INT175280

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Context Info
Confidence 0.08
First Reported 2003
Last Reported 2010
Negated 0
Speculated 1
Reported most in Body
Documents 19
Total Number 22
Disease Relevance 6.37
Pain Relevance 0.98

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

mitochondrion (DBT) small molecule metabolic process (DBT) transferase activity, transferring acyl groups (DBT)
cellular nitrogen compound metabolic process (DBT) cytoplasm (DBT)
Anatomy Link Frequency
covering 1
spike 1
endometrium 1
DBT (Homo sapiens)
Pain Link Frequency Relevance Heat
antagonist 65 99.74 Very High Very High Very High
Eae 9 97.68 Very High Very High Very High
GABA receptor 2 96.84 Very High Very High Very High
Opioid 9 95.96 Very High Very High Very High
GABAergic 12 94.60 High High
Dopamine 46 94.00 High High
Kinase C 24 91.56 High High
agonist 120 91.28 High High
Inflammatory response 5 90.24 High High
cocaine 8 85.92 High High
Disease Link Frequency Relevance Heat
Togavirus Infection 766 99.96 Very High Very High Very High
Targeted Disruption 13 98.72 Very High Very High Very High
Anxiety Disorder 18 98.56 Very High Very High Very High
Aging 3 97.32 Very High Very High Very High
Hepatitis 31 96.80 Very High Very High Very High
Death 35 95.20 Very High Very High Very High
Apoptosis 33 91.12 High High
Disease 93 90.32 High High
INFLAMMATION 24 90.24 High High
Cancer 40 89.56 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
A recombinant mutant of E2, p239 (ORF2 aa368–606), forms particles of diameter 23 nm, presumably via dimeric interactions [6],[9].
E2 Binding (interactions) of
1) Confidence 0.08 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2714988 Disease Relevance 0.14 Pain Relevance 0
The recognition by these mAb is totally lost with the dissociation of the dimeric form of E2 into its monomeric form.
E2 Binding (recognition) of
2) Confidence 0.08 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2714988 Disease Relevance 0.05 Pain Relevance 0
E2s is the shortest among all constructs of E2 (Figure 5) that can dimerize and recognize HEV antibodies, in a way similar to other E2 constructs, as well as the native HEV [8].
E2 Binding (recognize) of
3) Confidence 0.07 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2714988 Disease Relevance 0.09 Pain Relevance 0
The mitochondrial-enriched subfraction represented an important source of E2 binding, where the steroid was recognized in a stereospecific and high affinity manner.
E2 Binding (binding) of
4) Confidence 0.07 Published 2005 Journal Reprod Biol Endocrinol Section Body Doc Link PMC1266397 Disease Relevance 0.11 Pain Relevance 0
Neutralizing antibodies such as 8C11 and 8H3 bind with native HEV [8], as well as with the dimeric form of E2 constructs [6],[19].
E2 Binding (bind) of
5) Confidence 0.07 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2714988 Disease Relevance 0.26 Pain Relevance 0
Unlike E2, which binds to both ER subtypes with relatively equal affinity, some phytoestrogens bind with higher affinity to ER?
E2 Binding (binds) of
6) Confidence 0.05 Published 2010 Journal International Journal of Women's Health Section Body Doc Link PMC2971739 Disease Relevance 0.57 Pain Relevance 0
Second, the stimulatory effects of E2 on [Ca2+]i oscillations were blocked by tamoxifen (data not shown), which competes with E2 for binding to ER?
E2 Binding (binding) of
7) Confidence 0.05 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2910705 Disease Relevance 0.15 Pain Relevance 0.24
Phytoestrogens have been implicated in memory and learning,196,200 and can have anxiolytic effects.200–202 Some phytoestrogenic compounds can also antagonize the effects of E2; for example, while coumestrol by itself does not affect locomotor activity, it can antagonize the effects of E2.203 Besides its higher affinity for ER?
E2 Binding (effects) of associated with eae and anxiety disorder
8) Confidence 0.04 Published 2010 Journal International Journal of Women's Health Section Body Doc Link PMC2971739 Disease Relevance 0.10 Pain Relevance 0.11
When a correlation analysis between E2 or P4 and the interpubic distance was done, a positive temporal association was observed only with E2 serum levels (r = 0.6678; p < 0.01).


