INT341215

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Context Info
Confidence 0.10
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 5
Disease Relevance 0.41
Pain Relevance 0.33

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

RNA binding (Eif4e, Eif4g3) translation (Eif4e, Eif4g3) cellular_component (Eif4g3)
protein complex (Eif4e) cytoplasm (Eif4e)
Eif4e (Mus musculus)
Eif4g3 (Mus musculus)
Pain Link Frequency Relevance Heat
cerebral cortex 50 68.84 Quite High
ischemia 180 65.04 Quite High
anesthesia 5 37.12 Quite Low
addiction 5 5.00 Very Low Very Low Very Low
alcohol 5 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Cv Unclassified Under Development 175 65.04 Quite High
Stress 140 50.00 Quite Low
Body Weight 5 29.64 Quite Low
Hypoxia 30 5.00 Very Low Very Low Very Low
Cancer 30 5.00 Very Low Very Low Very Low
Toxicity 5 5.00 Very Low Very Low Very Low
Repression 5 5.00 Very Low Very Low Very Low
Cv General 4 Under Development 5 5.00 Very Low Very Low Very Low
Brain Disease 5 5.00 Very Low Very Low Very Low
Alzheimer's Dementia 5 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Association of eIF4E with eIF4G and 4E-BP1
eIF4E Binding (Association) of eIF4G
1) Confidence 0.10 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2966049 Disease Relevance 0 Pain Relevance 0.06
To study eIF4F complex formation and 4E-BP1 and eIF4G association with eIF4E, a cap-containing matrix was used as described previously (16, 19).
eIF4E Binding (association) of eIF4G
2) Confidence 0.10 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2966049 Disease Relevance 0 Pain Relevance 0.06
We studied the phosphorylation status of 4E-BP1 associated with eIF4E and the binding of eIF4G to eIF4E as eIF4F complex formation. eIF4E is identified by its ability to bind to the 5?
eIF4E Binding (binding) of eIF4G
3) Confidence 0.10 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2966049 Disease Relevance 0.23 Pain Relevance 0.11
Active hypophosphorylated forms of 4E-BPs bind to eIF4E, compete with eIF4G, and inhibit eIF4G binding to eIF4E, which prevents eIF4F complex formation and inhibits cap-dependent translation (1–8).
eIF4E Binding (binding) of eIF4G
4) Confidence 0.10 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2966049 Disease Relevance 0 Pain Relevance 0
The assembly of the eIF4F complex is usually defined operationally as the association of eIF4G to eIF4E.
eIF4E Binding (association) of eIF4G
5) Confidence 0.10 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2966049 Disease Relevance 0.18 Pain Relevance 0.09

General Comments

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