INT272467

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Context Info
Confidence 0.56
First Reported 2008
Last Reported 2010
Negated 0
Speculated 1
Reported most in Body
Documents 3
Total Number 5
Disease Relevance 1.61
Pain Relevance 0.05

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

mRNA binding (Celf1) mRNA processing (Celf1) RNA binding (Celf1)
nucleus (Celf1) cytoplasm (Celf1)
Anatomy Link Frequency
myoblasts 2
nucleus 2
Celf1 (Mus musculus)
Pain Link Frequency Relevance Heat
Kinase C 4 98.24 Very High Very High Very High
cytokine 6 5.00 Very Low Very Low Very 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
tolerance 2 5.00 Very Low Very Low Very Low
abdominal pain 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Myotonic Dystrophy 82 99.48 Very High Very High Very High
Targeted Disruption 73 97.12 Very High Very High Very High
Disease 65 96.16 Very High Very High Very High
Stress 3 84.12 Quite High
Cataract 29 75.16 Quite High
Arrhythmias 2 Under Development 8 74.72 Quite High
Hypopituitarism 22 73.60 Quite High
Frailty 27 73.20 Quite High
Congenital Anomalies 33 8.56 Low Low
Toxicity 52 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
CUGBP1 phosphorylated isoforms are increased in cytoplasm of DM2 myoblasts with elevated levels of CUGBP1; thus phosphorylation may also play a role in the stabilization of CUGBP1 in DM2 cells [52].
Positive_regulation (increased) of Phosphorylation (phosphorylated) of CUGBP1 in myoblasts
1) Confidence 0.56 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0 Pain Relevance 0
These data suggest that a lack of CDM in patients with DM2 may be, at least in part, due to normal phosphorylation of CUGBP1 at Ser302.


Positive_regulation (be) of Phosphorylation (phosphorylation) of CUGBP1 associated with myotonic dystrophy
2) Confidence 0.40 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.54 Pain Relevance 0
In addition, the phosphorylation of CUGBP1 on the putative PKC sites might stabilize CUGBP1 in DM1 cells leading to the enhancement of CUGBP1 functions.
Spec (might) Positive_regulation (stabilize) of Phosphorylation (phosphorylation) of CUGBP1
3) Confidence 0.40 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.10 Pain Relevance 0
Although the molecular mechanism leading to CUG-BP1 activation is not completely understood, inappropriate activation of the protein kinase C (PKC) pathway contributes to the pathogenic effect of noncoding CUG repeat RNA through hyperphosphorylation of nuclear CUG-BP1, which is stabilized in this cellular compartment [69].
Positive_regulation (stabilized) of Phosphorylation (hyperphosphorylation) of CUG-BP1 associated with kinase c
4) Confidence 0.21 Published 2008 Journal Current Genomics Section Body Doc Link PMC2694559 Disease Relevance 0.45 Pain Relevance 0.05
DM1 cells activate CELF family member CUG-BP1 protein through hyperphosphorylation and stabilization in the cell nucleus.
Positive_regulation (activate) of Phosphorylation (hyperphosphorylation) of CUG-BP1 in nucleus
5) Confidence 0.21 Published 2008 Journal Current Genomics Section Abstract Doc Link PMC2694559 Disease Relevance 0.52 Pain Relevance 0

General Comments

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