INT287580

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Context Info
Confidence 0.00
First Reported 2009
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 4
Disease Relevance 0.29
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.

RNA binding (Mex3c) nucleus (Mex3c) biological_process (Mex3c)
cytoplasm (Mex3c)
Mex3c (Mus musculus)
Pain Link Frequency Relevance Heat
agonist 28 5.00 Very Low Very Low Very Low
Glutamate receptor 8 5.00 Very Low Very Low Very Low
Hippocampus 8 5.00 Very Low Very Low Very Low
depression 4 5.00 Very Low Very Low Very Low
Pain 4 5.00 Very Low Very Low Very Low
nMDA receptor antagonist 4 5.00 Very Low Very Low Very Low
alcohol 4 5.00 Very Low Very Low Very Low
Immobilon 4 5.00 Very Low Very Low Very Low
isoflurane 4 5.00 Very Low Very Low Very Low
imagery 4 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Fragile X Syndrome 84 78.88 Quite High
Targeted Disruption 36 77.08 Quite High
Disease 36 38.72 Quite Low
Liver Disease 20 10.88 Low Low
Glycogen Storage Disease 8 8.48 Low Low
Intellectual Impairment 36 5.00 Very Low Very Low Very Low
Li-fraumeni Syndrome 20 5.00 Very Low Very Low Very Low
Anxiety Disorder 20 5.00 Very Low Very Low Very Low
Autism 16 5.00 Very Low Very Low Very Low
Convulsion 16 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The conclusion that I304N FMRP KH2 domain fails to bind RNA in vivo is consistent with structural studies of several RNA-binding proteins suggesting that this mutation should affect RNA binding.
KH2 Binding (bind) of
1) Confidence 0.00 Published 2009 Journal PLoS Genetics Section Body Doc Link PMC2779495 Disease Relevance 0 Pain Relevance 0
RGG-domain RNA binding to RNA over 200nt is not evident in the I304N mouse, suggesting either that it plays a minor or dependent role to KH2 binding to large RNAs.
KH2 Binding (binding) of
2) Confidence 0.00 Published 2009 Journal PLoS Genetics Section Body Doc Link PMC2779495 Disease Relevance 0.14 Pain Relevance 0
This finding suggests that loss of FMRP activity, including but not necessarily limited to KH2 RNA binding, may play a critical role in leading to the synaptic defects evident in the mouse, and, presumably, in human patients.
KH2 Binding (binding) of
3) Confidence 0.00 Published 2009 Journal PLoS Genetics Section Body Doc Link PMC2779495 Disease Relevance 0 Pain Relevance 0
While other interpretations cannot be ruled out, including the loss of KH2-dependent interaction with a protein partner, taken together our data suggest that the resulting loss of polysome association and, presumably, proper regulation of translation of FMRP mRNA targets, is most likely to contribute to the phenotype of the Fmr1I304N mouse.


KH2 Binding (interaction) of
4) Confidence 0.00 Published 2009 Journal PLoS Genetics Section Body Doc Link PMC2779495 Disease Relevance 0.15 Pain Relevance 0

General Comments

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