E2 Binding (association) of
9) Confidence 0.04 Published 2003 Journal Reprod Biol Endocrinol Section Body Doc Link PMC305330 Disease Relevance 0.22 Pain Relevance 0.08
The synthetic nonsteroidal compound, STX binds to Gq-mER and mimics the action of E2 in ER?
E2 Binding (action) of
10) Confidence 0.04 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2910705 Disease Relevance 0.19 Pain Relevance 0.28
Unlike E2, which binds to both ER subtypes with relatively equal affinity, some phytoestrogens bind with higher affinity to ER?
E2 Binding (bind) of
11) Confidence 0.04 Published 2010 Journal International Journal of Women's Health Section Body Doc Link PMC2971739 Disease Relevance 0.57 Pain Relevance 0.03
The E1 spike protein drives the fusion process, and E2 interacts with cellular receptors [14,15].
E2 Binding (interacts) of in spike
12) Confidence 0.03 Published 2007 Journal PLoS Pathogens Section Body Doc Link PMC1904475 Disease Relevance 0.38 Pain Relevance 0
Neutralization of these variants was also evaluated with the humanized Hy4 IgG which is known to bind to the mE2c epitope (E2 aa182) [36].
E2 Binding (bind) of
13) Confidence 0.03 Published 2010 Journal PLoS Neglected Tropical Diseases Section Body Doc Link PMC2903468 Disease Relevance 0.44 Pain Relevance 0
The VEEV envelope contains two glycoproteins E1 (mediates cell membrane fusion) and E2 (binds receptor and elicits virus neutralizing antibodies).
E2 Binding (binds) of associated with togavirus infection
14) Confidence 0.03 Published 2010 Journal PLoS Neglected Tropical Diseases Section Abstract Doc Link PMC2903468 Disease Relevance 0.50 Pain Relevance 0
Blocking with two E2-specific, non-neutralizing MAbs (F2 and H6) did not have the desired effect of increasing the isolation of neutralizing Fabs; instead this blocking seemed to have inhibited binding of E2-specific Fabs since only E1-specific Fabs were isolated.
E2 Spec (seemed) Binding (binding) of
15) Confidence 0.03 Published 2010 Journal PLoS Neglected Tropical Diseases Section Body Doc Link PMC2903468 Disease Relevance 0.07 Pain Relevance 0
Six E2 epitopes (E2c,d,e,f,g,h) bound VEEV-neutralizing antibody and mapped to amino acids (aa) 182–207.
E2 Binding (bound) of associated with togavirus infection
16) Confidence 0.03 Published 2010 Journal PLoS Neglected Tropical Diseases Section Abstract Doc Link PMC2903468 Disease Relevance 0.58 Pain Relevance 0
Membrane strips were incubated with the purified hMAbs and hFabs as well as protein E1- and E2-specific mMAbs for 2 h at room temperature, followed by incubation with either AP-conjugated goat anti-human IgG F(ab?)
E2 Binding (conjugated) of
17) Confidence 0.03 Published 2010 Journal PLoS Neglected Tropical Diseases Section Body Doc Link PMC2903468 Disease Relevance 0.26 Pain Relevance 0
While progesterone is an effective anti-estrogen, its role is to reduce ER-alpha concentration rather than to act as a competetive inhibitor of E2 binding, thereby rendering the endometrium resistant to estrogen during the window of implantation.
E2 Binding (binding) of in endometrium
18) Confidence 0.03 Published 2006 Journal Reprod Biol Endocrinol Section Body Doc Link PMC1679803 Disease Relevance 0 Pain Relevance 0
It was proposed that these E2 residues that formed an alternative neutralization site could be folded to form a binding site with the surface dimensions of approximately 600–750 Å, measurements similar to those determined for the interaction of lysozyme–anti-lysozyme immune complexes [69].
E2 Binding (binding) of
19) Confidence 0.03 Published 2010 Journal PLoS Neglected Tropical Diseases Section Body Doc Link PMC2903468 Disease Relevance 0.39 Pain Relevance 0
The effects of both E2 and testosterone were reversed by ICI-182,780, a selective estrogen antagonist, suggesting interactions with the cell-surface E2 receptors.
E2 Binding (interactions) of associated with antagonist
20) Confidence 0.02 Published 2006 Journal Journal of Biomedicine and Biotechnology Section Body Doc Link PMC1510947 Disease Relevance 1.05 Pain Relevance 0.24

General Comments

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