INT272470

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Context Info
Confidence 0.10
First Reported 2008
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 2
Total Number 4
Disease Relevance 0.95
Pain Relevance 0

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

translation (Eif2s2)
Anatomy Link Frequency
myoblasts 2
myotubes 1
Eif2s2 (Mus musculus)
Pain Link Frequency Relevance Heat
cytokine 6 50.00 Quite Low
Central nervous system 6 5.00 Very Low Very Low Very Low
spastic colon 3 5.00 Very Low Very Low Very Low
depression 3 5.00 Very Low Very Low Very Low
Inflammation 3 5.00 Very Low Very Low Very Low
Kinase C 2 5.00 Very Low Very Low Very Low
tolerance 1 5.00 Very Low Very Low Very Low
abdominal pain 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Stress 3 91.68 High High
Myotonic Dystrophy 74 88.32 High High
Targeted Disruption 65 82.52 Quite High
Disease 52 60.00 Quite High
Congenital Anomalies 33 50.36 Quite High
Cancer 3 23.04 Low Low
Necrosis 3 22.56 Low Low
Toxicity 50 5.00 Very Low Very Low Very Low
Myotonia 42 5.00 Very Low Very Low Very Low
Cataract 25 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
CUGBP1 binds to CUG repeats within the DM1 protein extracts mainly as a single protein; however, in DM2 extracts, CUGBP1 binds to CCUG repeats as a component of the high molecular weight CUGBP1-eIF2 complex [52].
eIF2 Binding (complex) of
1) Confidence 0.10 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.06 Pain Relevance 0
In contrast to DM1 myotubes, CUGBP1-eIF2 complexes are increased in DM2 differentiating myotubes similar to normal myotubes (Timchenko, L.; unpublished; Fig. 6).
eIF2 Binding (complexes) of in myotubes
2) Confidence 0.10 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.51 Pain Relevance 0
Ectopic expression of cyclin D3 promoted the formation of the CUGBP1-eIF2 complex in DM1 myotubes and improved fusion of DM1 myoblasts [78].
eIF2 Binding (complex) of in myoblasts
3) Confidence 0.09 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.38 Pain Relevance 0
[93] and Mef2A [70] in differentiating cells by interacting with translation initiation factor eIF2, the mechanism by which translation was inefficient in DM1 muscle cells was not fully understood, in particular after confirming that the levels of CUG-BP1 mRNA did not show any significant change in DM1 muscle cells when compared to normal myoblasts [94].
eIF2 Binding (interacting) of in myoblasts
4) Confidence 0.07 Published 2008 Journal Current Genomics Section Body Doc Link PMC2694559 Disease Relevance 0 Pain Relevance 0

General Comments

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