INT276616

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Context Info
Confidence 0.01
First Reported 2009
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 2
Disease Relevance 0.25
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.

protein modification process (UBE2S) cell cycle (UBE2S) cell division (UBE2S)
ligase activity (UBE2S)
UBE2S (Homo sapiens)
Pain Link Frequency Relevance Heat
Inflammation 2 5.00 Very Low Very Low Very Low
abdominal pain 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Gastroenteritis 10 95.04 Very High Very High Very High
Sprains And Strains 6 51.96 Quite High
Hepatitis E Virus Infection 14 50.00 Quite Low
Hepatitis 12 5.00 Very Low Very Low Very Low
Viral Infection 8 5.00 Very Low Very Low Very Low
Infection 8 5.00 Very Low Very Low Very Low
Hepatitis Virus Infection 4 5.00 Very Low Very Low Very Low
Liver Disease 4 5.00 Very Low Very Low Very Low
Jaundice 2 5.00 Very Low Very Low Very Low
Abdominal Pain 2 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
To verify that the dimerization of E2s is crucial for the host interaction of HEV, several mutations on dimer interface regions of E2/E2s were carried out (Figures 5 and 6), and their roles in destabilizing the dimer formation were studied.
E2s Binding (dimerization) of
1) Confidence 0.01 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2714988 Disease Relevance 0.25 Pain Relevance 0
The observed tight dimerization of E2s suggests a functionally important role of the dimer structure.
E2s Binding (dimerization) of
2) Confidence 0.01 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2714988 Disease Relevance 0 Pain Relevance 0

General Comments

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