low Very Low Very Low
addiction 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Tuberous Sclerosis 2 100.00 Very High Very High Very High
Aids-related Complex 44 96.60 Very High Very High Very High
Aging 83 95.88 Very High Very High Very High
Sepsis 6 88.80 High High
Heart Disease 2 72.48 Quite High
Frailty 10 71.36 Quite High
Coronary Artery Disease 4 70.72 Quite High
Apoptosis 28 66.72 Quite High
Myocardial Reperfusion Injury 1 65.92 Quite High
Decapitation 4 59.16 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Furthermore, while levels of p70 S6K and 4E-BP1 were not examined as part of the previous study, phosphorylation of other downstream targets of AKT kinase activity, namely Foxo1 and Foxo3, were shown to be similarly reduced.
Phosphorylation (phosphorylation) of Foxo1
1) Confidence 0.56 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2736646 Disease Relevance 0 Pain Relevance 0
Recent publication showed the phosphorylation of FoxO1 along with the activation of SirT1, SirT3 and SirT4 are localized in mitochondria where they regulate aging and energy metabolism.[4] Over the years,SIRT1 was known to be activated by resveratrol [33].
Phosphorylation (phosphorylation) of FoxO1 associated with aging
2) Confidence 0.56 Published 2010 Journal PLoS ONE Section Body Doc Link PMC3009730 Disease Relevance 0.30 Pain Relevance 0
Under our experimental conditions, leptin (intraperitoneally) did not change the acetylation state of either protein, suggesting that the fasting induced decrease in FoxO1 acetylation was leptin-independent.
Phosphorylation (acetylation) of FoxO1
3) Confidence 0.56 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2790615 Disease Relevance 0.24 Pain Relevance 0
Interestingly, these data do not appear to predict down-stream Akt signaling since the phosphorylation level of mTOR (Ser2448) [9] (Figure 2A), tuberous sclerosis complex-2 (TSC2) and forkhead box O1 (FoxO1) (data not shown) was lower in the very aged muscle.
Phosphorylation (phosphorylation) of forkhead box O1 in muscle associated with tuberous sclerosis
4) Confidence 0.55 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2712760 Disease Relevance 0.43 Pain Relevance 0.07
Interestingly, these data do not appear to predict down-stream Akt signaling since the phosphorylation level of mTOR (Ser2448) [9] (Figure 2A), tuberous sclerosis complex-2 (TSC2) and forkhead box O1 (FoxO1) (data not shown) was lower in the very aged muscle.
Phosphorylation (phosphorylation) of FoxO1 in muscle associated with tuberous sclerosis
5) Confidence 0.55 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2712760 Disease Relevance 0.43 Pain Relevance 0.07
500, Cell Signaling), acetylated FoxO1 (1?
Phosphorylation (acetylated) of FoxO1
6) Confidence 0.49 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2790615 Disease Relevance 0.22 Pain Relevance 0
We have recently shown the induction of lipopolysaccharide (LPS)-induced endotoxaemia in rodents to result in the reduction of total AKT protein levels, decreased cytosolic Foxo1 and Foxo3 phosphorylation, and increased levels of MAFbx/atrogin-1 protein and MuRF1 mRNA in fast-twitch skeletal muscle [3], where MAFbx/atrogin-1 and MuRF1 are considered important in the development of skeletal muscle proteolysis during catabolic events [4]–[6].
Phosphorylation (phosphorylation) of Foxo1 in skeletal muscle
7) Confidence 0.43 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2736646 Disease Relevance 0.17 Pain Relevance 0

General Comments

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