INT256594

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Context Info
Confidence 0.32
First Reported 2009
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 3
Total Number 7
Disease Relevance 0.29
Pain Relevance 0.25

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

nucleus (HBP1) DNA binding (HBP1)
HBP1 (Homo sapiens)
Pain Link Frequency Relevance Heat
diclofenac 15 67.88 Quite High
Inflammation 30 64.64 Quite High
cINOD 39 63.28 Quite High
Potency 23 32.88 Quite Low
Central nervous system 9 17.40 Low Low
cOX1 5 5.00 Very Low Very Low Very Low
imagery 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Alzheimer's Dementia 116 94.56 High High
Amyloidosis 52 67.60 Quite High
INFLAMMATION 35 64.64 Quite High
Cardiomyopathy 20 36.60 Quite Low
Disease 37 31.00 Quite Low
Familial Amyloidotic Polyneuropathy 23 25.04 Quite Low
Rheumatoid Arthritis 6 5.00 Very Low Very Low Very Low
Pressure And Volume Under Development 5 5.00 Very Low Very Low Very Low
Targeted Disruption 4 5.00 Very Low Very Low Very Low
Sprains And Strains 2 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The iodine atom in the iododiflunisal complex establishes close hydrophobic interactions with Leu17, Thr106, Ala108, Thr119 and Val121, thus, occupying the HBP1 pocket which is the outermost and more hydrophobic HBP.
HBP1 Binding (interactions) of
1) Confidence 0.32 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2607018 Disease Relevance 0 Pain Relevance 0
Thus, the iodine atom of these analogues interact with residues Leu17 and Ala 108 at distances ranging from 3.8 to 4.9 Å but it is more efficiently accommodated to the HBP1 because of a new hydrophobic interaction with Met13 and reinforcement of all the others.
HBP1 Binding (interaction) of
2) Confidence 0.32 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2607018 Disease Relevance 0 Pain Relevance 0
The sulfonamide pendant methyl group may also interact with the HBP1 and HBP1' pockets of the TTR outer binding pockets.
HBP1 Binding (interact) of
3) Confidence 0.13 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0 Pain Relevance 0
The sulfonamide pendant methyl group may also interact with the HBP1 and HBP1' pockets of the TTR outer binding pockets.
HBP1 Binding (interact) of
4) Confidence 0.13 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0 Pain Relevance 0
Six halogen binding pockets (HBP1, HBP1', HBP2, HBP2', HBP3 and HBP3') were also defined within each hormone binding pocket based on the positions of the halogen atoms of T4 in the TTR?
HBP1 Binding (binding) of
5) Confidence 0.10 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0.06 Pain Relevance 0.16
As shown in Figure 8e the aryl compound 24 predicted to bind in a forward binding mode while the fluorenyl analog 26 binds in the reverse binding mode (Figure 8f) with extended interactions in HBP3s and HBP1s respectively.


HBP1s Binding (interactions) of
6) Confidence 0.10 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0.23 Pain Relevance 0.09
The biaryl system facilitated additional hydrophobic interactions with the HBP1 residues (Figure 9b) and positioned its carboxyl group close to Glu54 to form additional hydrogen bond interactions, resulting in an improved fibrillization inhibition [22] of 73% inhibition at 3.6 µM.
HBP1 Binding (interactions) of
7) Confidence 0.09 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0 Pain Relevance 0

General Comments

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