INT330431

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Context Info
Confidence 0.03
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 1
Disease Relevance 0
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.

mitochondrion (Aldh2) small molecule metabolic process (ALDOA) lyase activity (ALDOA)
carbohydrate metabolic process (ALDOA) cytosol (ALDOA) cytoskeletal protein binding (ALDOA)
ALDOA (Homo sapiens)
Aldh2 (Mus musculus)
Pain Link Frequency Relevance Heat
agonist 2 45.20 Quite Low
Angina 5 30.88 Quite Low
tolerance 11 27.92 Quite Low
alcohol 9 5.00 Very Low Very Low Very Low
Dopamine 2 5.00 Very Low Very Low Very Low
fibrosis 1 5.00 Very Low Very Low Very Low
noradrenaline 1 5.00 Very Low Very Low Very Low
addiction 1 5.00 Very Low Very Low Very Low
gABA 1 5.00 Very Low Very Low Very Low
Kinase C 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Cardiovascular Disease 7 46.24 Quite Low
Disease 3 31.76 Quite Low
Cv General 3 Under Development 5 30.88 Quite Low
Myocardial Infarction 11 14.32 Low Low
Cv Unclassified Under Development 15 8.32 Low Low
Stress 23 5.00 Very Low Very Low Very Low
Targeted Disruption 10 5.00 Very Low Very Low Very Low
Toxicity 9 5.00 Very Low Very Low Very Low
Heart Disease 5 5.00 Very Low Very Low Very Low
Coronary Heart Disease 4 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
This enhancement of catalytic activity translates to a possibility of rescuing some enzymatic activity for the ALDH2*2/*2 individuals and restoring the activity of ALDH2*1/*2 individuals to almost the basal level in the wild-type ALDH2*1/*1 individual.9 Co-crystal structures of Alda-1 with both ALDH2*1 wild-type and ALDH2*2 mutant enzymes have recently been resolved and offered detailed mechanistic explanations on how Alda-1 can enhance the enzymatic activity, protect ALDH2 against 4-HNE inactivation, and restore the function of ALDH2*2 mutation.68 Structural comparison revealed that Alda-1 interacts with ALDH2 at the substrate-binding tunnel and kinetically increased the rate of catalysis by reducing the probability of non-productive substrate hydrolysis.
Alda-1 Binding (interacts) of ALDH2
1) Confidence 0.03 Published 2010 Journal Cardiovascular Research Section Body Doc Link PMC2936126 Disease Relevance 0 Pain Relevance 0

General Comments

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