INT312605

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Context Info
Confidence 0.80
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 13
Disease Relevance 3.12
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.

signal transduction (Musk) plasma membrane (Musk) kinase activity (Musk)
Anatomy Link Frequency
myotubes 1
Musk (Mus musculus)
Pain Link Frequency Relevance Heat
Action potential 13 21.44 Low Low
anesthesia 13 7.68 Low Low
imagery 13 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Congenital Myasthenic Syndromes 286 99.32 Very High Very High Very High
Congenital Anomalies 26 92.40 High High
Respiratory Failure 26 72.36 Quite High
Cyanosis 13 40.88 Quite Low
Patent Ductus Arteriosus 13 38.80 Quite Low
Syndrome 39 10.76 Low Low
Disease 13 7.88 Low Low
Myasthenia Gravis 39 5.00 Very Low Very Low Very Low
Muscle Weakness 26 5.00 Very Low Very Low Very Low
Frailty 13 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Our expression studies have identified impairment of MuSK phosphorylation and MuSK–Dok-7 interaction as central to the pathogenesis of the CMS described here.
Phosphorylation (phosphorylation) of MuSK associated with congenital myasthenic syndromes
1) Confidence 0.80 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.23 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).
Phosphorylation (phorphorylation) of MuSK
2) Confidence 0.80 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.23 Pain Relevance 0
Together, these findings suggest that impaired MuSK phosphorylation, which is a feature common to CMS due to MUSK and DOK7 mutations, is a key factor responsible for the abnormal endplate formation and presynaptic differentiation seen in CMS resulting from abnormalities of the agrin-MuSK signal transduction pathway.
Phosphorylation (phosphorylation) of MuSK associated with congenital myasthenic syndromes and congenital anomalies
3) Confidence 0.80 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.34 Pain Relevance 0
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).
Phosphorylation (autophosphorylation) of MuSK
4) Confidence 0.79 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.26 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).
Phosphorylation (phorphorylation) of MuSK
5) Confidence 0.70 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.23 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.
Phosphorylation (phosphorylation) of MuSK associated with congenital myasthenic syndromes
6) Confidence 0.70 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.23 Pain Relevance 0
Thus, these findings demonstrate that the identified MUSK mutations affect the normal interaction between MuSK and Dok-7 and impair MuSK phosphorylation.
Phosphorylation (phosphorylation) of MuSK
7) Confidence 0.61 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0 Pain Relevance 0
These mutations impair the expression and stability of MuSK, diminish agrin-dependent MuSK phosphorylation and AChR clustering, and fail to co-immunoprecipitate with Dok-7 but not with Lrp4 or Tid1.
Phosphorylation (phosphorylation) of MuSK
8) Confidence 0.61 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.38 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.
Phosphorylation (phosphorylation) of MuSK in myotubes
9) Confidence 0.61 Published 2010 Journal Human Molecular Genetics Section Abstract Doc Link PMC2876883 Disease Relevance 0.26 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.
Phosphorylation (phosphorylation) of MuSK
10) Confidence 0.61 Published 2010 Journal Human Molecular Genetics Section Abstract Doc Link PMC2876883 Disease Relevance 0.26 Pain Relevance 0
These mutations impair the expression and stability of MuSK, diminish agrin-dependent MuSK phosphorylation and AChR clustering, and fail to co-immunoprecipitate with Dok-7 but not with Lrp4 or Tid1.
Phosphorylation (phosphorylation) of MuSK
11) Confidence 0.61 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.38 Pain Relevance 0
Thus, these findings demonstrate that the identified MUSK mutations affect the normal interaction between MuSK and Dok-7 and impair MuSK phosphorylation.
Phosphorylation (phosphorylation) of MuSK
12) Confidence 0.61 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0 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.
Phosphorylation (phosphorylation) of MuSK
13) Confidence 0.54 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.31 Pain Relevance 0

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