INT314510

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Context Info
Confidence 0.10
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 4
Disease Relevance 3.28
Pain Relevance 1.86

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

pigmentation (TH) cytosol (TH) mitochondrion (TH)
small molecule metabolic process (TH) nucleus (TH) cellular nitrogen compound metabolic process (TH)
TH (Homo sapiens)
Pain Link Frequency Relevance Heat
agonist 60 94.28 High High
Dopamine 176 93.92 High High
antagonist 8 86.40 High High
Substantia nigra 4 72.48 Quite High
rheumatoid arthritis 4 62.24 Quite High
carbamazepine 12 5.00 Very Low Very Low Very Low
tolerance 12 5.00 Very Low Very Low Very Low
Pain 8 5.00 Very Low Very Low Very Low
Spinal cord 4 5.00 Very Low Very Low Very Low
midbrain 4 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Restless Legs Syndrome 336 96.24 Very High Very High Very High
Anaemia 20 87.20 High High
Syndrome 16 83.44 Quite High
Chronic Renal Failure 4 63.84 Quite High
Rheumatoid Arthritis 4 62.24 Quite High
Sleep Disorders 88 59.28 Quite High
Thyroid Disease 28 5.00 Very Low Very Low Very Low
Disease 24 5.00 Very Low Very Low Very Low
Hypothyroidism 16 5.00 Very Low Very Low Very Low
Pain 8 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The cytochrome P450 (CYP450) superfamily is another enzymatic complex that is down-regulated in response to iron scarcity.11 CYP450 is constituted by heme proteins and, thus, contains iron.12 In TH metabolism, the CYP450 complex is very important in the degradation of TH through what is called the “Phase 1 elimination of a drug”.13 Drugs that inhibit CYP450 activity down-regulate the degradation of substances, such as TH, that are substrates of CYP450.
Protein_catabolism (degradation) of TH
1) Confidence 0.10 Published 2010 Journal Clinics (Sao Paulo) Section Body Doc Link PMC2882550 Disease Relevance 0.64 Pain Relevance 0.39
The CYP450 enzymes are heme enzymes (all have iron) and the CPY450 enzyme superfamily is important for the biochemical degradation of TH.
Protein_catabolism (degradation) of TH
2) Confidence 0.10 Published 2010 Journal Clinics (Sao Paulo) Section Body Doc Link PMC2882550 Disease Relevance 1.01 Pain Relevance 0.55
The cytochrome P450 (CYP450) superfamily is another enzymatic complex that is down-regulated in response to iron scarcity.11 CYP450 is constituted by heme proteins and, thus, contains iron.12 In TH metabolism, the CYP450 complex is very important in the degradation of TH through what is called the “Phase 1 elimination of a drug”.13 Drugs that inhibit CYP450 activity down-regulate the degradation of substances, such as TH, that are substrates of CYP450.
Protein_catabolism (degradation) of TH
3) Confidence 0.09 Published 2010 Journal Clinics (Sao Paulo) Section Body Doc Link PMC2882550 Disease Relevance 0.58 Pain Relevance 0.41
However, low iron levels diminish the quantity of CYP450 available to degrade TH.
Protein_catabolism (degrade) of TH
4) Confidence 0.08 Published 2010 Journal Clinics (Sao Paulo) Section Body Doc Link PMC2882550 Disease Relevance 1.04 Pain Relevance 0.50

General Comments

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