INT285167

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Context Info
Confidence 0.04
First Reported 2009
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 2
Total Number 2
Disease Relevance 0.56
Pain Relevance 0.72

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

cytosol (PSMC4) nucleoplasm (PSMC4) mitochondrion (PSMC4)
small molecule metabolic process (PSMC4) nucleolus (PSMC4) ATPase activity (PSMC4)
Anatomy Link Frequency
hinge 1
pore 1
PSMC4 (Homo sapiens)
Pain Link Frequency Relevance Heat
sodium channel 9 89.52 High High
HCN1 46 88.04 High High
Paroxysmal extreme pain disorder 32 86.16 High High
Pain 16 84.56 Quite High
Neuronal excitability 2 82.88 Quite High
dorsal root ganglion 31 82.00 Quite High
local anesthetic 1 63.52 Quite High
Action potential 10 21.36 Low Low
tetrodotoxin 11 5.00 Very Low Very Low Very Low
hCN2 8 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Somatoform Disorder 32 86.16 High High
Erythermalgia 31 85.80 High High
Pain 19 84.56 Quite High
Ganglion Cysts 33 82.00 Quite High
Increased Venous Pressure Under Development 7 51.60 Quite High
Heart Rate Under Development 2 5.00 Very Low Very Low Very Low
Hypertension 1 5.00 Very Low Very Low Very Low
Syndrome 1 5.00 Very Low Very Low Very Low
Hypertrophy 1 5.00 Very Low Very Low Very Low
Disease 1 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Energetic interactions among the MFV377–379 triplet in S6 Among all the pore sites investigated, the S6 residues of the MFV377–379 triplet, which are in close proximity to each other, when Ala-substituted produced the most significant changes in their responses to ZD7288 and gating properties, consistent with the role of S6 residues in drug binding.
S6 Binding (interactions) of in pore
1) Confidence 0.04 Published 2009 Journal Pflugers Arch Section Body Doc Link PMC2765624 Disease Relevance 0 Pain Relevance 0.25
The S4-S5 linker potentially interacts with the C-terminal part of S6 which is bent around a glycine "hinge residue" [37], leading to the opening of the channel gate, and proximity of the S4-S5 linker to S6 within each domain has been verified in hERG channels by cysteine substitution [38].
S6 Binding (interacts) of in hinge
2) Confidence 0.02 Published 2010 Journal Mol Pain Section Body Doc Link PMC2876140 Disease Relevance 0.56 Pain Relevance 0.47

General Comments

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