INT173100

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Context Info
Confidence 0.39
First Reported 2003
Last Reported 2011
Negated 1
Speculated 0
Reported most in Body
Documents 39
Total Number 39
Disease Relevance 22.48
Pain Relevance 0.81

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) cytoplasmic membrane-bounded vesicle (KDR) plasma membrane (KDR)
nucleus (KDR) cytoplasm (KDR)
Anatomy Link Frequency
endothelial cells 6
Capan-1 3
plasma 2
liver 2
MIA PaCa-2 2
KDR (Homo sapiens)
KDR - H472Q (3)
Pain Link Frequency Relevance Heat
addiction 27 83.84 Quite High
corticosteroid 5 81.60 Quite High
Inflammation 43 79.60 Quite High
cytokine 98 75.92 Quite High
Chronic pancreatitis 30 72.40 Quite High
dexamethasone 39 61.56 Quite High
cva 31 50.88 Quite High
palliative 3 49.52 Quite Low
dysesthesia 4 37.44 Quite Low
antagonist 33 36.88 Quite Low
Disease Link Frequency Relevance Heat
Hypertension 376 100.00 Very High Very High Very High
Fibromyalgia 13 100.00 Very High Very High Very High
Breast Cancer 58 99.48 Very High Very High Very High
Toxicity 170 99.44 Very High Very High Very High
Malignant Neoplastic Disease 63 99.30 Very High Very High Very High
Cancer 1112 99.20 Very High Very High Very High
Pancreatic Cancer 810 98.92 Very High Very High Very High
Leukemia 109 97.76 Very High Very High Very High
Lymphatic System Cancer 49 97.40 Very High Very High Very High
Age-related Macular Degeneration 117 95.84 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Further, VEGF/VEGFR interactions can stimulate proliferation, migration and survival of leukemia/lymphoma cells by autocrinous and paracrinous loops.
VEGFR Binding (interactions) of associated with leukemia and lymphatic system cancer
1) Confidence 0.39 Published 2010 Journal J Angiogenes Res Section Body Doc Link PMC2902424 Disease Relevance 0.92 Pain Relevance 0.06
VEGFR2 H472Q and V297I genotypes vs. treatment associated toxicities and survival following sorafenib and/or bevacizumab therapy
VEGFR2 H472Q (H472Q) Binding (associated) of
2) Confidence 0.36 Published 2010 Journal J Exp Clin Cancer Res Section Body Doc Link PMC2913951 Disease Relevance 1.34 Pain Relevance 0
To determine whether the aforementioned association between HT and HFSR is confounded by VEGFR2 H472Q, the association between any two of the factors (i.e., HT, HFSR and VEGFR2 H472Q) with stratification by the remaining factor were tested.
VEGFR2 H472Q (H472Q) Binding (association) of associated with hypertension
3) Confidence 0.36 Published 2010 Journal J Exp Clin Cancer Res Section Body Doc Link PMC2913951 Disease Relevance 1.26 Pain Relevance 0
This is not surprising given the association of VEGFR2 variants and toxicity.
VEGFR2 Neg (not) Binding (association) of associated with toxicity
4) Confidence 0.35 Published 2010 Journal J Exp Clin Cancer Res Section Body Doc Link PMC2913951 Disease Relevance 0.92 Pain Relevance 0
HEK293 s cells that were transfected with VEGFR2 V297I SNP had significantly low VEGF binding efficiency regardless of VEGFR2 H472Q genotype, while variant VEGFR2 H472Q allele had minimal effect on VEGF binding efficiency [10].
VEGFR2 H472Q (H472Q) Binding (binding) of
5) Confidence 0.31 Published 2010 Journal J Exp Clin Cancer Res Section Body Doc Link PMC2913951 Disease Relevance 0.64 Pain Relevance 0
VEGF has a key, rate-limiting role in promoting tumor angiogenesis and exerts its effects by binding to one of three tyrosine kinase receptors: VEGF receptor-1 (VEGFR-1; fms-like tyrosine kinase-1, Flt-1), VEGFR-2 (human kinase domain region, KDR/murine fetal liver kinase-1, Flk-1) and VEGFR-3 (Flt-4).
VEGFR Binding (binding) of in liver associated with fibromyalgia and cancer
6) Confidence 0.31 Published 2010 Journal J Angiogenes Res Section Body Doc Link PMC2902424 Disease Relevance 0.44 Pain Relevance 0
VEGF has a key, rate-limiting role in promoting tumor angiogenesis and exerts its effects by binding to one of three tyrosine kinase receptors: VEGF receptor-1 (VEGFR-1; fms-like tyrosine kinase-1, Flt-1), VEGFR-2 (human kinase domain region, KDR/murine fetal liver kinase-1, Flk-1) and VEGFR-3 (Flt-4).
VEGFR Binding (binding) of in liver associated with fibromyalgia and cancer
7) Confidence 0.31 Published 2010 Journal J Angiogenes Res Section Body Doc Link PMC2902424 Disease Relevance 0.44 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
8) Confidence 0.30 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
A second indication was based on the observation that the formation of signaling VEGFR2 complexes was biphasic in the direction of total VEGFR density, allowing the most efficient net “pro-angiogenic potential” to be reached within the order of 10,000 total VEGFR/EC (Fig. 5D).
VEGFR2 Binding (complexes) of
9) Confidence 0.30 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0.04
We showed that the densities and affinities of the interstitial matrix binding sites did not affect steady-state predictions of plasma and interstitial levels of the soluble species, nor VEGFR occupancies.
VEGFR Binding (occupancies) of in plasma
10) Confidence 0.30 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
Sensitivity to VEGFR2?
VEGFR2 Binding (Sensitivity) of
11) Confidence 0.30 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
Among the major endothelial cell surface receptor targets for these VEGF isoforms are: the tyrosine kinases VEGFR1 (Flt-1; UniProt accession P17948-1) and VEGFR2 (mouse Flk-1; human KDR; UniProt accession P35968); as well as the co-receptor neuropilin-1 (NRP1; UniProt accession O14786), which couples directly with VEGFR1, and indirectly with VEGFR2 through non-overlapping binding sites on VEGF165 [7].


