INT301733

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Context Info
Confidence 0.68
First Reported 2009
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 2
Total Number 5
Disease Relevance 1.76
Pain Relevance 0.09

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
motor neuron 1
Musk (Mus musculus)
Pain Link Frequency Relevance Heat
Neurotransmitter 22 91.28 High High
sodium channel 3 90.00 High High
Action potential 4 17.68 Low Low
Hippocampus 12 5.00 Very Low Very Low Very Low
Central nervous system 8 5.00 Very Low Very Low Very Low
GABAergic 8 5.00 Very Low Very Low Very Low
Glutamate receptor 6 5.00 Very Low Very Low Very Low
amygdala 5 5.00 Very Low Very Low Very Low
anesthesia 4 5.00 Very Low Very Low Very Low
Kinase C 4 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Congenital Myasthenic Syndromes 88 98.88 Very High Very High Very High
Syndrome 14 80.24 Quite High
Disease 9 77.36 Quite High
Respiratory Failure 8 72.88 Quite High
Muscle Weakness 9 67.88 Quite High
Cyanosis 4 37.12 Quite Low
Patent Ductus Arteriosus 4 35.04 Quite Low
Congenital Anomalies 20 16.00 Low Low
Muscular Dystrophy 46 5.00 Very Low Very Low Very Low
Cognitive Disorder 16 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
MuSK phorphorylation and MuSKĀ–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).
Positive_regulation (increases) of MuSK
1) Confidence 0.68 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.21 Pain Relevance 0
In addition to agrin, MuSK activation requires phosphorylation of its Tyr553 residue, located within the juxtamembrane consensus recognition site (NPXY), via the phosphotyrosine-binding domain (PTB domain)-containing protein Dok-7 (11).
Positive_regulation (activation) of MuSK
2) Confidence 0.49 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.51 Pain Relevance 0
The agrin-dependent activation of MuSK through the low-density lipoprotein receptor (LDLR)-related protein (Lrp4) (8,9) is essential for the induction of presynaptic and postsynaptic differentiation, including the clustering of AChRs and rapsyn (10).
Positive_regulation (activation) of MuSK
3) Confidence 0.49 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.66 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.
Positive_regulation (stability) of MuSK
4) Confidence 0.45 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.38 Pain Relevance 0
One such pathway includes agrin, a heparin sulfate proteoglycan that is released from the motor neuron to activate the postsynaptic tyrosine kinase receptor, MuSK.
Positive_regulation (activate) of MuSK in motor neuron
5) Confidence 0.24 Published 2009 Journal Mol Neurobiol Section Body Doc Link PMC2840664 Disease Relevance 0 Pain Relevance 0.09

General Comments

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