INT168699

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Context Info
Confidence 0.02
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Abstract
Documents 1
Total Number 2
Disease Relevance 0.45
Pain Relevance 0.46

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

cytoplasm (Nedd4, Tyr) intracellular (Nedd4) ligase activity (Nedd4)
cytosol (Nedd4) cell proliferation (Tyr) pigmentation (Tyr)
Nedd4 (Mus musculus)
Tyr (Mus musculus)
Pain Link Frequency Relevance Heat
tetrodotoxin 2 87.20 High High
sodium channel 4 75.00 Quite High
Nav1.6 2 75.00 Quite High
dorsal root ganglion 2 70.28 Quite High
Neuronal excitability 2 56.44 Quite High
Disease Link Frequency Relevance Heat
Stress 6 97.68 Very High Very High Very High
Ganglion Cysts 2 70.28 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Thus, phosphorylation of the Pro-Gly-Ser-Pro motif within L1 of Na(v)1.6 is necessary for stress-induced current modulation, with positive or negative regulation depending upon the availability of the C-terminal Pro-Ser-Tyr motif to bind Nedd4-2.
Nedd4 Binding (bind) of Pro-Ser-Tyr motif associated with stress
1) Confidence 0.02 Published 2010 Journal J. Biol. Chem. Section Abstract Doc Link 20530479 Disease Relevance 0.19 Pain Relevance 0.17
We also report that the ubiquitin ligase Nedd4-2 interacts with Na(v)1.6 via a Pro-Ser-Tyr(1945) motif in the C terminus of the channel and reduces Na(v)1.6 current density, and we show that this regulation requires both the Pro-Gly-Ser-Pro motif in L1 and the Pro-Ser-Tyr motif in the C terminus.
Nedd4 Binding (interacts) of Pro-Ser-Tyr
2) Confidence 0.02 Published 2010 Journal J. Biol. Chem. Section Abstract Doc Link 20530479 Disease Relevance 0.26 Pain Relevance 0.29

General Comments

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