INT106823

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Context Info
Confidence 0.17
First Reported 2002
Last Reported 2008
Negated 0
Speculated 0
Reported most in Body
Documents 2
Total Number 6
Disease Relevance 3.89
Pain Relevance 0.05

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

cell differentiation (PAPPA) peptidase activity (PAPPA) extracellular region (PAPPA)
plasma membrane (MBP)
Anatomy Link Frequency
eosinophil 6
MBP (Homo sapiens)
PAPPA (Homo sapiens)
Pain Link Frequency Relevance Heat
metalloproteinase 26 90.24 High High
Inflammation 95 47.20 Quite Low
Angina 172 37.84 Quite Low
ischemia 120 5.00 Very Low Very Low Very Low
cytokine 10 5.00 Very Low Very Low Very Low
Pain 5 5.00 Very Low Very Low Very Low
Inflammatory marker 5 5.00 Very Low Very Low Very Low
Inflammatory response 5 5.00 Very Low Very Low Very Low
Inflammatory stimuli 5 5.00 Very Low Very Low Very Low
Bioavailability 5 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Down Syndrome 9 98.40 Very High Very High Very High
Acute Coronary Syndrome 350 83.36 Quite High
Stress 35 80.76 Quite High
Urological Neuroanatomy 140 79.08 Quite High
Atherosclerotic Plaque 50 75.12 Quite High
Death 105 64.76 Quite High
Myocardial Infarction 205 50.08 Quite High
INFLAMMATION 105 47.20 Quite Low
Angina 170 37.84 Quite Low
Threatened Abortion 1 36.40 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
PAPP-A exists in pregnancy serum as a heterotetrameric 2:2 complex with the proform of eosinophil major basic protein (proMBP), forming an approximately 500 kDa and called PAPP-A/proMBP.
basic protein Binding (complex) of PAPP-A in eosinophil
1) Confidence 0.17 Published 2002 Journal Bratisl Lek Listy Section Abstract Doc Link 12448565 Disease Relevance 0 Pain Relevance 0.05
Physiologically, PAPP-A circulates in a hetero-tetrameric complex consisting of two PAPP-A subunits covalently bound with two subunits of the pro-form of eosinophil major basic protein (proMBP), its endogenous inhibitor (Oxvig C et al. 1993).
proMBP Binding (complex) of PAPP-A in eosinophil
2) Confidence 0.01 Published 2008 Journal Biomarker Insights Section Body Doc Link PMC2688349 Disease Relevance 0.81 Pain Relevance 0
Physiologically, PAPP-A circulates in a hetero-tetrameric complex consisting of two PAPP-A subunits covalently bound with two subunits of the pro-form of eosinophil major basic protein (proMBP), its endogenous inhibitor (Oxvig C et al. 1993).
proMBP Binding (complex) of PAPP-A in eosinophil
3) Confidence 0.01 Published 2008 Journal Biomarker Insights Section Body Doc Link PMC2688349 Disease Relevance 0.79 Pain Relevance 0
Physiologically, PAPP-A circulates in a hetero-tetrameric complex consisting of two PAPP-A subunits covalently bound with two subunits of the pro-form of eosinophil major basic protein (proMBP), its endogenous inhibitor (Oxvig C et al. 1993).
proMBP Binding (bound) of PAPP-A in eosinophil
4) Confidence 0.01 Published 2008 Journal Biomarker Insights Section Body Doc Link PMC2688349 Disease Relevance 0.81 Pain Relevance 0
Physiologically, PAPP-A circulates in a hetero-tetrameric complex consisting of two PAPP-A subunits covalently bound with two subunits of the pro-form of eosinophil major basic protein (proMBP), its endogenous inhibitor (Oxvig C et al. 1993).
basic protein Binding (bound) of PAPP-A in eosinophil
5) Confidence 0.01 Published 2008 Journal Biomarker Insights Section Body Doc Link PMC2688349 Disease Relevance 0.73 Pain Relevance 0
Physiologically, PAPP-A circulates in a hetero-tetrameric complex consisting of two PAPP-A subunits covalently bound with two subunits of the pro-form of eosinophil major basic protein (proMBP), its endogenous inhibitor (Oxvig C et al. 1993).
basic protein Binding (bound) of PAPP-A in eosinophil
6) Confidence 0.01 Published 2008 Journal Biomarker Insights Section Body Doc Link PMC2688349 Disease Relevance 0.75 Pain Relevance 0

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