INT122575

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Context Info
Confidence 0.37
First Reported 2004
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 4
Total Number 4
Disease Relevance 3.89
Pain Relevance 0.29

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

cytoplasm (Akt1, Nos3) signal transduction (Akt1, Nos3) nucleus (Akt1, Nos3)
plasma membrane (Akt1, Nos3) mitochondrion (Nos3) transport (Akt1)
Akt1 (Mus musculus)
Nos3 (Mus musculus)
Pain Link Frequency Relevance Heat
Clonidine 4 88.24 High High
cytokine 1 73.96 Quite High
agonist 23 73.44 Quite High
tolerance 3 72.32 Quite High
imagery 38 5.00 Very Low Very Low Very Low
Hippocampus 20 5.00 Very Low Very Low Very Low
isoflurane 6 5.00 Very Low Very Low Very Low
Eae 4 5.00 Very Low Very Low Very Low
Inflammation 3 5.00 Very Low Very Low Very Low
anesthesia 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Hypoxia 4 99.46 Very High Very High Very High
Stress 33 97.24 Very High Very High Very High
Attention Deficit Hyperactivity Disorder 1 95.24 Very High Very High Very High
Increased Venous Pressure Under Development 9 87.52 High High
Diabetes Mellitus 14 86.16 High High
Hypertension 4 82.80 Quite High
Heart Disease 4 82.24 Quite High
Stroke 2 81.64 Quite High
Death 4 80.72 Quite High
Disease 147 76.96 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The phosphatidylinositol 3-kinase (PI3-K) pathway, which activates serine/threonine protein kinase Akt, enhances endothelial nitric oxide synthase (eNOS) phosphorylation and nitric oxide (NO) production.
Akt Positive_regulation (enhances) of Phosphorylation (phosphorylation) of eNOS
1) Confidence 0.37 Published 2004 Journal Hypertension Section Abstract Doc Link 15505117 Disease Relevance 0.45 Pain Relevance 0.21
This effect is mediated primarily by Akt-dependent phosphorylation of eNOS at serine 1177 [30], [31].
Akt Positive_regulation (mediated) of Phosphorylation (phosphorylation) of eNOS
2) Confidence 0.17 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2866668 Disease Relevance 1.53 Pain Relevance 0
In support of this possibility, SOD-2 overexpression returns the eNOS phosphorylation status back to normal. eNOS phosphorylation at serine 1177 is mediated by Akt [31], which has been extensively shown to be modulated by oxidative stress.
Akt Positive_regulation (mediated) of Phosphorylation (phosphorylation) of eNOS associated with stress
3) Confidence 0.15 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2866668 Disease Relevance 0.49 Pain Relevance 0
In addition, hypoxia-activated AMPK stimulates Akt that phosphorylates and activates endothelial nitrogen oxide synthase (eNOS) (Serine 1177) (Figure 2) [53, 54].
Akt Positive_regulation (phosphorylates) of Phosphorylation (phosphorylates) of eNOS associated with hypoxia
4) Confidence 0.05 Published 2010 Journal PPAR Research Section Body Doc Link PMC2929615 Disease Relevance 1.41 Pain Relevance 0.07

General Comments

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