INT303372

From wiki-pain
Jump to: navigation, search
Context Info
Confidence 0.47
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

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

cytoplasm (Myh3)
Anatomy Link Frequency
sarcomeres 1
myoblast 1
thick filaments 1
Myh3 (Mus musculus)
Pain Link Frequency Relevance Heat
imagery 10 5.00 Very Low Very Low Very Low
Spinal cord 5 5.00 Very Low Very Low Very Low
cytokine 5 5.00 Very Low Very Low Very Low
Pain 5 5.00 Very Low Very Low Very Low
Sciatic nerve 5 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Nutritional Deficiencies 5 12.04 Low Low
Injury 5 8.60 Low Low
Muscular Atrophy 45 5.00 Very Low Very Low Very Low
Frailty 20 5.00 Very Low Very Low Very Low
Pain 5 5.00 Very Low Very Low Very Low
Sprains And Strains 5 5.00 Very Low Very Low Very Low
Targeted Disruption 5 5.00 Very Low Very Low Very Low
Hypertrophy 5 5.00 Very Low Very Low Very Low
Stress 5 5.00 Very Low Very Low Very Low
Appetite Loss 5 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).
MyHCemb Binding (binding) of
1) Confidence 0.47 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0
Examination of the P myosin preparations with immunofluorescence microscopy confirmed the presence of fragments of sarcomeres staining positively for MyHCemb and ?
MyHCemb Binding (staining) of in sarcomeres
2) Confidence 0.36 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0
We found that Ozz recognizes the rod portion of MyHCemb, which forms the core of sarcomeric thick filaments where it is not easily accessed for binding or exchange by soluble cytoplasmic molecules.
MyHCemb Binding (binding) of in thick filaments
3) Confidence 0.36 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0
To verify whether the Ozz-MyHCemb interaction occurred in vivo, crude lysates of proliferating (day 0), differentiating (day 2) and terminally differentiated (day 4) primary myoblast cultures prepared from newborn wild-type mice were immunoprecipitated with anti-MyHCemb antibody or an isotype matching control IgG, and probed on immunoblots with anti-Ozz antibody.
MyHCemb Binding (interaction) of in myoblast
4) Confidence 0.35 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0
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).
MyHCemb Binding (interacting) of
5) Confidence 0.35 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox