INT157769

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Context Info
Confidence 0.47
First Reported 2007
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 8
Total Number 8
Disease Relevance 2.50
Pain Relevance 1.59

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 (LY96) extracellular region (LY96) plasma membrane (LY96)
Anatomy Link Frequency
MD2 6
immune cells 1
internal 1
LY96 (Homo sapiens)
Pain Link Frequency Relevance Heat
antagonist 16 99.74 Very High Very High Very High
Central nervous system 21 97.24 Very High Very High Very High
agonist 70 96.48 Very High Very High Very High
Lasting pain 5 95.36 Very High Very High Very High
Inflammation 133 88.88 High High
Inflammatory response 45 86.68 High High
cytokine 146 84.20 Quite High
chemokine 20 56.24 Quite High
fibrosis 18 51.68 Quite High
headache 3 15.12 Low Low
Disease Link Frequency Relevance Heat
Pain 11 95.36 Very High Very High Very High
Autoimmune Disease 5 95.04 Very High Very High Very High
Sepsis 126 94.68 High High
Disease 33 94.08 High High
INFLAMMATION 180 88.88 High High
Cirrhosis 61 83.76 Quite High
Injury 37 82.44 Quite High
Infection 31 75.56 Quite High
Endotoxemia 12 73.52 Quite High
Bacterial Respiratory Disease 1 66.88 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
We herein report a chemical biology approach by using a rationally designed peptide inhibitor to disrupt the TLR4-MD2 association, thereby blocking TLR4 signaling.
MD2 Binding (association) of in MD2
1) Confidence 0.47 Published 2009 Journal Chembiochem Section Abstract Doc Link 19184989 Disease Relevance 0.28 Pain Relevance 0.27
A peptide antagonist of the TLR4-MD2 interaction.
MD2 Binding (interaction) of in MD2 associated with antagonist
2) Confidence 0.35 Published 2009 Journal Chembiochem Section Title Doc Link 19184989 Disease Relevance 0.26 Pain Relevance 0.28
The binding and activation of LPS to TLR4 needs three additional components: MD2, a membrane protein whose association with TLR4 is required for the binding of LPS [5]; LPS-binding protein (LBP), which extracts LPS monomers from the aggregated form [6,7]; and CD14, which transfers LPS to the TLR4/MD2 transmembrane co-receptor, which then triggers the downstream molecular events [2].
MD2 Binding (association) of in MD2
3) Confidence 0.11 Published 2007 Journal Molecular Vision Section Body Doc Link PMC2768757 Disease Relevance 0.17 Pain Relevance 0.11
Several small molecule inhibitors of TLR4 are currently being tested, including:

(1) Lipid A mimetics (for example, E5564 and CRX-526 [150,151]) which bind to the TLR4-MD2 complex but lack intrinsic activity and thus prevent binding of the lipid A portion of LPS and subsequent TLR4 activation (2) TAK-242, which exerts its inhibitory effects at the intracellular domain of TLR4 [152].

MD2 Binding (bind) of in MD2 associated with agonist
4) Confidence 0.09 Published 2010 Journal Fibrogenesis Tissue Repair Section Body Doc Link PMC2984459 Disease Relevance 0.94 Pain Relevance 0.46
In the case of human TLR 4, two accessory molecules CD14 and MD2 are essential for LPS recognition [2, 7, 8].
MD2 Binding (recognition) of in MD2
5) Confidence 0.07 Published 2010 Journal Mediators of Inflammation Section Body Doc Link PMC2933899 Disease Relevance 0 Pain Relevance 0
While the major signalling pathway of LPS lies within its binding to the MD2/TLR4 complex, several reports have indicated that endotoxin may enter immune cells [48] and localize in the Golgi apparatus and other vesicles [49].
MD2 Binding (binding) of in immune cells
6) Confidence 0.06 Published 2010 Journal Mediators of Inflammation Section Body Doc Link PMC2855078 Disease Relevance 0.35 Pain Relevance 0.12
In the presence of soluble MD2, this protein binds LPS and inhibits LPS-induced TNF?
MD2 Binding (binds) of in MD2
7) Confidence 0.06 Published 2010 Journal Mediators of Inflammation Section Body Doc Link PMC2855078 Disease Relevance 0.23 Pain Relevance 0.10
The crystal structure of the TLR4-MD2 complex with bound eritoran was recently described, suggesting that eritoran mechanism of action lies within its binding in a large hydrophobic internal pocket in MD2 [31].
MD2 Binding (binding) of in internal
8) Confidence 0.05 Published 2010 Journal Mediators of Inflammation Section Body Doc Link PMC2855078 Disease Relevance 0.26 Pain Relevance 0.26

General Comments

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