INT157767

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Context Info
Confidence 0.54
First Reported 2007
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 8
Total Number 8
Disease Relevance 4.05
Pain Relevance 1.95

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

plasma membrane (TLR4, LY96) extracellular space (LY96) signal transduction (TLR4)
extracellular region (LY96) intracellular (TLR4) cytoplasm (TLR4)
Anatomy Link Frequency
MD2 6
TLR4 (Homo sapiens)
LY96 (Homo sapiens)
Pain Link Frequency Relevance Heat
antagonist 6 99.84 Very High Very High Very High
Central nervous system 12 97.24 Very High Very High Very High
Arthritis 213 96.96 Very High Very High Very High
Lasting pain 4 95.56 Very High Very High Very High
cytokine 90 77.04 Quite High
chemokine 13 76.16 Quite High
Inflammation 106 66.80 Quite High
Osteoarthritis 4 59.36 Quite High
Inflammatory response 32 55.04 Quite High
fibrosis 18 21.68 Low Low
Disease Link Frequency Relevance Heat
Autoimmune Disease 11 99.56 Very High Very High Very High
Leukemia 10 98.32 Very High Very High Very High
Lymphatic System Cancer 2 97.88 Very High Very High Very High
Rheumatoid Arthritis 207 96.96 Very High Very High Very High
Pain 8 95.56 Very High Very High Very High
Sepsis 9 94.88 High High
Disease 36 94.28 High High
Systemic Lupus Erythematosus 7 87.48 High High
Systemic Sclerosis 6 87.16 High High
Bacterial Respiratory Disease 1 67.68 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
A peptide antagonist of the TLR4-MD2 interaction.
TLR4 Binding (interaction) of MD2 in MD2 associated with antagonist
1) Confidence 0.54 Published 2009 Journal Chembiochem Section Title Doc Link 19184989 Disease Relevance 0.26 Pain Relevance 0.28
We herein report a chemical biology approach by using a rationally designed peptide inhibitor to disrupt the TLR4-MD2 association, thereby blocking TLR4 signaling.
TLR4 Binding (association) of MD2 in MD2
2) Confidence 0.40 Published 2009 Journal Chembiochem Section Abstract Doc Link 19184989 Disease Relevance 0.28 Pain Relevance 0.27
We herein report a chemical biology approach by using a rationally designed peptide inhibitor to disrupt the TLR4-MD2 association, thereby blocking TLR4 signaling.
TLR4 Binding (association) of MD2 in MD2
3) Confidence 0.40 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.
TLR4 Binding (interaction) of MD2 in MD2 associated with antagonist
4) Confidence 0.40 Published 2009 Journal Chembiochem Section Title Doc Link 19184989 Disease Relevance 0.26 Pain Relevance 0.28
So the interaction between LY96 in synovial tissue and TLR2 or TLR4 in the PBMC may indicate that the interaction between these two tissues in RA is mediated by the TLR signaling pathway.
TLR4 Binding (interaction) of LY96 associated with arthritis
5) Confidence 0.24 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2855702 Disease Relevance 1.29 Pain Relevance 0.36
The LY96 protein appears to be associated with TLR4 on the cell surface and confers responsiveness to lipopolysaccyaride (LPS), thus providing a link between the receptor and the LPS signaling pathway.
TLR4 Binding (associated) of LY96
6) Confidence 0.24 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2855702 Disease Relevance 1.49 Pain Relevance 0.38
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].
TLR4 Binding (association) of MD2 in MD2
7) Confidence 0.16 Published 2007 Journal Molecular Vision Section Body Doc Link PMC2768757 Disease Relevance 0.17 Pain Relevance 0.13
Despite the absence of a transmembrane domain, MD2 can attach to the cell surface via its interaction with TLR4 through specific epitopes.
TLR4 Binding (interaction) of MD2 in MD2
8) Confidence 0.09 Published 2010 Journal Fibrogenesis Tissue Repair Section Body Doc Link PMC2984459 Disease Relevance 0 Pain Relevance 0

General Comments

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