INT312645

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Context Info
Confidence 0.08
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 3
Disease Relevance 0.96
Pain Relevance 0.07

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 (DNAJA3, Musk) unfolded protein binding (DNAJA3) mitochondrion organization (DNAJA3)
embryo development (DNAJA3) cytoplasm (DNAJA3) cytosol (DNAJA3)
Anatomy Link Frequency
Tid1 2
DNAJA3 (Homo sapiens)
Musk (Mus musculus)
Pain Link Frequency Relevance Heat
anesthesia 3 70.40 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 78.88 Quite High
Respiratory Failure 6 61.92 Quite High
Syndrome 9 61.52 Quite High
Disease 3 58.64 Quite High
Muscle Weakness 6 49.16 Quite Low
Myasthenia Gravis 9 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

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
MuSK also binds to the short splice form of the human tumorous imaginal discs (Tid1) protein (12).
Tid1 Binding (binds) of MuSK in Tid1
1) Confidence 0.08 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.37 Pain Relevance 0
Finally, despite the fact that Tid1 interacts with the intracellular portion of MuSK, the patient's mutations do not affect the relationship between MuSK and Tid1.
Tid1 Binding (interacts) of MuSK
2) Confidence 0.06 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2876883 Disease Relevance 0.31 Pain Relevance 0.07
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.



Tid1 Binding (interact) of MuSK in Tid1 associated with congenital myasthenic syndromes
3) Confidence 0.06 Published 2010 Journal Human Molecular Genetics Section Abstract Doc Link PMC2876883 Disease Relevance 0.27 Pain Relevance 0

General Comments

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