INT215943

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Context Info
Confidence 0.21
First Reported 2007
Last Reported 2007
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 4
Disease Relevance 1.59
Pain Relevance 3.33

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

extracellular space (Timp2) peptidase activity (Mmp14) nucleus (Timp2)
cytoplasm (Mmp14)
Mmp14 (Mus musculus)
Timp2 (Mus musculus)
Pain Link Frequency Relevance Heat
metalloproteinase 260 100.00 Very High Very High Very High
cytokine 40 84.88 Quite High
chemokine 24 84.44 Quite High
Spinal cord 36 82.56 Quite High
Multiple sclerosis 12 39.88 Quite Low
Central nervous system 120 26.20 Quite Low
Inflammation 24 5.00 Very Low Very Low Very Low
anesthesia 4 5.00 Very Low Very Low Very Low
glial activation 4 5.00 Very Low Very Low Very Low
Inflammatory mediators 4 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Multiple Sclerosis 204 78.72 Quite High
Disease 24 77.04 Quite High
Cancer 20 54.96 Quite High
Malignant Neoplastic Disease 4 48.20 Quite Low
Bordatella Infection 12 29.12 Quite Low
Targeted Disruption 68 24.16 Low Low
Injury 40 18.00 Low Low
INFLAMMATION 28 5.00 Very Low Very Low Very Low
Paralysis 12 5.00 Very Low Very Low Very Low
Sprains And Strains 8 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
In addition, MT-MMPs are known to cleave and activate secreted MMPs, which was first described for activation of MMP-2 by MMP-14 through interaction with tissue inhibitor of metalloproteinases-2 (TIMP-2) [15,16].
MMP-14 Binding (interaction) of TIMP-2 associated with metalloproteinase
1) Confidence 0.21 Published 2007 Journal J Neuroinflammation Section Body Doc Link PMC2075488 Disease Relevance 0.40 Pain Relevance 0.83
In addition, MT-MMPs are known to cleave and activate secreted MMPs, which was first described for activation of MMP-2 by MMP-14 through interaction with tissue inhibitor of metalloproteinases-2 (TIMP-2) [15,16].
MMP-14 Binding (interaction) of TIMP-2 associated with metalloproteinase
2) Confidence 0.21 Published 2007 Journal J Neuroinflammation Section Body Doc Link PMC2075488 Disease Relevance 0.40 Pain Relevance 0.83
In addition, MT-MMPs are known to cleave and activate secreted MMPs, which was first described for activation of MMP-2 by MMP-14 through interaction with tissue inhibitor of metalloproteinases-2 (TIMP-2) [15,16].
MMP-14 Binding (interaction) of metalloproteinases-2 associated with metalloproteinase
3) Confidence 0.18 Published 2007 Journal J Neuroinflammation Section Body Doc Link PMC2075488 Disease Relevance 0.40 Pain Relevance 0.83
In addition, MT-MMPs are known to cleave and activate secreted MMPs, which was first described for activation of MMP-2 by MMP-14 through interaction with tissue inhibitor of metalloproteinases-2 (TIMP-2) [15,16].
MMP-14 Binding (interaction) of metalloproteinases-2 associated with metalloproteinase
4) Confidence 0.18 Published 2007 Journal J Neuroinflammation Section Body Doc Link PMC2075488 Disease Relevance 0.40 Pain Relevance 0.83

General Comments

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