INT312635

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Context Info
Confidence 0.47
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 12
Disease Relevance 3.41
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 (Musk, Dok7) lipid binding (Dok7) signal transduction (Musk)
kinase activity (Musk)
Anatomy Link Frequency
Tid1 1
myotubes 1
Musk (Mus musculus)
Dok7 (Mus musculus)
Musk - V790M (1)
Pain Link Frequency Relevance Heat
Action potential 12 38.24 Quite Low
anesthesia 12 5.00 Very Low Very Low Very Low
imagery 12 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Congenital Myasthenic Syndromes 264 99.28 Very High Very High Very High
Respiratory Failure 24 82.48 Quite High
Congenital Anomalies 24 79.28 Quite High
Cyanosis 12 57.68 Quite High
Patent Ductus Arteriosus 12 55.60 Quite High
Syndrome 36 20.88 Low Low
Lower Respiratory Tract Infection 12 20.08 Low Low
Disease 12 18.00 Low Low
Scoliosis 12 13.20 Low Low
Muscle Weakness 24 12.00 Low Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
In the case of the two previously described MUSK mutations, 220insC results in complete lack of expression of the protein and V790M impairs binding of MuSK to Dok-7 (11), but does not appear to alter MuSK autophosphorylation (5).
MuSK Binding (binding) of Dok-7
1) Confidence 0.47 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.25 Pain Relevance 0
More recently, it was reported that the MuSK V790M mutation also failed to co-immunoprecipitate with Dok-7 in co-transfected 293T cells (11).
MuSK (V790M) Binding (immunoprecipitate) of Dok-7
2) Confidence 0.35 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.32 Pain Relevance 0
Our findings confirm previous observations and further indicate that disruption of the interaction of MuSK with Dok-7 plays a fundamental role in the pathogenesis of MUSK-associated CMS.


MuSK Binding (interaction) of Dok-7 associated with congenital myasthenic syndromes
3) Confidence 0.35 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.50 Pain Relevance 0
Expression studies in MuSK deficient myotubes revealed that A727V, which is located within the catalytic loop of the enzyme, caused severe impairment of agrin-dependent MuSK phosphorylation, aggregation of acetylcholine receptors (AChRs) and interaction of MuSK with Dok-7, an essential intracellular binding protein of MuSK.
MuSK Binding (interaction) of Dok-7 in myotubes
4) Confidence 0.35 Published 2010 Journal Human Molecular Genetics Section Abstract Doc Link PMC2876883 Disease Relevance 0.26 Pain Relevance 0
Our findings demonstrate that missense mutations in MUSK can result in a severe form of CMS and indicate that the inability of MuSK mutants to interact with Dok-7, but not with Lrp4 or Tid1, is a major determinant of the pathogenesis of the CMS caused by MUSK mutations.



MuSK Binding (interact) of Dok-7 in Tid1 associated with congenital myasthenic syndromes
5) Confidence 0.35 Published 2010 Journal Human Molecular Genetics Section Abstract Doc Link PMC2876883 Disease Relevance 0.27 Pain Relevance 0
In contrast, M605I, resulted in only moderate impairment of agrin-dependent MuSK phosphorylation, aggregation of AChRs and interaction of MuSK with Dok-7.
MuSK Binding (interaction) of Dok-7
6) Confidence 0.35 Published 2010 Journal Human Molecular Genetics Section Abstract Doc Link PMC2876883 Disease Relevance 0.26 Pain Relevance 0
Finally, A727V, by virtue of being located in the catalytic loop of the enzyme, results in drastic impairment of phosphorylation and MuSK–Dok-7 interaction.
MuSK Binding (interaction) of Dok-7
7) Confidence 0.30 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.31 Pain Relevance 0
Our expression studies have identified impairment of MuSK phosphorylation and MuSK–Dok-7 interaction as central to the pathogenesis of the CMS described here.
MuSK Binding (interaction) of Dok-7 associated with congenital myasthenic syndromes
8) Confidence 0.30 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.23 Pain Relevance 0
Finally, A727V, by virtue of being located in the catalytic loop of the enzyme, results in drastic impairment of phosphorylation and MuSK–Dok-7 interaction.
MuSK Binding (interaction) of Dok-7
9) Confidence 0.30 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.31 Pain Relevance 0
MuSK phorphorylation and MuSK–Dok-7 interaction are fundamental steps of synaptic development since tyrosine autophosphorylation radically increases the catalytic activity of MuSK (21) and the recruitment of proteins containing the PTB binding domain, such as Dok-7, is essential for the downstream propagation of signaling events (33).
MuSK Binding (interaction) of Dok-7
10) Confidence 0.30 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.22 Pain Relevance 0
MuSK phorphorylation and MuSK–Dok-7 interaction are fundamental steps of synaptic development since tyrosine autophosphorylation radically increases the catalytic activity of MuSK (21) and the recruitment of proteins containing the PTB binding domain, such as Dok-7, is essential for the downstream propagation of signaling events (33).
MuSK Binding (interaction) of Dok-7
11) Confidence 0.30 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.22 Pain Relevance 0
Our expression studies have identified impairment of MuSK phosphorylation and MuSK–Dok-7 interaction as central to the pathogenesis of the CMS described here.
MuSK Binding (interaction) of Dok-7 associated with congenital myasthenic syndromes
12) Confidence 0.30 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.23 Pain Relevance 0

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