INT277278

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Context Info
Confidence 0.49
First Reported 2009
Last Reported 2010
Negated 4
Speculated 2
Reported most in Body
Documents 4
Total Number 16
Disease Relevance 4.63
Pain Relevance 0.48

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
muscle 2
skeletal muscle 2
heart 1
Celf1 (Mus musculus)
Pain Link Frequency Relevance Heat
GABAergic 40 98.22 Very High Very High Very High
Inflammation 12 98.00 Very High Very High Very High
cytokine 24 75.52 Quite High
medulla 4 42.12 Quite Low
imagery 40 5.00 Very Low Very Low Very Low
gABA 36 5.00 Very Low Very Low Very Low
Central nervous system 24 5.00 Very Low Very Low Very Low
spastic colon 12 5.00 Very Low Very Low Very Low
depression 12 5.00 Very Low Very Low Very Low
anesthesia 4 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Targeted Disruption 308 98.42 Very High Very High Very High
INFLAMMATION 12 98.00 Very High Very High Very High
Insulin Resistance 36 97.60 Very High Very High Very High
Frailty 168 96.68 Very High Very High Very High
Myotonic Dystrophy 264 96.00 Very High Very High Very High
Toxicity 192 93.76 High High
Muscle Disease 8 91.44 High High
Hypopituitarism 8 90.92 High High
Disease 200 88.44 High High
Congenital Anomalies 132 83.20 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Data discussed above suggest that CUG and CCUG repeats affect MBNL1 and CUGBP1 independently through aggregated and un-aggregated CUG and CCUG repeats.
Neg (independently) Regulation (affect) of CUGBP1
1) Confidence 0.49 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.27 Pain Relevance 0
In patients with DM1, CUGBP1 protein is increased without significant changes of CUGBP1 transcripts levels [39].
Neg (without) Regulation (changes) of CUGBP1
2) Confidence 0.49 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.29 Pain Relevance 0
Regulation of CUGBP1 RNA-Binding Activity by Phosphorylation
Regulation (Regulation) of CUGBP1
3) Confidence 0.49 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.52 Pain Relevance 0
Consistent with this suggestion, modulation of CUGBP1 levels in animal models dys-regulates normal muscle development and differentiation.
Regulation (modulation) of CUGBP1 in muscle
4) Confidence 0.49 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.41 Pain Relevance 0
It has been also shown that PKC phopshorylation regulates CUGBP1 [63].
Regulation (regulates) of CUGBP1
5) Confidence 0.43 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.22 Pain Relevance 0
To explore the molecular basis of the loss of GABAergic inhibition we investigated changes in expression levels and alternative splicing of the Cugbp1 CLIP target, Gabt4, in our mice.
Spec (investigated) Regulation (target) of Cugbp1 associated with gabaergic
6) Confidence 0.29 Published 2009 Journal PLoS Genetics Section Body Doc Link PMC2719092 Disease Relevance 0.08 Pain Relevance 0.09
In summary, these data show that biological functions of CUGBP1 are altered in DM1 patients not only by the elevation of the protein, but also by phosphorylation-specific changes in RNA-binding activity of CUGBP1.
Regulation (altered) of CUGBP1
7) Confidence 0.22 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.09 Pain Relevance 0
It has been shown that the site-specific phosphorylation of CUGBP1 by Akt and cyclinD3/cdk4 kinase regulates CUGBP1 function during normal myogenesis (Fig. 7).
Regulation (regulates) of CUGBP1
8) Confidence 0.22 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.14 Pain Relevance 0
Increase of TNF alpha in DM1 could be due to inflammation associated with dystrophic muscle; but it also could be due to increased levels of TNF through the dysregulation of CUGBP1.
Regulation (dysregulation) of CUGBP1 in muscle associated with inflammation
9) Confidence 0.22 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.48 Pain Relevance 0.12
Since CUGBP1 has been not found in the nuclear CUG and CCUG aggregates, nuclear CUG and CCUG foci do not appear to affect CUGBP1 levels.
Spec (appear) Regulation (affect) of CUGBP1
10) Confidence 0.22 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.12 Pain Relevance 0
Growing number of new reports suggest that additional pathways are involved in the regulation of activity and levels of CUGBP1 in DM1 and DM2 cells.
Regulation (regulation) of CUGBP1
11) Confidence 0.22 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.06 Pain Relevance 0
A comprehensive analysis of CUGBP1-RNPs from the CUGBP1 transgenic and MBNL1-RNPs from the wild type and MBNL1 knock out mice would be one of the approaches for identification of mRNAs which are targets of CUGBP1 and MBNL1 in vivo.
Regulation (targets) of CUGBP1 associated with targeted disruption
12) Confidence 0.22 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.20 Pain Relevance 0
In addition, the antagonistic relationship between CUGBP1 and MBNL1, previously documented in heart and skeletal muscle, has not been demonstrated in the CNS.
Neg (not) Regulation (demonstrated) of CUGBP1 in skeletal muscle
13) Confidence 0.21 Published 2009 Journal PLoS Genetics Section Body Doc Link PMC2719092 Disease Relevance 0.09 Pain Relevance 0.09
CUGBP1 is homologous to the Xenopus EDEN-BP protein which regulates RNA deadenylation through EDEN element during development [79,81].
Regulation (regulates) of EDEN element
14) Confidence 0.19 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.56 Pain Relevance 0.10
In addition, CUGexp or CCUGexp transcripts accumulate as ribonuclear inclusions in DM1 and DM2 patient skeletal muscle [9]–[11] and alter the localization or regulation of RNA binding proteins CUGBP1 [12],[13] and MBNL1 [14],[15].
Regulation (regulation) of CUGBP1 in skeletal muscle
15) Confidence 0.11 Published 2009 Journal PLoS Genetics Section Body Doc Link PMC2719092 Disease Relevance 1.00 Pain Relevance 0
In addition, the antagonistic relationship between CUGBP1 and MBNL1, previously documented in heart and skeletal muscle, has not been demonstrated in the CNS.
Neg (not) Regulation (demonstrated) of CUGBP1 in heart
16) Confidence 0.07 Published 2009 Journal PLoS Genetics Section Body Doc Link PMC2719092 Disease Relevance 0.09 Pain Relevance 0.09

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