INT215945

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Context Info
Confidence 0.11
First Reported 2007
Last Reported 2007
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 1
Disease Relevance 0.40
Pain Relevance 0.84

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, Mmp2) peptidase activity (Mmp14, Mmp2) nucleus (Timp2, Mmp2)
cytoplasm (Mmp14, Mmp2) extracellular region (Mmp2) proteinaceous extracellular matrix (Mmp2)
Mmp14 (Mus musculus)
Timp2 (Mus musculus)
Mmp2 (Mus musculus)
Pain Link Frequency Relevance Heat
metalloproteinase 65 100.00 Very High Very High Very High
cytokine 10 85.80 High High
chemokine 6 85.36 High High
Spinal cord 9 82.56 Quite High
Multiple sclerosis 3 40.80 Quite Low
Central nervous system 30 27.12 Quite Low
Inflammation 6 5.00 Very Low Very Low Very Low
anesthesia 1 5.00 Very Low Very Low Very Low
glial activation 1 5.00 Very Low Very Low Very Low
Inflammatory mediators 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Multiple Sclerosis 51 78.72 Quite High
Disease 6 77.04 Quite High
Cancer 5 55.88 Quite High
Malignant Neoplastic Disease 1 49.12 Quite Low
Bordatella Infection 3 29.12 Quite Low
Targeted Disruption 17 24.16 Low Low
Injury 10 18.00 Low Low
INFLAMMATION 7 5.00 Very Low Very Low Very Low
Paralysis 3 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
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 Positive_regulation (activation) of MMP-2 associated with metalloproteinase
1) Confidence 0.11 Published 2007 Journal J Neuroinflammation Section Body Doc Link PMC2075488 Disease Relevance 0.40 Pain Relevance 0.84

General Comments

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