INT162725

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Context Info
Confidence 0.42
First Reported 2008
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 13
Total Number 13
Disease Relevance 8.86
Pain Relevance 1.79

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

cytoplasmic membrane-bounded vesicle (Kdr) plasma membrane (Kdr) nucleus (Kdr)
cytoplasm (Kdr)
Anatomy Link Frequency
endothelial cells 3
plasma 1
retina 1
Kdr (Rattus norvegicus)
Pain Link Frequency Relevance Heat
endometriosis 276 93.64 High High
cytokine 25 88.88 High High
Intracerebroventricular 1 88.40 High High
ischemia 12 87.92 High High
Inflammation 5 82.60 Quite High
metalloproteinase 14 50.00 Quite Low
nMDA receptor 9 50.00 Quite Low
Angina 3 50.00 Quite Low
imagery 14 22.16 Low Low
agonist 4 20.64 Low Low
Disease Link Frequency Relevance Heat
Hypoxia 156 100.00 Very High Very High Very High
Diabetes Mellitus 261 99.50 Very High Very High Very High
Disease 44 98.64 Very High Very High Very High
Myocardial Infarction 69 96.48 Very High Very High Very High
Targeted Disruption 4 95.52 Very High Very High Very High
Endometriosis 396 93.64 High High
Cancer 102 91.56 High High
Apoptosis 33 91.36 High High
Cv General 4 Under Development 2 87.92 High High
INFLAMMATION 5 82.60 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Its activity depends on its binding to different receptors, such as VEGFR-2 (Flk-1).
VEGFR-2 Binding (binding) of
1) Confidence 0.42 Published 2010 Journal J Exp Clin Cancer Res Section Body Doc Link PMC2826344 Disease Relevance 1.00 Pain Relevance 0.40
Its activity depends on its binding to different receptors, such as VEGFR-2 (Flk-1).
Flk-1 Binding (binding) of
2) Confidence 0.42 Published 2010 Journal J Exp Clin Cancer Res Section Body Doc Link PMC2826344 Disease Relevance 1.00 Pain Relevance 0.40
FLT-1 on endothelial cells may function as a negative regulator of FLK-1, acting as a so-called “decoy” receptor that regulates the activity of VEGFs on vascular endothelium by sequestering VEGF-A and thus rendering it less available to bind to FLK-1 (27).
FLK-1 Binding (bind) of in endothelial cells
3) Confidence 0.42 Published 2008 Journal Diabetes Section Body Doc Link PMC2836241 Disease Relevance 0.36 Pain Relevance 0
It is speculated that triggering of FLT-1 induces weak or undetectable ligand-dependent tyrosine phosphorylation in porcine aortic endothelial cells, whereas FLK-1 binding induces a strong response (28).
FLK-1 Binding (binding) of in endothelial cells
4) Confidence 0.42 Published 2008 Journal Diabetes Section Body Doc Link PMC2836241 Disease Relevance 0.45 Pain Relevance 0
Its activity depends on its binding to different receptors, such as VEGFR-2 (Flk-1).
VEGFR-2 Binding (receptors) of
5) Confidence 0.33 Published 2010 Journal J Exp Clin Cancer Res Section Body Doc Link PMC2826344 Disease Relevance 0.99 Pain Relevance 0.39
Its activity depends on its binding to different receptors, such as VEGFR-2 (Flk-1).
Flk-1 Binding (receptors) of
6) Confidence 0.33 Published 2010 Journal J Exp Clin Cancer Res Section Body Doc Link PMC2826344 Disease Relevance 0.99 Pain Relevance 0.39
Furthermore, VEGF-A mutants that bind selectively to FLK-1 are able to induce mitogenesis and chemotaxis in endothelial cells, and vascular permeability and angiogenesis in vivo, whereas VEGF-A mutants that selectively bind to FLT-1 do not have the activities stated above (29,30).
FLK-1 Binding (bind) of in endothelial cells
7) Confidence 0.31 Published 2008 Journal Diabetes Section Body Doc Link PMC2836241 Disease Relevance 0.56 Pain Relevance 0
Our results confirmed and extended previous observations that genes associated with hypoxia (specifically VEGF, Flk-1, and EPO) are indeed elevated following hypoxia in the retina.
Flk-1 Binding (associated) of in retina associated with hypoxia
8) Confidence 0.21 Published 2009 Journal Molecular Vision Section Body Doc Link PMC2635851 Disease Relevance 1.25 Pain Relevance 0.03
VEGF-A binds both VEGFR-1 and VEGFR-2, while PlGF and VEGF-B interact only with VEGFR-1.
VEGFR-2 Binding (binds) of
9) Confidence 0.21 Published 2010 Journal Acta Histochemica et Cytochemica Section Body Doc Link PMC2875861 Disease Relevance 0.37 Pain Relevance 0
VEGF-C and VEGF-D bind VEGFR-2 and VEGFR-3.
VEGFR-2 Binding (bind) of
10) Confidence 0.21 Published 2010 Journal Acta Histochemica et Cytochemica Section Body Doc Link PMC2875861 Disease Relevance 0.30 Pain Relevance 0
The impairment of myocardial angiogenesis in a diabetic condition has also been associated with compromised signaling mechanisms through the receptors, Flk-1 for VEGF and Tie-2 for Ang-1 (6,28,29).
Flk-1 Binding (associated) of associated with diabetes mellitus
11) Confidence 0.09 Published 2010 Journal Diabetes Section Body Doc Link PMC2797944 Disease Relevance 1.17 Pain Relevance 0.04
RESULTS: A synergistic interaction (P = 0.015) between decreased CD34+/KDR+ cell counts and increased plasma ADMA, but not symmetrical dimethyl-L-arginine, was the sole significant multivariate DeltaeGFR predictor irrespective of baseline eGFR.
KDR Binding (interaction) of in plasma
12) Confidence 0.04 Published 2010 Journal Nephrol. Dial. Transplant. Section Body Doc Link 19729464 Disease Relevance 0.15 Pain Relevance 0
VEGF is one of the signaling molecules that binds to its receptors on cell membrane, VEGFR1 and VEGFR2, initiating signaling pathways through Akt activation.
VEGFR2 Binding (binds) of
13) Confidence 0.01 Published 2010 Journal BMC Neurol Section Body Doc Link PMC3020671 Disease Relevance 0.26 Pain Relevance 0.13

General Comments

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