INT333601

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Context Info
Confidence 0.73
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 6
Total Number 6
Disease Relevance 2.09
Pain Relevance 0.19

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

cytosol (IRF3) nucleoplasm (IRF3) plasma membrane (IRF3)
nucleus (IRF3) DNA binding (IRF3) cytoplasm (IRF3)
Anatomy Link Frequency
nucleus 1
IRF3 (Homo sapiens)
Pain Link Frequency Relevance Heat
addiction 5 76.88 Quite High
agonist 6 73.20 Quite High
cytokine 25 51.92 Quite High
chemokine 7 51.12 Quite High
fibrosis 7 51.00 Quite High
Inflammation 15 50.00 Quite Low
adenocard 1 32.08 Quite Low
Inflammatory response 1 23.56 Low Low
anesthesia 10 5.00 Very Low Very Low Very Low
imagery 5 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Sprains And Strains 85 97.08 Very High Very High Very High
Targeted Disruption 20 96.48 Very High Very High Very High
Hepatitis C Virus Infection 72 95.36 Very High Very High Very High
Viral Infection 10 82.92 Quite High
Infection 155 77.48 Quite High
Carcinoma 5 67.92 Quite High
Disorder Of Lipid Metabolism 2 58.48 Quite High
Bacteriuria 20 57.60 Quite High
Hepatocellular Cancer 76 52.76 Quite High
Cirrhosis 28 51.00 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
IRF3 phosphorylation in response to ceramide was controlled by TLR4 and TRAM, as shown using specific siRNA knock down.
Phosphorylation (phosphorylation) of IRF3 associated with targeted disruption
1) Confidence 0.73 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2944801 Disease Relevance 0.59 Pain Relevance 0
IRF3 is an interferon regulatory transcription factor and following TLR4 activation, phosphorylated IRF3 homodimers translocate from the cytosol to the nucleus [43], [44], [45], [46].
Phosphorylation (phosphorylated) of IRF3 in nucleus
2) Confidence 0.73 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2944801 Disease Relevance 0.07 Pain Relevance 0
The involvement of TBK1 is not clear, but preliminary experiments did not provide evidence that TBK1 controlled IRF3 phosphorylation in this pathway.
Phosphorylation (phosphorylation) of IRF3
3) Confidence 0.73 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2944801 Disease Relevance 0.35 Pain Relevance 0.04
E. coli S1918pap induced higher nuclear IRF3 translocation and IRF3 phosphorylation than E. coli S1918, consistent with results in ceramide-stimulated cells (Figure 5A and Figure S10, p<0.01 for a broader view).
Phosphorylation (phosphorylation) of IRF3
4) Confidence 0.56 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2944801 Disease Relevance 0.23 Pain Relevance 0.04
E. coli S1918pap induced higher nuclear IRF3 translocation and IRF3 phosphorylation than E. coli S1918, consistent with results in ceramide-stimulated cells (Figure 5A and Figure S10, p<0.01 for a broader view).
Phosphorylation (phosphorylation) of IRF3
5) Confidence 0.56 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2944801 Disease Relevance 0.24 Pain Relevance 0.04
These two kinases in turn phosphorylate the interferon regulator factor-3 (IRF-3) that activates the IFN-?
Phosphorylation (phosphorylate) of IRF-3
6) Confidence 0.11 Published 2010 Journal J Transl Med Section Body Doc Link PMC2991329 Disease Relevance 0.62 Pain Relevance 0.08

General Comments

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