INT79169

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Context Info
Confidence 0.47
First Reported 1998
Last Reported 2010
Negated 2
Speculated 0
Reported most in Body
Documents 10
Total Number 11
Disease Relevance 5.88
Pain Relevance 0.72

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

peptidase activity (PLG) extracellular space (PLG) extracellular region (PLG)
plasma membrane (PLG)
Anatomy Link Frequency
lung 1
neurite 1
PLG (Homo sapiens)
Pain Link Frequency Relevance Heat
metalloproteinase 150 100.00 Very High Very High Very High
Central nervous system 9 100.00 Very High Very High Very High
cINOD 162 74.60 Quite High
Inflammatory mediators 15 74.28 Quite High
Inflammatory response 12 67.08 Quite High
ischemia 5 58.40 Quite High
acular 48 48.00 Quite Low
Inflammation 204 47.56 Quite Low
diclofenac 26 46.96 Quite Low
palliative 1 25.00 Low Low
Disease Link Frequency Relevance Heat
Coronary Artery Disease 3 99.92 Very High Very High Very High
Cardiovascular Disease 13 98.92 Very High Very High Very High
Fibrosis 11 97.28 Very High Very High Very High
Metastasis 54 96.16 Very High Very High Very High
Periodontal Disease 48 95.80 Very High Very High Very High
Cancer 88 95.00 High High
Myocardial Infarction 24 94.08 High High
Breast Cancer 118 91.84 High High
Malignant Neoplastic Disease 3 89.28 High High
Infarction 1 88.64 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Furthermore, we have shown that plasmin associated with the cell surface is responsible for activating the fibrillar collagenase, MMP-13.
plasmin Binding (associated) of
1) Confidence 0.47 Published 2005 Journal Cancer Cell Int Section Body Doc Link PMC548674 Disease Relevance 0.37 Pain Relevance 0.04
Thus by generating plasmin, uPA regulates not only fibrinolysis, but also ECM degradation and fibrotic processes in the lung.


plasmin Binding (generating) of in lung associated with fibrosis
2) Confidence 0.36 Published 2008 Journal International Journal of Chronic Obstructive Pulmonary Disease Section Body Doc Link PMC2629972 Disease Relevance 0.22 Pain Relevance 0.06
This would explain why interfering with only one element, plasmin or MMP activity, has such powerful biological effects.
plasmin Binding (interfering) of
3) Confidence 0.36 Published 2005 Journal Cancer Cell Int Section Body Doc Link PMC548674 Disease Relevance 0.57 Pain Relevance 0.18
Myocardial ischaemia is associated with the activation of MMPs and the serine proteinase plasmin.
plasmin Binding (associated) of associated with coronary artery disease and metalloproteinase
4) Confidence 0.36 Published 2008 Journal The Open Dentistry Journal Section Body Doc Link PMC2581528 Disease Relevance 1.41 Pain Relevance 0.12
The PA/plasmin system and its inhibitors participate in a number of physiological and pathological events in the CNS [15]–[17], and facilitate neurite outgrowth and sustain synaptic plasticity via interaction with extracellular matrix proteoglycans [18]–[20].
plasmin Binding (interaction) of in neurite associated with central nervous system
5) Confidence 0.35 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2815778 Disease Relevance 0.40 Pain Relevance 0.17
From its discovery in 1986 tetranectin (TN) has been suggested to participate in proteolytic processes through its binding to plasminogen, which enhances the activation of plasminogen to plasmin.
plasminogen Binding (binding) of
6) Confidence 0.31 Published 1998 Journal APMIS Suppl. Section Abstract Doc Link 9868384 Disease Relevance 0.23 Pain Relevance 0
By binding to plasminogen, tetranectin may enhance activation of plasminogen to plasmin, which plays a role in the degradation of extracellular proteins and cancer progression.
plasminogen Binding (binding) of associated with cancer
7) Confidence 0.19 Published 2010 Journal International Journal of Molecular Sciences Section Body Doc Link PMC2956083 Disease Relevance 1.21 Pain Relevance 0
Tetranectin binds specifically to the kringle 4 domain of plasminogen, which is a circulating zymogen [51].
plasminogen Binding (binds) of
8) Confidence 0.14 Published 2010 Journal International Journal of Molecular Sciences Section Body Doc Link PMC2956083 Disease Relevance 1.04 Pain Relevance 0
Streptokinase (SK) is an indirect fibrinolytic agent that interacts with plasminogen, forming an active complex with protease activity that converts plasminogen to plasmin [1].
plasminogen Binding (interacts) of
9) Confidence 0.10 Published 2005 Journal BMC Clin Pharmacol Section Body Doc Link PMC1291362 Disease Relevance 0.30 Pain Relevance 0
Enzyme activity is also poorly discernable in the aqueous with exception of plasminogen and plasminogen activator (Blakemore 1995).
plasminogen Neg (exception) Binding (exception) of
10) Confidence 0.04 Published 2008 Journal Clinical ophthalmology (Auckland, N.Z.) Section Body Doc Link PMC2693998 Disease Relevance 0.06 Pain Relevance 0.07
Enzyme activity is also poorly discernable in the aqueous with exception of plasminogen and plasminogen activator (Blakemore 1995).
plasminogen Neg (exception) Binding (exception) of
11) Confidence 0.03 Published 2008 Journal Clinical ophthalmology (Auckland, N.Z.) Section Body Doc Link PMC2693998 Disease Relevance 0.06 Pain Relevance 0.07

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