INT196158

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Context Info
Confidence 0.06
First Reported 2006
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 16
Total Number 17
Disease Relevance 7.03
Pain Relevance 1.73

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

cell differentiation (NRP2) cell adhesion (NRP2) plasma membrane (NRP2)
Anatomy Link Frequency
blood vessels 2
plasma 1
NRP2 (Homo sapiens)
Pain Link Frequency Relevance Heat
rheumatoid arthritis 180 99.96 Very High Very High Very High
metalloproteinase 1 99.00 Very High Very High Very High
Inflammation 93 95.48 Very High Very High Very High
Inflammatory mediators 7 94.56 High High
Bioavailability 1 90.20 High High
Osteoarthritis 9 89.84 High High
cytokine 24 82.76 Quite High
Arthritis 24 66.36 Quite High
chemokine 16 51.68 Quite High
antagonist 16 50.48 Quite High
Disease Link Frequency Relevance Heat
Rheumatoid Arthritis 183 99.96 Very High Very High Very High
Cancer 235 99.24 Very High Very High Very High
Fibromyalgia 3 98.48 Very High Very High Very High
INFLAMMATION 105 95.48 Very High Very High Very High
Coronary Heart Disease 2 93.72 High High
Shock 51 93.28 High High
Hyperplasia 18 92.84 High High
Osteoarthritis 9 89.84 High High
Apoptosis 13 83.20 Quite High
Chronic Sinusitis 110 83.12 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
While this may be indeed the case, our data suggests that the degree of histological changes is not associated with NP1 and NP2, following endoscopic observations.
NP2 Binding (associated) of
1) Confidence 0.06 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2832699 Disease Relevance 0.52 Pain Relevance 0.16
Along similar lines, there was no significant difference in the overall quantity of se detected in NP1 and NP2 patients groups.
NP2 Binding (groups) of
2) Confidence 0.04 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2832699 Disease Relevance 0.36 Pain Relevance 0.16
This isoform binds to VEGF-R2 with the same affinity as VEGF165, but does not activate downstream signaling pathways.17 Mice engineered to express only VEGF121, die within the first 2 weeks of life secondary to ischemic cardiomyopathy and failure of myocardial angiogenesis.19,20 In mice lacking VEGF165, severe defects in developing blood vessels are seen.
VEGF165 Binding (binds) of in blood vessels associated with coronary heart disease
3) Confidence 0.01 Published 2010 Journal Cancer management and research Section Body Doc Link PMC3004565 Disease Relevance 0.52 Pain Relevance 0
Specifically, VEGF145, the major tumor-associated isoform, will inhibit the binding of VEGF165 to the KDR/FLK1 receptor.24 Additionally, VEGF regulates the permeability of blood vessels,25 in a dose dependent manner.
VEGF165 Binding (binding) of in blood vessels associated with cancer
4) Confidence 0.01 Published 2010 Journal Cancer management and research Section Body Doc Link PMC3004565 Disease Relevance 0.66 Pain Relevance 0
VEGF165 is the predominantly active isoform that can be found both circulating in plasma and bound to ECM [12].
VEGF165 Binding (bound) of in plasma
5) Confidence 0.01 Published 2010 Journal Journal of Oncology Section Body Doc Link PMC2902148 Disease Relevance 0.28 Pain Relevance 0.09
VEGF165 exerts its biological effects by binding with its receptor subtypes, that is, fms-like tyrosine kinase (Flt-1), kinase insert domain-containing receptor (KDR) and neuropilin-1 (NP-1) [3].
VEGF165 Binding (binding) of associated with fibromyalgia
6) Confidence 0.01 Published 2008 Journal Mediators of Inflammation Section Body Doc Link PMC2638142 Disease Relevance 1.15 Pain Relevance 0.34
Second, via interaction with Flt-1, VEGF165 may directly stimulate the productions of cytochemokines, such as TNF-?
VEGF165 Binding (interaction) of
7) Confidence 0.01 Published 2008 Journal Mediators of Inflammation Section Body Doc Link PMC2638142 Disease Relevance 1.30 Pain Relevance 0.53
Through the screening of positional scanning synthetic peptide libraries, we identified a soluble arginine-rich hexapeptide sequence, RRKRRR (Arg-Arg-Lys-Arg-Arg-Arg), which binds to VEGF165, and thereby prevents it from interacting with its receptor [14].
VEGF165 Binding (binds) of
8) Confidence 0.01 Published 2008 Journal Mediators of Inflammation Section Body Doc Link PMC2638142 Disease Relevance 1.18 Pain Relevance 0.42
The degree of interaction among semaphorins is also poorly understood.
semaphorins Binding (interaction) of
9) Confidence 0.01 Published 2006 Journal Genome Biol Section Body Doc Link PMC1557745 Disease Relevance 0.05 Pain Relevance 0.03
Interestingly, plexins also contain sema domains, albeit highly divergent, that are important for binding to semaphorins [8].
semaphorins Binding (binding) of
10) Confidence 0.00 Published 2006 Journal Genome Biol Section Body Doc Link PMC1557745 Disease Relevance 0.06 Pain Relevance 0
Several other proteins have also been identified that bind to the extracellular portions of semaphorins (Figure 3).
semaphorins Binding (bind) of
11) Confidence 0.00 Published 2006 Journal Genome Biol Section Body Doc Link PMC1557745 Disease Relevance 0.06 Pain Relevance 0
All classes of semaphorins except class 2 have been found to bind directly to members of the plexin (Plex) family of transmembrane receptors (reviewed in [41]; see Table 2 for a summary of the receptors and signaling proteins associated with semaphorins and Figure 3 for the primary structure of known semaphorin receptors).
semaphorins Binding (bind) of
12) Confidence 0.00 Published 2006 Journal Genome Biol Section Body Doc Link PMC1557745 Disease Relevance 0.20 Pain Relevance 0
These effects occur primarily through binding of semaphorins to their receptors, although transmembrane semaphorins also serve as receptors themselves.
semaphorins Binding (binding) of
13) Confidence 0.00 Published 2006 Journal Genome Biol Section Abstract Doc Link PMC1557745 Disease Relevance 0.11 Pain Relevance 0
Interestingly, neuropilins also bind plexins, such that class 3 semaphorins, which bind to neuropilins, signal their effects through the cytoplasmic domain of plexins.
semaphorins Binding (bind) of
14) Confidence 0.00 Published 2006 Journal Genome Biol Section Body Doc Link PMC1557745 Disease Relevance 0 Pain Relevance 0
Transmembrane semaphorins also form disulfide-linked dimers and depend on oligomerization for at least some of their functional effects [5,11,16,36,38-40].


semaphorins Binding (oligomerization) of
15) Confidence 0.00 Published 2006 Journal Genome Biol Section Body Doc Link PMC1557745 Disease Relevance 0.24 Pain Relevance 0
These effects occur primarily through binding of semaphorins to their receptors, although transmembrane semaphorins also serve as receptors themselves.
semaphorins Binding (binding) of
16) Confidence 0.00 Published 2006 Journal Genome Biol Section Abstract Doc Link PMC1557745 Disease Relevance 0.11 Pain Relevance 0
Semaphorins exert the majority of their effects by serving as ligands and binding to other proteins through their extracellular domains.
Semaphorins Binding (binding) of
17) Confidence 0.00 Published 2006 Journal Genome Biol Section Body Doc Link PMC1557745 Disease Relevance 0.22 Pain Relevance 0

General Comments

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