INT272471

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Context Info
Confidence 0.39
First Reported 2008
Last Reported 2010
Negated 1
Speculated 2
Reported most in Body
Documents 5
Total Number 34
Disease Relevance 4.97
Pain Relevance 0.56

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
myotubes 2
myoblasts 1
poly 1
Celf1 (Mus musculus)
Pain Link Frequency Relevance Heat
cytokine 58 97.56 Very High Very High Very High
GABAergic 30 95.76 Very High Very High Very High
imagery 30 93.92 High High
gABA 27 90.96 High High
Inflammation 29 72.00 Quite High
Central nervous system 58 5.00 Very Low Very Low Very Low
spastic colon 29 5.00 Very Low Very Low Very Low
depression 29 5.00 Very Low Very Low Very Low
Kinase C 4 5.00 Very Low Very Low Very Low
anesthesia 3 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Targeted Disruption 627 99.64 Very High Very High Very High
Necrosis 29 98.36 Very High Very High Very High
Cancer 29 98.00 Very High Very High Very High
Stress 29 91.96 High High
Myotonic Dystrophy 654 90.04 High High
Disease 436 83.28 Quite High
Congenital Anomalies 319 83.12 Quite High
Toxicity 468 74.56 Quite High
INFLAMMATION 29 72.00 Quite High
Frailty 272 63.00 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
These data suggest that CUGBP1 interacts in vivo with CUG and CCUG RNAs located outside of aggregated CUG and CCUG repeats (Fig. 4, 5).
CUGBP1 Binding (interacts) of
1) Confidence 0.39 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.09 Pain Relevance 0
In agreement with these observations, the analysis of CUGBP1 in tissues from DM2 transgenic mice showed that CUGBP1 is associated with cytoplasmic CCUG RNA [52].
CUGBP1 Binding (associated) of associated with targeted disruption
2) Confidence 0.39 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.10 Pain Relevance 0
Further studies showed that RBD1+2 interact with CUG repeats; while RBD3 of CUGBP1 binds to GCN-rich regions in the 5’ UTRs of mRNA targets [ref. 71, and Timchenko L., unpublished].
CUGBP1 Binding (binds) of
3) Confidence 0.39 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.11 Pain Relevance 0
It has been shown that specificity of interaction of CUGBP1 with mRNAs is regulated by phosphorylation [75,76,78].
CUGBP1 Binding (interaction) of
4) Confidence 0.39 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.49 Pain Relevance 0
As has been discussed above, CUGBP1 does not bind to aggregated CUG and CCUG repeats.
CUGBP1 Neg (not) Binding (bind) of
5) Confidence 0.39 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.15 Pain Relevance 0
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].
CUGBP1 Binding (binds) of
6) Confidence 0.39 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.07 Pain Relevance 0
The formation of these complexes depends on CUG/CCUG RNAs because ectopic expression of pure CUG or CCUG RNAs causes interaction of CUGBP1 with un-aggregated CUG and CCUG repeats [39,52].
CUGBP1 Binding (interaction) of
7) Confidence 0.39 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.14 Pain Relevance 0
During DM1 myogenesis, phosphorylation of CUGBP1 and CUGBP1 interactions with its RNA targets are altered.
CUGBP1 Binding (interactions) of
8) Confidence 0.39 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.11 Pain Relevance 0
Thus, stabilization of CUGBP1 in DM1 is achieved by a complex mechanism involving specific phosphorylation of CUGBP1, its interactions with un-aggregated CUG repeats, and possibly some other factors.
CUGBP1 Binding (interactions) of
9) Confidence 0.39 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.06 Pain Relevance 0
If this is the case, then the RNA-binding activity of CUGBP1 toward its RNA targets might be different in DM1 and in DM2.


CUGBP1 Binding (binding) of
10) Confidence 0.39 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0 Pain Relevance 0.04
It seems that the best way to determine biologically relevant binding sites for these proteins is to identify mRNAs which are associated with CUGBP1 and MBNL1 in vivo, particularly in normal and in DM cells.
CUGBP1 Binding (associated) of
11) Confidence 0.39 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.18 Pain Relevance 0
CUGBP1 has been identified as the protein which binds to RNA oligonucleotide containing eight CUG repeats (CUG8) [27,28].
CUGBP1 Binding (binds) of
12) Confidence 0.39 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.11 Pain Relevance 0
During DM1 myogenesis, phosphorylation of CUGBP1 and CUGBP1 interactions with its RNA targets are altered.
CUGBP1 Binding (interactions) of
13) Confidence 0.39 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.11 Pain Relevance 0
It has been later shown that CUGBP1 also binds to U(A/G) repeat and to GRE elements [79,81,83].
CUGBP1 Binding (binds) of
14) Confidence 0.39 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.13 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].
CUGBP1 Binding (complex) of in myoblasts
15) Confidence 0.30 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.38 Pain Relevance 0
If this is the case, then the RNA-binding activity of CUGBP1 toward its RNA targets might be different in DM1 and in DM2.


CUGBP1 Spec (might) Binding (activity) of
16) Confidence 0.30 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0 Pain Relevance 0.04
CUGBP1 has a dual effect on translation of mRNAs which depends on the efficiency of the binding of CUGBP1 to its targets.
CUGBP1 Binding (binding) of
17) Confidence 0.30 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.50 Pain Relevance 0
As noted above, in normal myotubes, CUGBP1 interacts with cyclin D3/cdk4 complex which phosphorylates CUGBP1 at Ser302 [68].
CUGBP1 Binding (interacts) of in myotubes
18) Confidence 0.30 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.07 Pain Relevance 0
It has been shown that CUGBP1 binds to the 3’ UTR of TNF mRNA and destabilizes it through the direct interaction with poly A ribonuclease (PARN) removing the poly(A) tail [80].
CUGBP1 Binding (interaction) of in poly
19) Confidence 0.30 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.37 Pain Relevance 0.13
In contrast to DM1 myotubes, CUGBP1-eIF2 complexes are increased in DM2 differentiating myotubes similar to normal myotubes (Timchenko, L.; unpublished; Fig. 6).
CUGBP1 Binding (complexes) of in myotubes
20) Confidence 0.30 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.51 Pain Relevance 0

General Comments

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