VEGFR2 Binding (tyrosine) of in endothelial cell
12) Confidence 0.30 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0.43 Pain Relevance 0.03
Among the major endothelial cell surface receptor targets for these VEGF isoforms are: the tyrosine kinases VEGFR1 (Flt-1; UniProt accession P17948-1) and VEGFR2 (mouse Flk-1; human KDR; UniProt accession P35968); as well as the co-receptor neuropilin-1 (NRP1; UniProt accession O14786), which couples directly with VEGFR1, and indirectly with VEGFR2 through non-overlapping binding sites on VEGF165 [7].


VEGFR2 Binding (tyrosine) of in endothelial cell
13) Confidence 0.30 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0.41 Pain Relevance 0.03
We have previously developed several computational models of the in vivo biochemical interactions between VEGF121, VEGF165, VEGFR1, VEGFR2, NRP1, and the interstitial matrix in skeletal muscle, including: a spatially-averaged single-tissue model of the human vastus lateralis muscle at rest [54]; and several 3D models for predicting spatial molecular gradients and intra-muscular pro-angiogenic treatment outcomes in resting and exercising rat extensor digitorum longus muscle [55]–[58].
VEGFR2 Binding (interactions) of in extensor digitorum longus
14) Confidence 0.30 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0.31 Pain Relevance 0
Blocking the interaction between VEGF and Flk-1/KDR can abolish VEGF induced proliferation.
KDR Binding (interaction) of
15) Confidence 0.30 Published 2007 Journal BMC Nephrol Section Body Doc Link PMC1852096 Disease Relevance 1.02 Pain Relevance 0
Blocking the interaction between VEGF and Flk-1/KDR can abolish VEGF induced proliferation.
Flk-1 Binding (interaction) of
16) Confidence 0.30 Published 2007 Journal BMC Nephrol Section Body Doc Link PMC1852096 Disease Relevance 1.02 Pain Relevance 0
Receptor densities and ratios affected plasma and interstitial concentrations of VEGF and sVEGFR1, as well as surface-bound VEGFR occupancy
VEGFR Binding (occupancy) of in plasma
17) Confidence 0.29 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
Additional studies by this group have confirmed overexpression of VEGF mRNA and protein compared to normal pancreas, and interestingly, have demonstrated the presence of VEGF receptors, VEGFR-1 and VEGFR-2, on both cultured human pancreatic cancer cells (AsPC-1, Capan-1, and MIA PaCa-2) and tissue specimens [82].
VEGFR Binding (presence) of in Capan-1 associated with pancreatic cancer
18) Confidence 0.29 Published 2003 Journal Mol Cancer Section Body Doc Link PMC150383 Disease Relevance 0.90 Pain Relevance 0.05
VEGF-A exerts its effects on target endothelial cells through interactions with its two specific transmembrane tyrosine kinase receptors, VEGFR-1 (Flt-1) and VEGFR-2 (KDR, flk-1) [70].
VEGFR Binding (kinase) of in endothelial cells
19) Confidence 0.29 Published 2003 Journal Mol Cancer Section Body Doc Link PMC150383 Disease Relevance 0.36 Pain Relevance 0.04
VEGF-A exerts its effects on target endothelial cells through interactions with its two specific transmembrane tyrosine kinase receptors, VEGFR-1 (Flt-1) and VEGFR-2 (KDR, flk-1) [70].
VEGFR Binding (kinase) of in endothelial cells
20) Confidence 0.29 Published 2003 Journal Mol Cancer Section Body Doc Link PMC150383 Disease Relevance 0.36 Pain Relevance 0.04

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