INT312601

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Context Info
Confidence 0.62
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 5
Disease Relevance 1.39
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.

lipid binding (Dok7) plasma membrane (Dok7)
Dok7 (Mus musculus)
Pain Link Frequency Relevance Heat
anesthesia 5 5.00 Very Low Very Low Very Low
Action potential 5 5.00 Very Low Very Low Very Low
imagery 5 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Congenital Myasthenic Syndromes 110 97.96 Very High Very High Very High
Congenital Anomalies 10 78.32 Quite High
Syndrome 15 69.12 Quite High
Disease 5 66.24 Quite High
Muscle Weakness 10 56.76 Quite High
Respiratory Failure 10 54.72 Quite High
Myasthenia Gravis 15 5.00 Very Low Very Low Very Low
Frailty 5 5.00 Very Low Very Low Very Low
Ocular Toxicity (including Many Sub-types) 5 5.00 Very Low Very Low Very Low
Cognitive Disorder 5 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
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).
Phosphorylation (phosphorylation) of protein Dok-7
1) Confidence 0.62 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.56 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 Dok-7 associated with congenital myasthenic syndromes
2) Confidence 0.55 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.
Phosphorylation (phosphorylation) of Dok-7
3) Confidence 0.55 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.31 Pain Relevance 0
In contrast, M605I results in moderate impairment of both phosphorylation and binding to Dok-7.
Phosphorylation (phosphorylation) of Dok-7
4) Confidence 0.55 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.28 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 Dok-7
5) Confidence 0.55 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0 Pain Relevance 0

General Comments

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