INT273867

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Context Info
Confidence 0.45
First Reported 2007
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 18
Total Number 18
Disease Relevance 3.14
Pain Relevance 0.25

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)
Anatomy Link Frequency
muscle 3
embryos 2
fibroblast 1
blood 1
neck 1
Jag1 (Mus musculus)
Pain Link Frequency Relevance Heat
Multiple sclerosis 123 96.88 Very High Very High Very High
cytokine 14 61.52 Quite High
Angina 1 13.32 Low Low
imagery 28 5.00 Very Low Very Low Very Low
Pain 16 5.00 Very Low Very Low Very Low
Spinal cord 14 5.00 Very Low Very Low Very Low
Sciatic nerve 14 5.00 Very Low Very Low Very Low
anesthesia 4 5.00 Very Low Very Low Very Low
Inflammation 3 5.00 Very Low Very Low Very Low
Demyelination 3 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Disease 28 99.90 Very High Very High Very High
Alagille Syndrome 1 99.40 Very High Very High Very High
Muscular Atrophy 126 97.64 Very High Very High Very High
Demyelinating Disease 126 96.88 Very High Very High Very High
Coronary Heart Disease 1 96.16 Very High Very High Very High
Frailty 56 95.16 Very High Very High Very High
Neurological Disease 3 93.92 High High
Leukemia 1 93.76 High High
Hypertrophy 14 91.64 High High
Diabetes Mellitus 24 89.48 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
We found that Ozz is associated with sarcomeric but not soluble MyHCemb from the earliest stages of muscle formation.
Ozz Binding (associated) of in muscle
1) Confidence 0.45 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0.12 Pain Relevance 0
To further validate these results, we checked whether all components of the Ozz-E3 complex were bound to assembled myosin in the insoluble preparations (P) from muscles of E16.5 embryos.
Ozz Binding (complex) of in embryos
2) Confidence 0.35 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0
From these findings, we can infer that the orderly removal of assembled MyHCemb is achieved by tagging it with the Ozz-E3 ubiquitin ligase (Fig. 8).
Ozz Binding (tagging) of
3) Confidence 0.35 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0
To further validate these results, we checked whether all components of the Ozz-E3 complex were bound to assembled myosin in the insoluble preparations (P) from muscles of E16.5 embryos.
Ozz Binding (bound) of in embryos
4) Confidence 0.35 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0
Similarly, two truncated fragments spanning amino acids 1872–1941, encompassing the ACD domain, also showed no interaction with Ozz.
Ozz Neg (no) Binding (interaction) of
5) Confidence 0.33 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
6) Confidence 0.33 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0.32 Pain Relevance 0
We found that Ozz interacted strongly with the full-length tail, but not with the head/neck domain.
Ozz Binding (interacted) of in head
7) Confidence 0.33 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0
We report here that the sarcomeric embryonic myosin heavy chain (MyHCemb/Myh3) is a novel substrate of Ozz, which specifically recognizes the rod domain or tail region of this protein.
Ozz Binding (recognizes) of in tail region
8) Confidence 0.33 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0.07 Pain Relevance 0.03
To ascertain whether the other components of the Ozz-E3 complex associated with the Ozzylated sarcomeric MyHCemb, extracted muscle proteins were immunoprecipitated with anti-Elo C from the S and P fractions and probed on immunoblots with both anti-MyHCemb and antibodies against the remaining E3 components.
Ozz Binding (associated) of in muscle
9) Confidence 0.33 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0
By further deleting the latter fragment at either its C-terminus (1738–1941 aa) or N-terminus (1536–1871 aa) we completely abolished Ozz binding.
Ozz Binding (binding) of
10) Confidence 0.33 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0
Six genes were chosen to confirm the temporal expression analysis: fibroblast growth factor 13 (Fgf13) mitogen-activated protein kinase 8 interacting protein 3 (Mapk8ip3), trafficking protein, kinesin binding 2 (Trak2), Jagged 1 (Jag1), serine/threonine kinase 3 (Stk3), and kruppel-like factor 9 (Klf9).


Jag1 Binding (binding) of in fibroblast
11) Confidence 0.31 Published 2007 Journal Molecular Vision Section Body Doc Link PMC2774458 Disease Relevance 0 Pain Relevance 0
In addition, we found that during muscle differentiation Ozz recognizes the developmental isoform MyHCemb as one of its substrates, marks it for ubiquitination, and is both necessary and sufficient for its ubiquitination in an in vitro assay.
Ozz Binding (recognizes) of in muscle
12) Confidence 0.29 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0.16 Pain Relevance 0
In a yeast 2-hybrid screen of an E14.5 mouse cDNA library we identified MyHCemb as a novel interaction partner of Ozz.
Ozz Binding (interaction) of
13) Confidence 0.29 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0.35 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 in myoblast
14) Confidence 0.29 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0
We found that Ozz interacted strongly with the full-length tail, but not with the head/neck domain.
Ozz Binding (interacted) of in neck
15) Confidence 0.11 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2844429 Disease Relevance 0 Pain Relevance 0
Protein jagged-1 is a ligand for multiple Notch receptors and involved in the mediation of Notch signaling, which influences neuronal function and development [20].
jagged-1 Binding (ligand) of in neuronal
16) Confidence 0.06 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2929207 Disease Relevance 0.60 Pain Relevance 0.22
Alagille syndrome, a developmental disease, is associated with mutations in Jagged1 and in less extent with mutations in Notch2.
Jagged1 Binding (associated) of associated with alagille syndrome and disease
17) Confidence 0.02 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2699037 Disease Relevance 1.04 Pain Relevance 0
The HTU provided four major functions: (1) videoconferencing over plain old telephone service (POTS) connections, allowing patients to interact with nurse case managers; (2) remote monitoring of glucose and blood pressure; (3) dial-up Internet service provider access and secure Web-based messaging with nurse case managers; and (4) access to an educational website created for the project by the American Diabetes Association.
HTU Binding (interact) of in blood associated with diabetes mellitus
18) Confidence 0.01 Published 2010 Journal Journal of Medical Internet Research Section Body Doc Link PMC2956232 Disease Relevance 0.48 Pain Relevance 0

General Comments

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