INT173059

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Context Info
Confidence 0.43
First Reported 2003
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 43
Total Number 44
Disease Relevance 29.63
Pain Relevance 1.10

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

cytoplasm (KDR, VEGFA) extracellular region (KDR, VEGFA) extracellular space (VEGFA)
growth (VEGFA) proteinaceous extracellular matrix (VEGFA) nucleus (KDR)
Anatomy Link Frequency
endothelial cells 9
Capan-1 3
endothelium 2
vascular endothelium 1
KDR (Homo sapiens)
VEGFA (Homo sapiens)
KDR - H472Q (1)
Pain Link Frequency Relevance Heat
addiction 24 85.84 High High
Bioavailability 1 79.60 Quite High
cva 17 78.28 Quite High
Central nervous system 17 77.84 Quite High
Chronic pancreatitis 22 74.64 Quite High
headache 8 74.04 Quite High
abdominal pain 1 73.64 Quite High
Pain 22 71.04 Quite High
cytokine 92 70.96 Quite High
corticosteroid 10 68.48 Quite High
Disease Link Frequency Relevance Heat
Malignant Neoplastic Disease 94 99.40 Very High Very High Very High
Pancreatic Cancer 1121 98.88 Very High Very High Very High
Apoptosis 86 98.80 Very High Very High Very High
Cancer 1570 97.84 Very High Very High Very High
Leukemia 211 97.76 Very High Very High Very High
Hematologic Neoplasms 84 97.52 Very High Very High Very High
Lymphatic System Cancer 108 97.40 Very High Very High Very High
Carcinoma 36 96.80 Very High Very High Very High
Colon Cancer 74 96.72 Very High Very High Very High
Infection 5 95.44 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
VEGF affinity of VEGFR1 and VEGFR2 varied from Kd?
VEGFR2 Binding (affinity) of VEGF
1) Confidence 0.43 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
Thus, multiple studies demonstrate the presence of VEGF-A and VEGFRs in malignant pancreatic ductal cells, and VEGF-VEGFR interactions appear to be mitogenic for pancreatic cancer cells.
VEGFR Binding (interactions) of VEGF associated with malignant neoplastic disease and pancreatic cancer
2) Confidence 0.37 Published 2003 Journal Mol Cancer Section Body Doc Link PMC150383 Disease Relevance 1.58 Pain Relevance 0.04
Existing evidence indicates that neuropilin-1 acts as a coreceptor which enhances the activity of VEGFR-2 upon binding to VEGF-A165, leading to increased endothelial cell migration [73].
VEGFR Binding (binding) of VEGF-A165 in endothelial cell
3) Confidence 0.37 Published 2003 Journal Mol Cancer Section Body Doc Link PMC150383 Disease Relevance 0.35 Pain Relevance 0
Functional receptor binding studies by this group confirmed high levels of VEGF-VEGFR interaction only in Capan-1 cells; VEGF dose-dependently enhanced proliferation, promoted MAPK phosphorylation, and induced c-fos activity only in these Capan-1 cells [82].
VEGFR Binding (interaction) of VEGF in Capan-1
4) Confidence 0.37 Published 2003 Journal Mol Cancer Section Body Doc Link PMC150383 Disease Relevance 0.74 Pain Relevance 0.07
VEGFR-3, largely restricted to lymphatic endothelial cells, binds the VEGF homologues VEGF-C and VEGF-D and may play an important role in the regulation of lymphangiogenesis.
VEGFR Binding (binds) of VEGF in endothelial cells
5) Confidence 0.34 Published 2010 Journal J Angiogenes Res Section Body Doc Link PMC2902424 Disease Relevance 0.37 Pain Relevance 0
VEGFR-3, largely restricted to lymphatic endothelial cells, binds the VEGF homologues VEGF-C and VEGF-D and may play an important role in the regulation of lymphangiogenesis.
VEGFR Binding (binds) of VEGF in endothelial cells
6) Confidence 0.34 Published 2010 Journal J Angiogenes Res Section Body Doc Link PMC2902424 Disease Relevance 0.38 Pain Relevance 0
VEGFR-3, largely restricted to lymphatic endothelial cells, binds the VEGF homologues VEGF-C and VEGF-D and may play an important role in the regulation of lymphangiogenesis.
VEGFR Binding (binds) of VEGF in endothelial cells
7) Confidence 0.34 Published 2010 Journal J Angiogenes Res Section Body Doc Link PMC2902424 Disease Relevance 0.37 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 VEGF
8) Confidence 0.33 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0.04
Thus far we have used the cell surface densities of VEGF-VEGFR complexes as surrogate markers for “angiogenic signaling potential” [158]; however, there is increasing experimental information on intracellular VEGF signaling, whose contribution can only be assessed with detailed model extensions to keep track of endosomal and caveolar populations of internalized complexes, as well as VEGF-regulated sorting towards degradation, nuclear translocation, or recycling back to the cell surface [159], [160].
