INT354204

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Context Info
Confidence 0.32
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 11
Disease Relevance 4.44
Pain Relevance 2.49

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

extracellular space (Igfbp7) extracellular region (Igfbp7) cell adhesion (Igfbp7)
Igfbp7 (Mus musculus)
Pain Link Frequency Relevance Heat
Inflammation 187 99.40 Very High Very High Very High
Pain 143 99.20 Very High Very High Very High
addiction 11 99.16 Very High Very High Very High
Glutamate 11 94.08 High High
ASIC 165 85.44 High High
agonist 22 83.92 Quite High
ischemia 44 83.04 Quite High
Potency 11 81.56 Quite High
Glutamate receptor 11 76.88 Quite High
IPN 77 68.84 Quite High
Disease Link Frequency Relevance Heat
INFLAMMATION 209 99.40 Very High Very High Very High
Aids-related Complex 88 99.40 Very High Very High Very High
Pain 132 99.20 Very High Very High Very High
Acidosis 154 97.80 Very High Very High Very High
Cancer 22 96.16 Very High Very High Very High
Injury 33 95.68 Very High Very High Very High
Infection 33 95.36 Very High Very High Very High
Cv Unclassified Under Development 22 83.04 Quite High
Inflammatory Pain 77 68.84 Quite High
Coronary Artery Disease 22 39.52 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Interestingly, AGM evokes ASIC3-dependent pain-behavior in mice [10], suggesting that AGM-ASIC3 interaction may become functionally relevant under pathological conditions.


AGM Binding (interaction) of associated with pain
1) Confidence 0.32 Published 2010 Journal Mol Pain Section Body Doc Link PMC3017031 Disease Relevance 0.86 Pain Relevance 0.40
Among these, AGM and polyamines (including spermine, spermidine, and putrescine) are positively charged at physiological pH and thus can interact electrostatically with negatively charged nucleic acids and proteins, including receptors and ion channels.
AGM Binding (interact) of
2) Confidence 0.28 Published 2010 Journal Mol Pain Section Body Doc Link PMC3017031 Disease Relevance 0.07 Pain Relevance 0.27
To address this issue, we explored the interaction between AGM and pH 7.0 more specifically (Figure 2D-F).
AGM Binding (interaction) of
3) Confidence 0.28 Published 2010 Journal Mol Pain Section Body Doc Link PMC3017031 Disease Relevance 0.69 Pain Relevance 0.28
To understand the functional relevance of AGM-ASIC3 interaction, we examined the pH dependence of AGM action by applying graded pH to the CHO cell expressing ASIC3 channels, in the presence or absence of AGM (Figure 2A).
AGM Binding (interaction) of associated with addiction
4) Confidence 0.28 Published 2010 Journal Mol Pain Section Body Doc Link PMC3017031 Disease Relevance 0.83 Pain Relevance 0.31
For comparison, we tested 2-aminoethyl-methanethiosulfonate (MTSEA), a linear thiol-reactive compound on ASIC3E79C channels, in which the residue Glu79 was replaced by a cysteine, thus mimicking AGM-E79 interaction (Figure 6A).
AGM-E79 Binding (interaction) of
5) Confidence 0.28 Published 2010 Journal Mol Pain Section Body Doc Link PMC3017031 Disease Relevance 0 Pain Relevance 0
The extracellular Ca2+ concentration can decrease from a resting value of around 1.2-1.8 mM to values as low as 0.08 mM under certain conditions [38], suggesting that the signaling cascade induced by AGM-ASIC3 interaction might be markedly amplified under such conditions.
AGM Binding (interaction) of
6) Confidence 0.24 Published 2010 Journal Mol Pain Section Body Doc Link PMC3017031 Disease Relevance 0.27 Pain Relevance 0.11
Thus, similar to GMQ [10], AGM-ASIC3 interaction is highly sensitive to altered extracellular Ca2+.
AGM Binding (interaction) of
7) Confidence 0.24 Published 2010 Journal Mol Pain Section Body Doc Link PMC3017031 Disease Relevance 0.20 Pain Relevance 0.10
AGM-induced ASIC3 channel activation was not through the chelation of extracellular Ca2+ as occurs with increased lactate, but rather through a direct interaction with the newly identified nonproton ligand sensing domain.
AGM-induced Binding (interaction) of
8) Confidence 0.21 Published 2010 Journal Mol Pain Section Abstract Doc Link PMC3017031 Disease Relevance 0.50 Pain Relevance 0.27
For example, extracellular AGM binds to imidazoline receptors [12,13], and blocks N-methyl-D-aspartate (NMDA) receptors [14] and other ligand- or voltage-gated cation channels [15-17].
AGM Binding (binds) of
9) Confidence 0.21 Published 2010 Journal Mol Pain Section Body Doc Link PMC3017031 Disease Relevance 0.06 Pain Relevance 0.24
In this study, we extended the previous finding that ASIC3 can be activated by small molecules with basic groups such as GMQ, AGM, and ARC by uncovering the functional interactions of AGM with multiple inflammatory factors such as hyperosmolarity, arachidonic acid, and lactate.
AGM Binding (interactions) of associated with inflammation and aids-related complex
10) Confidence 0.21 Published 2010 Journal Mol Pain Section Body Doc Link PMC3017031 Disease Relevance 0.47 Pain Relevance 0.24
Cysteine modification with a linear thiol-reactive compound that mimics AGM binding induces ASIC3 opening in a sustained manner similar to AGM, supporting the critical role of the newly identified nonproton ligand sensing domain.
AGM Binding (binding) of
11) Confidence 0.21 Published 2010 Journal Mol Pain Section Body Doc Link PMC3017031 Disease Relevance 0.49 Pain Relevance 0.27

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