INT171382

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Context Info
Confidence 0.51
First Reported 2002
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 6
Total Number 6
Disease Relevance 3.41
Pain Relevance 0.94

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

cytosol (Insr) endosome (Insr) plasma membrane (Insr)
nucleus (Insr) kinase activity (Insr)
Anatomy Link Frequency
macrophages 1
stems 1
Insr (Mus musculus)
Pain Link Frequency Relevance Heat
chemokine 12 99.60 Very High Very High Very High
cytokine 48 99.00 Very High Very High Very High
metalloproteinase 64 98.64 Very High Very High Very High
Inflammation 104 94.48 High High
Opioid 23 94.08 High High
antagonist 14 85.20 High High
Hippocampus 20 72.16 Quite High
cerebral cortex 6 71.36 Quite High
Central nervous system 30 53.40 Quite High
Pyramidal cell 4 43.76 Quite Low
Disease Link Frequency Relevance Heat
Apoptosis 42 100.00 Very High Very High Very High
Obesity 257 99.88 Very High Very High Very High
Insulin Resistance 83 97.34 Very High Very High Very High
Diabetes Mellitus 113 96.80 Very High Very High Very High
Disease 202 95.44 Very High Very High Very High
INFLAMMATION 116 94.48 High High
Hyperinsulinism 17 87.32 High High
Glioma 13 84.00 Quite High
Cognitive Disorder 16 82.36 Quite High
Dementia 30 50.00 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
However, it has been demonstrated that insulin resistance associated with obesity largely stems from posttranslational modifications of insulin signaling proteins, such as inhibitory serine phosphorylation of the insulin receptor or its downstream signaling mediators [33].
Phosphorylation (phosphorylation) of insulin receptor in stems associated with obesity and insulin resistance
1) Confidence 0.51 Published 2010 Journal PLoS Genetics Section Body Doc Link PMC2865520 Disease Relevance 1.24 Pain Relevance 0.22
Insulin receptor–deficient macrophages exhibit increased susceptibility to lipid-induced apoptosis and reduced expression of matrix metalloproteinase 9
Phosphorylation (apoptosis) of Insulin receptor in macrophages associated with metalloproteinase and apoptosis
2) Confidence 0.50 Published 2010 Journal PLoS Genetics Section Body Doc Link PMC2865520 Disease Relevance 1.24 Pain Relevance 0.23
M, neither DSLET, DADLE, nor DPDPE were found to increase the tyrosine phosphorylation of the IR or the PDGFR, whereas insulin (100 ng/ml) or PDGF (50 ng/ml) induced significant tyrosine phosphorylation of these sites (Figure 8).
Phosphorylation (phosphorylation) of IR
3) Confidence 0.11 Published 2002 Journal BMC Pharmacol Section Body Doc Link PMC88976 Disease Relevance 0.14 Pain Relevance 0.40
The increase in mTORC1 activity and PKB phosphorylation in the absence of IRS1/2 associated p85 is consistent with other models of contraction in which PKB is activated independent of any increase in tyrosine phosphorylation of the insulin receptor or IRS1 [49], [50].
Phosphorylation (phosphorylation) of insulin receptor
4) Confidence 0.08 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2905373 Disease Relevance 0 Pain Relevance 0
Insulin and IGF1 receptors are tyrosine kinases that mediate the phosphorylation of insulin receptor substrates (IRSs) including IRS1-4.
Phosphorylation (phosphorylation) of insulin receptor
5) Confidence 0.07 Published 2010 Journal The Open Biochemistry Journal Section Body Doc Link PMC2864432 Disease Relevance 0.43 Pain Relevance 0
The receptor for IGF1 is structurally similar to the insulin receptor; both are tyrosine kinases that phosphorylate similar insulin receptor substrate proteins [72].
Phosphorylation (phosphorylate) of insulin receptor
6) Confidence 0.05 Published 2010 Journal The Open Biochemistry Journal Section Body Doc Link PMC2864432 Disease Relevance 0.37 Pain Relevance 0.10

General Comments

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