INT167636

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Context Info
Confidence 0.52
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 5
Total Number 5
Disease Relevance 5.09
Pain Relevance 0.41

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

extracellular region (Vwf) cell adhesion (Vwf) endoplasmic reticulum (Vwf)
proteinaceous extracellular matrix (Vwf) molecular_function (Vwf) response to stress (Vwf)
Anatomy Link Frequency
neurons 2
platelet 2
plasma 1
Vwf (Rattus norvegicus)
Pain Link Frequency Relevance Heat
metalloproteinase 2 99.66 Very High Very High Very High
Central nervous system 2 89.76 High High
Neuropeptide 70 84.72 Quite High
abdominal pain 3 25.00 Low Low
Intracerebroventricular 6 5.00 Very Low Very Low Very Low
adenocard 2 5.00 Very Low Very Low Very Low
projection neuron 2 5.00 Very Low Very Low Very Low
Pain 2 5.00 Very Low Very Low Very Low
agonist 2 5.00 Very Low Very Low Very Low
Potency 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Cv Unclassified Under Development 13 98.66 Very High Very High Very High
Congenital Anomalies 2 98.16 Very High Very High Very High
Thrombotic Thrombocytopenic Purpura 10 98.06 Very High Very High Very High
Thrombotic Microangiopathies 10 95.88 Very High Very High Very High
Hemolytic Uremic Syndrome 6 93.36 High High
Renal Failure 3 92.76 High High
Solid Tumor 1 92.72 High High
Myeloproliferative Disorder 1 92.12 High High
Syndrome 23 90.12 High High
Fever 4 88.68 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Vascular abnormalities, such as aortic stenosis, may cause increased shear rate of the flowing blood that lead to degradation of large VWF multimers in plasma through proteolytic cleavages.
Protein_catabolism (degradation) of VWF in plasma associated with congenital anomalies and cv unclassified under development
1) Confidence 0.52 Published 2010 Journal BMC Gastroenterol Section Body Doc Link PMC2955688 Disease Relevance 1.67 Pain Relevance 0
Normally the VWF is processed in endothelial cells, however AAV transduces mainly neurons.
Protein_catabolism (processed) of VWF in neurons
2) Confidence 0.42 Published 2010 Journal BMC Neurosci Section Body Doc Link PMC2928777 Disease Relevance 0.06 Pain Relevance 0.12
Therefore, after the VWF signal peptide a furin recognition site (RKRR) was inserted, this to ensure that the VWF signal peptide was cleaved from AgRP83-132 in neurons.
Protein_catabolism (cleaved) of VWF signal peptide in neurons
3) Confidence 0.42 Published 2010 Journal BMC Neurosci Section Body Doc Link PMC2928777 Disease Relevance 0.05 Pain Relevance 0.11
TTP is usually associated with a severe deficiency of ADAMTS13 [a metalloproteinase involved in the degradation of von Willebrand factor (vWF) multimers], causing excessive accumulation of ultra-large vWF multimers and platelet aggregation with organ failure.
Protein_catabolism (degradation) of vWF in platelet associated with metalloproteinase and thrombotic thrombocytopenic purpura
4) Confidence 0.18 Published 2010 Journal Cardiovasc Hematol Disord Drug Targets Section Abstract Doc Link 20397971 Disease Relevance 1.61 Pain Relevance 0.09
TTP is usually associated with a severe deficiency of ADAMTS13 [a metalloproteinase involved in the degradation of von Willebrand factor (vWF) multimers], causing excessive accumulation of ultra-large vWF multimers and platelet aggregation with organ failure.
Protein_catabolism (degradation) of vWF in platelet associated with metalloproteinase and thrombotic thrombocytopenic purpura
5) Confidence 0.16 Published 2010 Journal Cardiovasc Hematol Disord Drug Targets Section Abstract Doc Link 20397971 Disease Relevance 1.70 Pain Relevance 0.09

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