INT196322

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Context Info
Confidence 0.15
First Reported 2006
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 18
Total Number 18
Disease Relevance 7.74
Pain Relevance 0.83

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)
Anatomy Link Frequency
platelet 3
blood 2
cleavage 1
smooth muscle cells 1
bladder 1
F2 (Mus musculus)
Pain Link Frequency Relevance Heat
Inflammation 134 99.64 Very High Very High Very High
Glutamate 1 98.86 Very High Very High Very High
cytokine 20 89.20 High High
Hyperalgesia 4 84.28 Quite High
Pain 12 83.60 Quite High
fibrosis 13 80.72 Quite High
Crohn's disease 1 75.20 Quite High
bradykinin 6 61.48 Quite High
rheumatoid arthritis 3 58.88 Quite High
Multiple sclerosis 82 44.24 Quite Low
Disease Link Frequency Relevance Heat
INFLAMMATION 156 99.64 Very High Very High Very High
Coagulation Disorder 116 97.76 Very High Very High Very High
Thrombosis 116 97.64 Very High Very High Very High
Adhesions 28 95.60 Very High Very High Very High
Carcinoma 18 95.00 High High
Sepsis 51 92.48 High High
Vasculitis 7 92.12 High High
Neuropathic Pain 1 91.52 High High
Bacteremia 50 91.48 High High
Necrosis 10 90.72 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
In addition, we also sacrificed another 37 F2 and F3 mice (18 males and 19 females) at different time points during 2–10 months of age.
F2 Binding (sacrificed) of
1) Confidence 0.15 Published 2006 Journal J Carcinog Section Body Doc Link PMC1559682 Disease Relevance 0.79 Pain Relevance 0.11
The KD for the coagulase·prothrombin interaction is lower than the reported affinity for the D1D2 domain alone [36]; we currently do not appreciate the basis for this difference.
prothrombin Binding (interaction) of
2) Confidence 0.14 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2916881 Disease Relevance 0.24 Pain Relevance 0
A unique N-terminal fragment of OPN (trOPN), produced by thrombin cleavage has previously been shown to be present in plasma and milk and may have physiologically distinct roles[17]-[19].
thrombin Binding (cleavage) of in cleavage
3) Confidence 0.14 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2791444 Disease Relevance 0 Pain Relevance 0
The new insights on the role of thrombin and tcOPN as well as the well characterized binding of the latter to the integrins ?
thrombin Binding (binding) of
4) Confidence 0.14 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2791444 Disease Relevance 0.06 Pain Relevance 0
Thrombin or a specific PAR1 or PAR4 activating peptide (PAR1/4-AP) caused functional effects characteristic of activation of the PLC?
Thrombin Binding (specific) of
5) Confidence 0.12 Published 2010 Journal Mol Pain Section Abstract Doc Link PMC2956715 Disease Relevance 0.39 Pain Relevance 0.17
Nevertheless, association of the tetrameric (Coa·prothrombin)2 complex enables fibrinogen binding at a new site with high affinity [19].
prothrombin Binding (association) of
6) Confidence 0.11 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2916881 Disease Relevance 0.21 Pain Relevance 0
To assess vWbp-prothrombin and vWbp-fibrinogen interactions, vWbp was injected at 1 nM, 10 nM, 50 nM, 100 nM, 500 nM, and 1 µM for 60 seconds followed by 60 seconds of dissociation and regeneration.
prothrombin Binding (interactions) of
7) Confidence 0.11 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2916881 Disease Relevance 0 Pain Relevance 0
Clinical isolates of the human pathogen Staphylococcus aureus secrete coagulase (Coa), a polypeptide that binds to and activates prothrombin, thereby converting fibrinogen to fibrin and promoting clotting of plasma or blood.
prothrombin Binding (binds) of in blood associated with coagulation disorder
8) Confidence 0.11 Published 2010 Journal PLoS Pathogens Section Abstract Doc Link PMC2916881 Disease Relevance 0.92 Pain Relevance 0
