INT312639

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Context Info
Confidence 0.23
First Reported 2010
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 1
Total Number 3
Disease Relevance 0.91
Pain Relevance 0.06

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, Lrp4) anatomical structure development (Lrp4) signal transduction (Musk)
kinase activity (Musk)
Anatomy Link Frequency
Tid1 1
Musk (Mus musculus)
Lrp4 (Mus musculus)
Pain Link Frequency Relevance Heat
anesthesia 3 63.52 Quite High
Action potential 3 5.00 Very Low Very Low Very Low
imagery 3 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Congenital Myasthenic Syndromes 66 99.28 Very High Very High Very High
Congenital Anomalies 6 92.00 High High
Myasthenia Gravis 9 5.00 Very Low Very Low Very Low
Syndrome 9 5.00 Very Low Very Low Very Low
Respiratory Failure 6 5.00 Very Low Very Low Very Low
Muscle Weakness 6 5.00 Very Low Very Low Very Low
Frailty 3 5.00 Very Low Very Low Very Low
Ocular Toxicity (including Many Sub-types) 3 5.00 Very Low Very Low Very Low
Cognitive Disorder 3 5.00 Very Low Very Low Very Low
Disease 3 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
This was not entirely unexpected since Lrp4 interacts with the extracellular portion of MuSK and the mutations are situated in the TKD of the enzyme located intracellularly.
MuSK Binding (interacts) of Lrp4
1) Confidence 0.23 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.32 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 Lrp4 in Tid1 associated with congenital myasthenic syndromes
2) Confidence 0.17 Published 2010 Journal Human Molecular Genetics Section Abstract Doc Link PMC2876883 Disease Relevance 0.27 Pain Relevance 0
Thus, the abnormal function of the MuSK mutants can not be explained on the basis of an impaired interaction between agrin and MuSK through the co-receptor Lrp4.
MuSK Neg (impaired) Binding (interaction) of Lrp4
3) Confidence 0.17 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.32 Pain Relevance 0.06

General Comments

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