INT329649

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Context Info
Confidence 0.02
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 3
Disease Relevance 2.39
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.

cytoplasm (VEGFA, Rrm2) nuclear envelope (Rrm2) extracellular space (VEGFA)
oxidoreductase activity (Rrm2) growth (VEGFA) extracellular region (VEGFA)
VEGFA (Homo sapiens)
Rrm2 (Mus musculus)
Pain Link Frequency Relevance Heat
psoriasis 3 5.00 Very Low Very Low Very Low
anesthesia 3 5.00 Very Low Very Low Very Low
Arthritis 3 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Apoptosis 81 98.60 Very High Very High Very High
Acute Liver Failure 66 86.04 High High
Pathologic Processes 6 77.56 Quite High
Pathologic Neovascularization 6 70.24 Quite High
Disease 3 68.08 Quite High
Cancer 9 67.44 Quite High
Wound Healing 3 63.72 Quite High
Injury 12 28.08 Quite Low
Poisoning 24 5.00 Very Low Very Low Very Low
Diabetic Retinopathy 3 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Although R1 shows a high affinity to VEGF, at least 10-fold higher than R2, R2 is a major positive mitogenic signal transducer through its strong kinase activity as compared with R1 [9].
VEGF Binding (affinity) of R2
1) Confidence 0.02 Published 2010 Journal J Angiogenes Res Section Body Doc Link PMC2933582 Disease Relevance 0.63 Pain Relevance 0
In addition, treatment with R2-mAb was more potent than that with R1-mAb, indicating that VEGF-R2 interaction was a major regulator of the anti-apoptotic effect as well as the maintenance of the SEC architecture.
VEGF Binding (interaction) of R2 associated with apoptosis
2) Confidence 0.02 Published 2010 Journal J Angiogenes Res Section Body Doc Link PMC2933582 Disease Relevance 0.88 Pain Relevance 0
In addition, treatment with R2-mAb was more potent than that with R1-mAb, indicating that VEGF-R2 interaction was a major regulator of the anti-apoptotic effect as well as the maintenance of the SEC architecture.
VEGF Binding (interaction) of R2 associated with apoptosis
3) Confidence 0.02 Published 2010 Journal J Angiogenes Res Section Body Doc Link PMC2933582 Disease Relevance 0.88 Pain Relevance 0

General Comments

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