INT230060

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Context Info
Confidence 0.47
First Reported 2008
Last Reported 2010
Negated 2
Speculated 0
Reported most in Body
Documents 7
Total Number 7
Disease Relevance 5.61
Pain Relevance 3.20

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

aging (Timp1) extracellular region (Timp1) proteinaceous extracellular matrix (Timp1)
Anatomy Link Frequency
joint 1
upper 1
Timp1 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
metalloproteinase 268 100.00 Very High Very High Very High
fibrosis 153 99.48 Very High Very High Very High
cytokine 37 95.08 Very High Very High Very High
Inflammation 26 84.24 Quite High
agonist 57 82.00 Quite High
antagonist 11 53.00 Quite High
Potency 16 16.16 Low Low
Osteoarthritis 8 5.00 Very Low Very Low Very Low
anesthesia 7 5.00 Very Low Very Low Very Low
alcohol 5 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Arthritis 4 100.00 Very High Very High Very High
Cirrhosis 152 99.48 Very High Very High Very High
Pathologic Processes 5 98.64 Very High Very High Very High
Fibrosis 106 97.44 Very High Very High Very High
Keloid Scars 5 94.68 High High
Injury 115 91.28 High High
Disease 6 86.80 High High
Hepatocellular Cancer 5 85.84 High High
Congenital Anomalies 10 85.68 High High
INFLAMMATION 27 84.24 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Because matrix turnover is tightly regulated, activation of pro-MMPs to active MMPs is strictly controlled by complex formation with TIMPs (20).
TIMP Binding (formation) of associated with metalloproteinase
1) Confidence 0.47 Published 2010 Journal Journal of Korean Medical Science Section Body Doc Link PMC2844613 Disease Relevance 1.20 Pain Relevance 0.48
MMP activities are regulated by TIMPs, which bind in substrate and tissue specific manners to MMPs, blocking their proteolytic activity (19).
TIMP Binding (bind) of associated with metalloproteinase
2) Confidence 0.47 Published 2010 Journal Journal of Korean Medical Science Section Body Doc Link PMC2844613 Disease Relevance 1.43 Pain Relevance 0.48
We did not characterize MMPs or TIMPs function or conversion from pro to active forms, which may be confirmed in future studies.
TIMP Neg (not) Binding (characterize) of associated with metalloproteinase
3) Confidence 0.36 Published 2010 Journal Journal of Korean Medical Science Section Body Doc Link PMC2844613 Disease Relevance 0.98 Pain Relevance 0.67
The mechanism of activation involves TIMP-2 interaction with MT1-MMP to form a receptor complex that regulates the activation of MMP-2 (8-11).
TIMP Binding (interaction) of
4) Confidence 0.34 Published 2010 Journal Journal of Korean Medical Science Section Body Doc Link PMC2844613 Disease Relevance 0.72 Pain Relevance 0.40
MMP, TIMP, and ?
TIMP Binding (MMP) of
5) Confidence 0.26 Published 2010 Journal Journal of Korean Medical Science Section Abstract Doc Link PMC2844613 Disease Relevance 0.72 Pain Relevance 0.39
The exception was for tissue inhibitor of metalloproteinase-1 (TIMP-1) and tissue inhibitor of metalloproteinase-2 (TIMP-2), which were detected in ACCS at the upper limit of known physiological levels.
TIMP-1 Neg (exception) Binding (was) of in upper associated with metalloproteinase
6) Confidence 0.14 Published 2008 Journal Eplasty Section Body Doc Link PMC2323202 Disease Relevance 0.33 Pain Relevance 0.45
TIMP-1 and TIMP-3 may be beneficial for normal joints; however, their increase in human or bovine arthritic joint has been associated with pathological remodelling [36].
TIMP-1 Binding (associated) of in joint associated with arthritis
7) Confidence 0.12 Published 2010 Journal PPAR Research Section Body Doc Link PMC2957135 Disease Relevance 0.22 Pain Relevance 0.35

General Comments

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