INT76915

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Context Info
Confidence 0.14
First Reported 1997
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 6
Total Number 7
Disease Relevance 4.48
Pain Relevance 0.89

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 (Gpx3) oxidoreductase activity (Gpx3) extracellular region (Gpx3)
Anatomy Link Frequency
extracellular matrix 3
Cleavage 1
plaques 1
immune system 1
Gpx3 (Mus musculus)
Pain Link Frequency Relevance Heat
Inflammation 41 100.00 Very High Very High Very High
cytokine 9 100.00 Very High Very High Very High
Angina 1 92.52 High High
fibrosis 38 88.56 High High
Central nervous system 3 77.92 Quite High
metalloproteinase 43 70.24 Quite High
antagonist 4 68.24 Quite High
Inflammatory response 5 23.68 Low Low
imagery 54 5.00 Very Low Very Low Very Low
long-term potentiation 26 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
INFLAMMATION 46 100.00 Very High Very High Very High
Rupture 1 98.48 Very High Very High Very High
Injury 50 98.28 Very High Very High Very High
Cirrhosis 15 97.96 Very High Very High Very High
Atherosclerotic Plaque 1 97.92 Very High Very High Very High
Atherosclerosis 4 96.04 Very High Very High Very High
Dwarfism 25 93.92 High High
Hutchinson-gilford Progeria Syndrome 41 93.44 High High
Myocardial Infarction 1 93.44 High High
Adhesions 13 93.20 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Moreover, lipid-filled macrophages, by secreting extracellular matrix-degrading enzymes, may weaken rupture-prone atherosclerotic plaques, thus increasing the probability of precipitating atherosclerotic acute symptoms (i.e., myocardial infarction, angina, etc.).
Localization (secreting) of extracellular in plaques associated with atherosclerotic plaque, angina, atherosclerosis, rupture and myocardial infarction
1) Confidence 0.14 Published 1997 Journal Ann. N. Y. Acad. Sci. Section Abstract Doc Link 9704060 Disease Relevance 0.83 Pain Relevance 0.13
Hepatocellular injury usually leads to inflammation and activation of the innate immune system, leading to release of growth factors, cytokines and small molecular mediators that can stimulate extracellular matrix (ECM) synthesis by activation of quiescent hepatic stellate cells and fibroblasts/myofibroblasts (collectively named HSCs) [1], [2].
Localization (release) of extracellular in immune system associated with cirrhosis, inflammation, injury and cytokine
2) Confidence 0.02 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2892485 Disease Relevance 1.41 Pain Relevance 0.46
If microglia directly modulate the extracellular space, they may do this through the secretion of various proteases that degrade extracellular matrix proteins, including cathepsins, metalloproteases, and tissue-type plasminogen activator [35].
Localization (secretion) of extracellular in extracellular matrix
3) Confidence 0.02 Published 2010 Journal PLoS Biology Section Body Doc Link PMC2970556 Disease Relevance 0 Pain Relevance 0
In the event of pathological insult, microglia rapidly become activated, thicken and retract their processes, migrate to the site of injury, proliferate, and participate in the presentation of antigens, phagocytosis of cellular debris, and secretion of proteases that promote microglial motility, as well as myelin and extracellular matrix degradation [5]–[7].
Localization (secretion) of extracellular in extracellular matrix associated with injury
4) Confidence 0.02 Published 2010 Journal PLoS Biology Section Body Doc Link PMC2970556 Disease Relevance 0.18 Pain Relevance 0.04
Mechanistically, this may be due to not only reduced proliferative capacity per se but also altered characteristics of senescent cells such as secretion of inflammatory cytokines and extracellular matrix-degrading enzymes [44].
Localization (secretion) of extracellular in extracellular matrix associated with inflammation and cytokine
5) Confidence 0.02 Published 2006 Journal PLoS Genetics Section Body Doc Link PMC1698946 Disease Relevance 1.63 Pain Relevance 0.10
Cleavage at the cell surface would release soluble proteins for extracellular degradation or clearance.
Localization (release) of extracellular in Cleavage
6) Confidence 0.01 Published 2006 Journal Mol Neurodegener Section Body Doc Link PMC1635701 Disease Relevance 0.29 Pain Relevance 0
To gain insight into the possible mechanisms of soluble apoE receptors, we will briefly consider the functions of released extracellular domains of various other transmembrane proteins.
Localization (released) of extracellular
7) Confidence 0.01 Published 2006 Journal Mol Neurodegener Section Body Doc Link PMC1635701 Disease Relevance 0.15 Pain Relevance 0.17

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