VEGFR Binding (complexes) of VEGF
9) Confidence 0.33 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
Thus far we have used the cell surface densities of VEGF-VEGFR complexes as surrogate markers for “angiogenic signaling potential” [158]; however, there is increasing experimental information on intracellular VEGF signaling, whose contribution can only be assessed with detailed model extensions to keep track of endosomal and caveolar populations of internalized complexes, as well as VEGF-regulated sorting towards degradation, nuclear translocation, or recycling back to the cell surface [159], [160].
VEGFR Binding (complexes) of VEGF
10) Confidence 0.33 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
As for the soluble species, total free VEGF in all compartments decreased with increasing VEGF-binding affinity of either VEGFR1 or VEGFR2 – presumably through enhanced internalization of complexed VEGF (Fig. 6B).
VEGFR2 Binding (affinity) of VEGF-binding
11) Confidence 0.33 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
Further, VEGF/VEGFR interactions can stimulate proliferation, migration and survival of leukemia/lymphoma cells by autocrinous and paracrinous loops.
VEGFR Binding (interactions) of VEGF associated with leukemia and lymphatic system cancer
12) Confidence 0.33 Published 2010 Journal J Angiogenes Res Section Body Doc Link PMC2902424 Disease Relevance 0.92 Pain Relevance 0.06
Anti-angiogenic therapies are mostly based on inhibiting the binding of VEGF to VEGFR by neutralizing antibodies to the ligand or to the receptor, soluble receptors, small molecule inhibitors or are directed against the tyrosine kinase activity of the VEGF receptors (Figure 1).
VEGFR Binding (binding) of VEGF
13) Confidence 0.33 Published 2010 Journal J Angiogenes Res Section Body Doc Link PMC2902424 Disease Relevance 1.68 Pain Relevance 0
Further, VEGF/VEGFR interactions can stimulate proliferation, migration and survival of leukemia/lymphoma cells by autocrinous and paracrinous loops.
VEGFR Binding (interactions) of VEGF associated with leukemia and lymphatic system cancer
14) Confidence 0.33 Published 2010 Journal J Angiogenes Res Section Body Doc Link PMC2902424 Disease Relevance 0.92 Pain Relevance 0.06
2% about controls), with negligible effects on VEGF-VEGFR complex formation; while free sVEGFR1 varied up to 2.5 pM (?
VEGFR Binding (formation) of VEGF
15) Confidence 0.32 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
As for the soluble species, total free VEGF in all compartments decreased with increasing VEGF-binding affinity of either VEGFR1 or VEGFR2 – presumably through enhanced internalization of complexed VEGF (Fig. 6B).
VEGFR2 Binding (affinity) of VEGF
16) Confidence 0.32 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
2% about controls), with negligible effects on VEGF-VEGFR complex formation; while free sVEGFR1 varied up to 2.5 pM (?
VEGFR Binding (formation) of VEGF
17) Confidence 0.32 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
Blocking the interaction between VEGF and Flk-1/KDR can abolish VEGF induced proliferation.
Flk-1 Binding (interaction) of VEGF
18) Confidence 0.32 Published 2007 Journal BMC Nephrol Section Body Doc Link PMC1852096 Disease Relevance 1.02 Pain Relevance 0
Functional receptor binding studies by this group confirmed high levels of VEGF-VEGFR interaction only in Capan-1 cells; VEGF dose-dependently enhanced proliferation, promoted MAPK phosphorylation, and induced c-fos activity only in these Capan-1 cells [82].
VEGFR Binding (interaction) of VEGF in Capan-1
19) Confidence 0.28 Published 2003 Journal Mol Cancer Section Body Doc Link PMC150383 Disease Relevance 0.69 Pain Relevance 0.07
Functional receptor binding studies by this group confirmed high levels of VEGF-VEGFR interaction only in Capan-1 cells; VEGF dose-dependently enhanced proliferation, promoted MAPK phosphorylation, and induced c-fos activity only in these Capan-1 cells [82].
VEGFR Binding (interaction) of VEGF in Capan-1
20) Confidence 0.27 Published 2003 Journal Mol Cancer Section Body Doc Link PMC150383 Disease Relevance 0.74 Pain Relevance 0.07

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