INT303390

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Context Info
Confidence 0.07
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 4
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.

plasma membrane (Jag1) molecular_function (Myo1f)
Anatomy Link Frequency
tail 1
thick filaments 1
Jag1 (Mus musculus)
Myo1f (Mus musculus)
Pain Link Frequency Relevance Heat
imagery 8 5.00 Very Low Very Low Very Low
Spinal cord 4 5.00 Very Low Very Low Very Low
cytokine 4 5.00 Very Low Very Low Very Low
Pain 4 5.00 Very Low Very Low Very Low
Sciatic nerve 4 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Injury 4 37.24 Quite Low
Frailty 16 33.64 Quite Low
Muscular Atrophy 36 28.24 Quite Low
Pain 4 5.00 Very Low Very Low Very Low
Sprains And Strains 4 5.00 Very Low Very Low Very Low
Targeted Disruption 4 5.00 Very Low Very Low Very Low
Hypertrophy 4 5.00 Very Low Very Low Very Low
Nutritional Deficiencies 4 5.00 Very Low Very Low Very Low
Stress 4 5.00 Very Low Very Low Very Low
Appetite Loss 4 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Together these data show that Ozz is bound in a stable form to assembled sarcomeric myosin since the early stages of myofibrillogenesis, but at an untraceable level to soluble myosin.
Ozz Binding (bound) of myosin
1) Confidence 0.07 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0
Western blot analysis of these preparations demonstrated the co-purification of Ozz and its direct interacting partner Elo C with the thin-thick filaments, indicating an association of the entire Ozz-E3 complex with fully assembled myosin (Fig. 5A).
Ozz Binding (association) of myosin in thick filaments
2) Confidence 0.06 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0
In the same high molecular weight column fractions of sarcomeric preparations (P), a portion of Ozz consistently co-eluted with filamentous myosin, suggesting that Ozz is already bound to sarcomeric myosin during the early stages of myofibrillogenesis (E14.5, Fig. 3).
Ozz Binding (bound) of myosin
3) Confidence 0.06 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0
Two deletion fragments of the myosin tail encompassing either the N-terminal amino acids 1041–1535, or the C-terminal amino acids 1536 to 1941 interacted differently with the full length Ozz: the former bound weakly, while the latter maintained a strong interaction (Fig. 1E and Fig.
Ozz Binding (interacted) of myosin in tail
4) Confidence 0.05 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0

General Comments

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