INT303386

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Context Info
Confidence 0.02
First Reported 2010
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 1
Total Number 3
Disease Relevance 0
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.

transport (Laptm5) plasma membrane (Jag1) lysosome (Laptm5)
Anatomy Link Frequency
myofibrils 1
Jag1 (Mus musculus)
Laptm5 (Mus musculus)
Pain Link Frequency Relevance Heat
imagery 6 5.00 Very Low Very Low Very Low
Spinal cord 3 5.00 Very Low Very Low Very Low
cytokine 3 5.00 Very Low Very Low Very Low
Pain 3 5.00 Very Low Very Low Very Low
Sciatic nerve 3 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Muscular Atrophy 27 5.00 Very Low Very Low Very Low
Frailty 12 5.00 Very Low Very Low Very Low
Pain 3 5.00 Very Low Very Low Very Low
Sprains And Strains 3 5.00 Very Low Very Low Very Low
Targeted Disruption 3 5.00 Very Low Very Low Very Low
Hypertrophy 3 5.00 Very Low Very Low Very Low
Injury 3 5.00 Very Low Very Low Very Low
Nutritional Deficiencies 3 5.00 Very Low Very Low Very Low
Stress 3 5.00 Very Low Very Low Very Low
Appetite Loss 3 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
However, under these stringent experimental conditions (high salt concentration), while we were able to demonstrate Ozz binding with its direct interacting partners, MyHCemb and Elo C, we could not co-immunoprecipitate the remaining components of the Ozz-E3 complex (not shown).
Ozz Neg (not) Binding (complex) of E3
1) Confidence 0.02 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0
Fractions from both S and P preparations were also probed on immunoblots with antibodies against each component of the Ozz-E3 complex (Elo B/C, Cul5, and Rbx1).
Ozz Binding (component) of E3
2) Confidence 0.02 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0
Nonetheless, the presence in the sarcomeric, insoluble fractions of all Ozz partners and the demonstrated interaction of Ozz, Elo C and MyHCemb strongly support the notion that the Ozz-E3 complex is assembled within the myofibrils.
Ozz Binding (interaction) of E3 in myofibrils
3) Confidence 0.02 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0

General Comments

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