INT303180

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Context Info
Confidence 0.40
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 5
Disease Relevance 0
Pain Relevance 0.09

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

intracellular (Trim3, Shank1) cytoplasm (Trim3, Shank1) cell differentiation (Shank1)
plasma membrane (Shank1) protein complex assembly (Shank1)
Anatomy Link Frequency
finger 2
neurons 1
Trim3 (Rattus norvegicus)
Shank1 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
tetrodotoxin 20 85.16 High High
Glutamate receptor 10 5.00 Very Low Very Low Very Low
imagery 5 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Syndrome 10 5.00 Very Low Very Low Very Low
Anxiety Disorder 5 5.00 Very Low Very Low Very Low
Attention Deficit Hyperactivity Disorder 5 5.00 Very Low Very Low Very Low
Intellectual Impairment 5 5.00 Very Low Very Low Very Low
Cognitive Disorder 5 5.00 Very Low Very Low Very Low
Disease 5 5.00 Very Low Very Low Very Low
Autism 5 5.00 Very Low Very Low Very Low
Angelman Syndrome 5 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
From this experiment, we conclude that the RING finger domain and the C-terminal half of TRIM3 containing the NHL repeats are both required for TRIM3 to suppress GKAP protein levels.
TRIM3 Negative_regulation (suppress) of GKAP protein in finger
1) Confidence 0.40 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844417 Disease Relevance 0 Pain Relevance 0
Although TRIM3 suppressed protein levels of Shank1 in heterologous cells, this effect was surprisingly not dependent on the presence of the RING finger domain and was not completely blocked by proteasome inhibitors, in contrast to suppression of GKAP by TRIM3.
TRIM3 Negative_regulation (suppressed) of Shank1 in finger
2) Confidence 0.40 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844417 Disease Relevance 0 Pain Relevance 0
At least in heterologous cells, therefore, the inhibition of Shank1A protein levels by TRIM3 appears to be unrelated to the E3 ligase activity of TRIM3.
TRIM3 Negative_regulation (inhibition) of Shank1A protein
3) Confidence 0.40 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844417 Disease Relevance 0 Pain Relevance 0
Mutation of the first two conserved cysteine residues (C22S/C25S) abolished the ability of TRIM3 to suppress GKAP protein levels (Figure 3E).
TRIM3 Negative_regulation (suppress) of GKAP protein
4) Confidence 0.40 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844417 Disease Relevance 0 Pain Relevance 0
The TRIM3 RNAi phenotype implies that TRIM3 normally functions to suppress the postsynaptic levels of Shank1 protein in neurons.
TRIM3 Negative_regulation (suppress) of Shank1 protein in neurons
5) Confidence 0.40 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844417 Disease Relevance 0 Pain Relevance 0.09

General Comments

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