INT168000

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Context Info
Confidence 0.63
First Reported 2006
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 6
Total Number 6
Disease Relevance 2.19
Pain Relevance 0.63

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 (F2) extracellular space (F2) extracellular region (F2)
plasma membrane (F2)
Anatomy Link Frequency
endothelial cell 1
cleavage 1
platelet 1
F2 (Homo sapiens)
Pain Link Frequency Relevance Heat
Inflammation 142 94.36 High High
cva 5 91.92 High High
Potency 2 87.24 High High
anesthesia 5 83.68 Quite High
cytokine 149 79.48 Quite High
abdominal pain 4 51.84 Quite High
tolerance 1 48.44 Quite Low
rheumatoid arthritis 2 17.72 Low Low
Inflammatory response 10 5.00 Very Low Very Low Very Low
addiction 3 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Coagulation Disorder 2 99.50 Very High Very High Very High
Myocardial Infarction 1 98.96 Very High Very High Very High
Thrombosis 52 98.28 Very High Very High Very High
INFLAMMATION 154 94.36 High High
Thromboembolism 3 92.28 High High
Pressure Volume 2 Under Development 4 90.40 High High
Death 16 81.40 Quite High
Cv General 4 Under Development 3 76.96 Quite High
Paroxysmal Nocturnal Hemoglobinuria 1 75.80 Quite High
Thrombosis Related Under Development 3 74.08 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
This is possible because the variant prothrombin is resistant to degradation.
Protein_catabolism (degradation) of prothrombin
1) Confidence 0.63 Published 2010 Journal J Med Case Reports Section Body Doc Link PMC2868876 Disease Relevance 0.94 Pain Relevance 0.09
To design the efficient thrombin inhibitors we have synthesized and studied peptide-based inhibitors resistant to enzymatic degradation.
Protein_catabolism (degradation) of thrombin
2) Confidence 0.48 Published 2008 Journal The Open Biochemistry Journal Section Abstract Doc Link PMC2627521 Disease Relevance 0.29 Pain Relevance 0.09
As prothrombin can be enzymatically cleaved into thrombin in the presence of active proteases, labeling was performed in the presence of the serine protease inhibitor PPACK.
Protein_catabolism (cleaved) of prothrombin
3) Confidence 0.18 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2861630 Disease Relevance 0.06 Pain Relevance 0
When bound to thrombomodulin, a thrombin receptor on the endothelial cell surface, thrombin activates protein C, which can degrade Factor VIIIa and Factor Va, essential cofactors in the activation of Factor X and prothrombin respectively [164].
Protein_catabolism (degrade) of prothrombin in endothelial cell
4) Confidence 0.09 Published 2006 Journal Malar J Section Body Doc Link PMC1629020 Disease Relevance 0.51 Pain Relevance 0.22
Coagulation parameters such as hematocrit, activated clotting time (ACT), fibrinogen, prothrombin time (PT), international normalized ratio (INR), platelet count, and fibrin degradation products (FDP) were investigated before cardiopulmonary bypass (CPB), after protamine administration, and at four hours postoperatively in the ICU.
Protein_catabolism (degradation) of prothrombin in platelet associated with coagulation disorder
5) Confidence 0.08 Published 2010 Journal Ann Card Anaesth Section Abstract Doc Link 20442540 Disease Relevance 0.31 Pain Relevance 0.23
To address this issue, we analyzed the time course of human prothrombin cleavage by Bi-VSP and found that thrombin was the major cleavage product (Figure 4).
Protein_catabolism (cleavage) of prothrombin in cleavage
6) Confidence 0.07 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2862700 Disease Relevance 0.08 Pain Relevance 0

General Comments

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