INT265750

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Context Info
Confidence 0.37
First Reported 2009
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 8
Disease Relevance 0.54
Pain Relevance 0.07

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

cytoplasm (FLT1, KDR) extracellular region (FLT1, KDR) nucleus (FLT1, KDR)
plasma membrane (FLT1, KDR) cell differentiation (FLT1) endosome (FLT1)
Anatomy Link Frequency
lymph 1
FLT1 (Homo sapiens)
KDR (Homo sapiens)
Pain Link Frequency Relevance Heat
addiction 24 72.80 Quite High
metalloproteinase 24 13.36 Low Low
antagonist 24 5.00 Very Low Very Low Very Low
ischemia 16 5.00 Very Low Very Low Very Low
Restless leg syndrome 8 5.00 Very Low Very Low Very Low
Central nervous system 8 5.00 Very Low Very Low Very Low
cytokine 8 5.00 Very Low Very Low Very Low
Inflammation 8 5.00 Very Low Very Low Very Low
tolerance 8 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Peripheral Arterial Disease 144 98.44 Very High Very High Very High
Increased Venous Pressure Under Development 16 74.08 Quite High
Tumor Necrosis Factor Receptor-associated Periodic Syndrome 16 66.24 Quite High
Hypoxia 8 61.92 Quite High
Disease 56 5.00 Very Low Very Low Very Low
Coronary Artery Disease 48 5.00 Very Low Very Low Very Low
Cancer 40 5.00 Very Low Very Low Very Low
Atherosclerosis 32 5.00 Very Low Very Low Very Low
Diabetes Mellitus 32 5.00 Very Low Very Low Very Low
Eclampsia 24 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
However, the present study did not rule out the possibility that monomeric sVEGFR1, in its capacity to heterodimerize with surface VEGFR1 or VEGFR2 monomers, can significantly alter these distributions.


sVEGFR1 Binding (heterodimerize) of VEGFR2
1) Confidence 0.37 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
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-VEGF165-NRP1 Binding (bound) of VEGFR2
2) Confidence 0.33 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
In the interstitium, the fractional VEGF-occupancies of VEGFR1 and VEGFR2 decreased <1% within the 100-fold increase in kL tested.
VEGFR1 Binding (occupancies) of VEGFR2
3) Confidence 0.32 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0.07 Pain Relevance 0
In the interstitium, the fractional occupancies of VEGFR1 and VEGFR2 by VEGF decreased <0.5% within the 100-fold increase in kP tested.

6.2.

VEGFR1 Binding (occupancies) of VEGFR2
4) Confidence 0.32 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0.07 Pain Relevance 0
Furthermore, sVEGFR1-heterodimerization with surface VEGFRs (i.e., the association between monomeric sVEGFR1 and surface VEGFR monomers) was neglected in this first study to independently investigate sVEGFR1's VEGF-trapping function (Fig. 1C: interactions ‘T1-3’).

2.

sVEGFR1-heterodimerization Binding (association) of VEGFR
5) Confidence 0.29 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0.04
If future considerations of sVEGFR1 heterodimerization with surface VEGFR can establish a link between transport-dependent fluctuations in sVEGFR1 levels and angiogenic signalling intensity, the clinical implications would be significant: e.g., therapeutic delivery of VEGF-C/D (the VEGF family members involved in lymphangiogenesis) alongside VEGF-A to ischemic tissues could be explored for synergistic effects of increased lymph flow on the angiogenic efficacy of VEGF-A.
sVEGFR1 Binding (heterodimerization) of VEGFR in lymph
6) Confidence 0.29 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0.32 Pain Relevance 0
sVEGFR1-heterodimerization of surface VEGFRs is expected to present an alternative way for sVEGFR1 to modulate VEGF signal transduction even when interstitial free VEGF levels remain high, by effectively reducing the availability of functional endothelial surface VEGFR dimers for VEGF activation, assuming that VEGFR heterodimers with sVEGFR1 cannot signal.
sVEGFR1 Binding (heterodimers) of VEGFR
7) Confidence 0.29 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0.07 Pain Relevance 0
Furthermore, sVEGFR1-heterodimerization with surface VEGFRs (i.e., the association between monomeric sVEGFR1 and surface VEGFR monomers) was neglected in this first study to independently investigate sVEGFR1's VEGF-trapping function (Fig. 1C: interactions ‘T1-3’).

2.

sVEGFR1 Binding (association) of VEGFR
8) Confidence 0.28 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0.04

General Comments

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