To measure the interaction of coagulase with prothrombin and fibrinogen, Coa was diluted into HBS-P buffer (20 mM HEPES [pH 7.4], 150 mM NaCl, 0.005% [vol/vol] surfactant P20) at a range of concentrations.
prothrombin Binding (interaction) of
9) Confidence 0.11 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2916881 Disease Relevance 0.06 Pain Relevance 0
Importantly, a high affinity thrombin binding site exists on an alternatively spliced variant of fibrinogen (??
thrombin Binding (site) of
10) Confidence 0.08 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2861630 Disease Relevance 0.13 Pain Relevance 0
Thrombin is a critical player in blood coagulation and is known to bind to the platelet surface and to fibrin(ogen) [13], [29], [30], [31], [32]; however, where thrombin is localized during clot formation is largely unknown.
Thrombin Binding (bind) of in blood
11) Confidence 0.08 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2861630 Disease Relevance 0.16 Pain Relevance 0
FXa bound in a punctate manner to thrombi under shear, while thrombin and fibrin(ogen) distributed ubiquitously over platelet-fibrin thrombi.
thrombin Binding (bound) of in platelet
12) Confidence 0.08 Published 2010 Journal PLoS ONE Section Abstract Doc Link PMC2861630 Disease Relevance 0.27 Pain Relevance 0
Another human bladder cell line, RT4, responds to thrombin, tryptase or PAR-APs with an increase in intracellular phospholipase A2 activity, arachidonic acid and prostaglandin E2 release [30].
thrombin Binding (responds) of in bladder
13) Confidence 0.06 Published 2007 Journal BMC Physiol Section Body Doc Link PMC1853108 Disease Relevance 0.49 Pain Relevance 0.09
TF is a transmembrane cell surface glycoprotein that acts as a receptor for coagulation factor VII/VIIa, catalyzes the conversion of factor X to the active form Xa and ultimately leads to thrombin formation.
thrombin Binding (formation) of
14) Confidence 0.05 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2735777 Disease Relevance 0.91 Pain Relevance 0.10
Together with other components, the tissue factor-driven generation of thrombin with fibrin accumulation and platelet activation play a pivotal role in this setting [4].
thrombin Binding (generation) of in platelet
15) Confidence 0.05 Published 2006 Journal Crit Care Section Body Doc Link PMC1751084 Disease Relevance 0.90 Pain Relevance 0.08
1, promoting the migration and/or growth potential of lymphocytes, macrophages, endothelial cells, and vascular smooth muscle cells; and (ii) a cryptic serine-valine-valine-tyrosine-glutamate-leucine-arginine (SVVYGLR)-containing domain cleaved by thrombin that interacts with ?
thrombin Binding (interacts) of in smooth muscle cells associated with glutamate
16) Confidence 0.03 Published 2010 Journal Cardiovasc Diabetol Section Body Doc Link PMC2988001 Disease Relevance 1.31 Pain Relevance 0.18
Furthermore, at pharmacological (that is, supraphysiological) doses, rFVIIa triggers the thrombin burst through direct binding to activated platelets; sufficient platelets must therefore be available.
thrombin Binding (binding) of in platelets
17) Confidence 0.02 Published 2006 Journal Crit Care Section Body Doc Link PMC1750973 Disease Relevance 0.37 Pain Relevance 0
Lastly, thrombin itself has long been recognized for its inflammatory actions, recently extended by the finding that it is required to initiate CCR2-dependent leukocyte recruitment, and that it is "the principal determinant of the outcome after vascular injury" in several animal models (LPS-induced endotoxemia, antibody-mediated graft rejection, carotid artery ligation) [214].


thrombin Binding (recognized) of in carotid artery associated with endotoxemia, inflammation, vasculitis and graft vs host disease
18) Confidence 0.02 Published 2010 Journal J Neuroinflammation Section Body Doc Link PMC2829540 Disease Relevance 0.52 Pain Relevance 0.11

General Comments

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