INT265772

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Context Info
Confidence 0.29
First Reported 2009
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 3
Disease Relevance 0
Pain Relevance 0.04

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 (KDR, NRP1) plasma membrane (KDR, NRP1) cell differentiation (NRP1)
cell-cell signaling (NRP1) cytoplasm (KDR) cytosol (NRP1)
KDR (Homo sapiens)
NRP1 (Homo sapiens)
Pain Link Frequency Relevance Heat
addiction 9 86.36 High High
metalloproteinase 9 5.00 Very Low Very Low Very Low
antagonist 9 5.00 Very Low Very Low Very Low
ischemia 6 5.00 Very Low Very Low Very Low
Restless leg syndrome 3 5.00 Very Low Very Low Very Low
Central nervous system 3 5.00 Very Low Very Low Very Low
cytokine 3 5.00 Very Low Very Low Very Low
Inflammation 3 5.00 Very Low Very Low Very Low
tolerance 3 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Peripheral Arterial Disease 54 5.00 Very Low Very Low Very Low
Disease 21 5.00 Very Low Very Low Very Low
Coronary Artery Disease 18 5.00 Very Low Very Low Very Low
Cancer 15 5.00 Very Low Very Low Very Low
Atherosclerosis 12 5.00 Very Low Very Low Very Low
Diabetes Mellitus 12 5.00 Very Low Very Low Very Low
Eclampsia 9 5.00 Very Low Very Low Very Low
Breast Cancer 6 5.00 Very Low Very Low Very Low
Leukemia 6 5.00 Very Low Very Low Very Low
Pressure And Volume Under Development 6 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The minute attenuation of pro-angiogenic potential reflected a declining availability of VEGF165-bound NRP1s for coupling with VEGFR2, hence the diminishing quantities of VEGFR2-VEGF165-NRP1 (Fig. 6D).
VEGFR2 Binding (bound) of NRP1s
1) Confidence 0.29 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
The former effects increased quantities of non-NRP1-coupled VEGF-VEGFR complexes with increasing total VEGFR density, despite the diminishing fractional occupancies of VEGFRs (Fig. 5D).
VEGFR Binding (complexes) of NRP1
2) Confidence 0.29 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0.04
On the other hand, the overall rise in “pro-angiogenic potential”, as represented by ligated VEGFR2 complexes, can be explained by NRP1's role as a co-receptor in presenting NRP1-bound VEGF165 to VEGFR2, as well as in stabilizing VEGF165-VEGFR2 through their triplet configuration.
VEGFR2 Binding (bound) of VEGF165
3) Confidence 0.29 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0

General Comments

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