INT255690

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Context Info
Confidence 0.34
First Reported 2008
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 8
Total Number 12
Disease Relevance 3.44
Pain Relevance 0.61

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

cytoplasm (VEGFA, Flt1) cell differentiation (Flt1) endosome (Flt1)
Golgi apparatus (Flt1) extracellular space (VEGFA) extracellular region (VEGFA)
Anatomy Link Frequency
endothelial cell 2
fibroblasts 1
VEGFA (Homo sapiens)
Flt1 (Mus musculus)
Pain Link Frequency Relevance Heat
metalloproteinase 5 93.36 High High
Arthritis 8 92.32 High High
Bioavailability 5 84.56 Quite High
antagonist 10 82.44 Quite High
Inflammation 69 79.28 Quite High
cytokine 28 79.20 Quite High
Kinase C 5 70.16 Quite High
rheumatoid arthritis 57 48.32 Quite Low
cINOD 3 40.92 Quite Low
imagery 120 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Death 6 99.16 Very High Very High Very High
Cancer 485 98.48 Very High Very High Very High
Hematological Disease 10 96.20 Very High Very High Very High
Arthritis 8 92.32 High High
Corneal Neovascularization 111 88.84 High High
Metastasis 31 87.92 High High
Stomach Cancer 3 83.68 Quite High
Colon Cancer 18 81.76 Quite High
Disease 27 79.60 Quite High
INFLAMMATION 70 79.28 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
It prevents VEGF-A from ligating to its endothelial receptors, VEGFR-1 and VEGFR-2 [22,23], but does not neutralize other members of the VEGF gene family, such as VEGF-B or VEGF-C [24-26].
VEGF Binding (ligating) of VEGFR-1
1) Confidence 0.34 Published 2009 Journal Molecular Vision Section Body Doc Link PMC2779062 Disease Relevance 0.45 Pain Relevance 0
VEGF exerts its activity by binding to several high-affinity transmembrane endothelial cell receptors, especially VEGFR-1 (Flt-1) and VEGFR-2 (KDR/Flk-1).
VEGF Binding (binding) of VEGFR-1 in endothelial cell
2) Confidence 0.34 Published 2009 Journal Molecular Vision Section Body Doc Link PMC2779062 Disease Relevance 0.34 Pain Relevance 0.04
VEGF exerts its activity by binding to several high-affinity transmembrane endothelial cell receptors, especially VEGFR-1 (Flt-1) and VEGFR-2 (KDR/Flk-1).
VEGF Binding (binding) of Flt-1 in endothelial cell
3) Confidence 0.34 Published 2009 Journal Molecular Vision Section Body Doc Link PMC2779062 Disease Relevance 0.34 Pain Relevance 0.04
The Nrps can also bind to certain heparin binding isofoms of VEGF (e.g., VEGF165) to enhance the binding of VEGF to VEGFR1, and VEGFR2 (Figure 1) [31, 32].
VEGF Binding (binding) of VEGFR1
4) Confidence 0.32 Published 2010 Journal Journal of Oncology Section Body Doc Link PMC2902148 Disease Relevance 0.67 Pain Relevance 0.07
The biological functions of VEGF are mediated upon binding to receptor tyrosine kinases Vascular Endothelial Growth Factor Receptor-1, -2 (VEGFR1, 2).
VEGF Binding (binding) of VEGFR1
5) Confidence 0.32 Published 2010 Journal Journal of Oncology Section Body Doc Link PMC2902148 Disease Relevance 0.29 Pain Relevance 0.09
VEGFR1 binds VEGF with high affinity (KD ~ 10–20?
VEGF Binding (binds) of VEGFR1
6) Confidence 0.32 Published 2010 Journal Journal of Oncology Section Body Doc Link PMC2902148 Disease Relevance 0.25 Pain Relevance 0.07
VEGFR1 binds VEGF, VEGF-B, and PlGF [14, 15].
VEGF Binding (binds) of VEGFR1
7) Confidence 0.25 Published 2010 Journal Journal of Oncology Section Body Doc Link PMC2902148 Disease Relevance 0.24 Pain Relevance 0.08
VEGFR1 binds VEGF, VEGF-B, and PlGF [14, 15].
VEGF Binding (binds) of VEGFR1
8) Confidence 0.25 Published 2010 Journal Journal of Oncology Section Body Doc Link PMC2902148 Disease Relevance 0.24 Pain Relevance 0.08
This peptide selectively binds to Flt-1, and thereby, blocks the interaction between Flt-1 and VEGF or PlGF.
VEGF Binding (interaction) of Flt-1
9) Confidence 0.13 Published 2008 Journal Mediators of Inflammation Section Body Doc Link PMC2638142 Disease Relevance 0.50 Pain Relevance 0.13
Seetharam et al. demonstrated a high binding affinity of VEGFR-1 to VEGF without generating a mitogenic response in transfected NIH3T3 fibroblasts that over-expressed VEGFR-1 [35].
VEGF Binding (affinity) of VEGFR-1 in fibroblasts
10) Confidence 0.02 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2603310 Disease Relevance 0.05 Pain Relevance 0
It is known that the extracellular portion and the soluble fraction of VEGFR-1 have a 10-fold higher affinity for the VEGF ligand with limited or no detectable autophosphorylation activity.
VEGF Binding (affinity) of VEGFR-1
11) Confidence 0.01 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2603310 Disease Relevance 0.06 Pain Relevance 0
Based on this information, excessive expression of VEGFR-1 could result in increased binding to VEGF ligand, resulting in competitive suppression of VEFGR-2 activation and the angiogenic response.
VEGF Binding (binding) of VEGFR-1
12) Confidence 0.01 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2603310 Disease Relevance 0 Pain Relevance 0

General Comments

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