INT303399

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Context Info
Confidence 0.50
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 11
Disease Relevance 0.85
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.

plasma membrane (Jag1) cytoplasm (Myh3)
Anatomy Link Frequency
myoblast 3
thick filaments 2
muscle 1
tail region 1
head 1
Jag1 (Mus musculus)
Myh3 (Mus musculus)
Pain Link Frequency Relevance Heat
Spinal cord 11 47.96 Quite Low
cytokine 11 19.28 Low Low
Sciatic nerve 11 19.12 Low Low
Pain 11 15.60 Low Low
imagery 22 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Frailty 44 95.16 Very High Very High Very High
Hypertrophy 11 91.64 High High
Muscular Atrophy 99 90.20 High High
Injury 11 66.04 Quite High
Nutritional Deficiencies 11 54.64 Quite High
Pain 11 15.60 Low Low
Sprains And Strains 11 5.00 Very Low Very Low Very Low
Targeted Disruption 11 5.00 Very Low Very Low Very Low
Stress 11 5.00 Very Low Very Low Very Low
Appetite Loss 11 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The fact that Ozz and its direct partner Elo C could be co-immunoprecipitated from sarcomeric but not soluble myosin extracts of E16.5 embryonic muscle indicates that at this age a proportion of Ozz molecules bound to MyHCemb is assembled into the E3 ligase complex.
Ozz Binding (bound) of MyHCemb in muscle
1) Confidence 0.50 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0.05 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.
Ozz Binding (recognizes) of MyHCemb in thick filaments
2) Confidence 0.50 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0
Direct interaction of Ozz with myofilamentous MyHCemb was proven by co-immunoprecipitation of Ozz with anti-MyHCemb antibody only from the insoluble preparations (P), but not from the soluble preparations (S), albeit the amount of Ozz was greater in the latter (Fig. 5B, panels 2 and 6).
Ozz Binding (interaction) of MyHCemb
3) Confidence 0.44 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0
Ozz-MyHCemb complexes were detected in crude lysates of myoblast by immunoprecipitation with anti-MyHCemb antibody, followed by Western blotting of the immunoprecipitates with the anti-Ozz antibody.
Ozz Binding (complexes) of MyHCemb in myoblast
4) Confidence 0.39 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0
Here we present evidence that the Ozz-E3 ligase, by binding to the rod domain of a fully assembled MyHCemb, marks it for ubiquitination and degradation, probably facilitating the subsequent assembly of new isoforms.
Ozz Binding (binding) of MyHCemb
5) Confidence 0.37 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0.38 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.
Ozz Binding (recognizes) of MyHCemb in thick filaments
6) Confidence 0.37 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).
Ozz Binding (binding) of MyHCemb
7) Confidence 0.34 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0
Ozz binding to MyHCemb differs from that of other E3 ligases in that it targets the tail portion of assembled sarcomeric myosin rather than the head portion of soluble myosin, and we suggest that these properties are fundamental to its role in muscle development as opposed to muscle atrophy.
Ozz Binding (binding) of MyHCemb in head associated with muscular atrophy
8) Confidence 0.33 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0.23 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.
Ozz Binding (interaction) of MyHCemb in myoblast
9) Confidence 0.33 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0
To confirm Ozz' interaction with the tail of MyHCemb and to identify the minimal regions of the tail needed for this interaction, we performed a series of 2-hybrid experiments using as preys either the full length tail domain (residues 1040–1941), the full length head/neck domain (residues 1–1040), or several deletion mutants of the tail region (Fig. 1E and Fig.
Ozz Binding (interaction) of MyHCemb in tail region
10) Confidence 0.33 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0.19 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.
Ozz Binding (interaction) of MyHCemb in myoblast
11) Confidence 0.33 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0

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