INT157802

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Context Info
Confidence 0.54
First Reported 2006
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 7
Total Number 11
Disease Relevance 5.75
Pain Relevance 5.51

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) nucleus (Timp2)
Anatomy Link Frequency
amniotic cavity 2
nodules 2
Timp2 (Mus musculus)
Pain Link Frequency Relevance Heat
metalloproteinase 352 100.00 Very High Very High Very High
palliative 215 97.52 Very High Very High Very High
cytokine 32 83.32 Quite High
chemokine 12 82.88 Quite High
Spinal cord 18 82.56 Quite High
anesthesia 3 66.88 Quite High
Inflammation 30 62.88 Quite High
fibrosis 3 50.00 Quite Low
Multiple sclerosis 6 38.32 Quite Low
Central nervous system 62 25.76 Quite Low
Disease Link Frequency Relevance Heat
Rupture 12 97.24 Very High Very High Very High
Cancer 313 96.72 Very High Very High Very High
Multiple Sclerosis 102 78.72 Quite High
Premature Birth 80 77.76 Quite High
Pre-term Labor 26 77.48 Quite High
Disease 14 77.04 Quite High
Lifespan 40 76.16 Quite High
Metastasis 122 75.76 Quite High
Fibrosis 3 75.08 Quite High
Hepatocellular Cancer 290 75.00 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
TIMP2 was down-regulated with reductions in TIMP2 levels to 15.6% of control levels (P < 0.05, Figure 2B).
Negative_regulation (reductions) of TIMP2
1) Confidence 0.54 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2976755 Disease Relevance 0.53 Pain Relevance 0.46
In the palliative resection group, the number of lung metastatic nodules increased markedly as compared to the sham operation group (14.3 ± 4.7 versus 8.7 ± 3.6, P < 0.05); tumor matrix metalloproteinase 2 (MMP2) activity was elevated by 1.4-fold, with up-regulation of vascular endothelial growth factor (VEGF) and down-regulation of tissue inhibitor of metalloproteinase 2 (TIMP2).
Negative_regulation (inhibitor) of TIMP2 in nodules associated with cancer, metalloproteinase and palliative
2) Confidence 0.40 Published 2010 Journal BMC Cancer Section Abstract Doc Link PMC2976755 Disease Relevance 0.92 Pain Relevance 0.76
TIMP2 was down-regulated with reductions in TIMP2 levels to 15.6% of control levels (P < 0.05, Figure 2B).
Negative_regulation (down) of TIMP2
3) Confidence 0.40 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2976755 Disease Relevance 0.53 Pain Relevance 0.47
TIMP2 was down-regulated with reductions in TIMP2 levels to 15.6% of control levels (P < 0.05, Figure 2B).
Negative_regulation (regulated) of TIMP2
4) Confidence 0.40 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2976755 Disease Relevance 0.53 Pain Relevance 0.47
In the palliative resection group, the number of lung metastatic nodules increased markedly as compared to the sham operation group (14.3 ± 4.7 versus 8.7 ± 3.6, P < 0.05); tumor matrix metalloproteinase 2 (MMP2) activity was elevated by 1.4-fold, with up-regulation of vascular endothelial growth factor (VEGF) and down-regulation of tissue inhibitor of metalloproteinase 2 (TIMP2).
Negative_regulation (inhibitor) of metalloproteinase 2 in nodules associated with cancer, metalloproteinase and palliative
5) Confidence 0.34 Published 2010 Journal BMC Cancer Section Abstract Doc Link PMC2976755 Disease Relevance 0.87 Pain Relevance 0.75
Invasion was inhibited by tissue inhibitor of metalloproteinase, TIMP-2, and the broad spectrum synthetic MMP inhibitor, GM6001.
Negative_regulation (inhibitor) of TIMP-2 associated with metalloproteinase
6) Confidence 0.28 Published 2006 Journal BMC Cancer Section Body Doc Link PMC1450297 Disease Relevance 0.39 Pain Relevance 0.60
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].
Negative_regulation (inhibitor) of TIMP-2 associated with metalloproteinase
7) Confidence 0.26 Published 2007 Journal J Neuroinflammation Section Body Doc Link PMC2075488 Disease Relevance 0.40 Pain Relevance 0.80
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].
Negative_regulation (inhibitor) of metalloproteinases-2 associated with metalloproteinase
8) Confidence 0.23 Published 2007 Journal J Neuroinflammation Section Body Doc Link PMC2075488 Disease Relevance 0.39 Pain Relevance 0.80
Moreover, Maymon et al. (2001) found a decrease in tissue inhibitor of matrix metalloproteinase-2 (TIMP-2) in association with term and preterm parturition, term and preterm rupture of fetal membranes, and microbial invasion of the amniotic cavity [50].
Negative_regulation (inhibitor) of TIMP-2 in amniotic cavity associated with rupture and metalloproteinase
9) Confidence 0.16 Published 2010 Journal Obstetrics and Gynecology International Section Body Doc Link PMC2913859 Disease Relevance 0.55 Pain Relevance 0.21
Moreover, Maymon et al. (2001) found a decrease in tissue inhibitor of matrix metalloproteinase-2 (TIMP-2) in association with term and preterm parturition, term and preterm rupture of fetal membranes, and microbial invasion of the amniotic cavity [50].
Negative_regulation (inhibitor) of metalloproteinase-2 in amniotic cavity associated with rupture and metalloproteinase
10) Confidence 0.14 Published 2010 Journal Obstetrics and Gynecology International Section Body Doc Link PMC2913859 Disease Relevance 0.55 Pain Relevance 0.21
RESULTS: Halofuginone prevented cerulein-dependent increase in collagen synthesis, collagen cross-linking enzyme P4Hbeta, Cygb/STAP, and tissue inhibitors of metalloproteinase 2.
Negative_regulation (inhibitors) of metalloproteinase 2
11) Confidence 0.08 Published 2009 Journal Pancreas Section Body Doc Link 19188864 Disease Relevance 0.08 Pain Relevance 0

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