INT306327

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Context Info
Confidence 0.10
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 7
Disease Relevance 1.83
Pain Relevance 0.91

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

signal transduction (Tlr4) extracellular region (Ly96) plasma membrane (Tlr4)
intracellular (Tlr4) cytoplasm (Tlr4)
Ly96 (Mus musculus)
Tlr4 (Mus musculus)
Pain Link Frequency Relevance Heat
Inflammation 189 99.52 Very High Very High Very High
chemokine 35 98.44 Very High Very High Very High
cytokine 77 97.84 Very High Very High Very High
Inflammatory response 49 96.76 Very High Very High Very High
anesthesia 7 5.00 Very Low Very Low Very Low
isoflurane 7 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
INFLAMMATION 91 99.52 Very High Very High Very High
Pneumonia 161 86.08 High High
Bacterial Infection 7 85.16 High High
Targeted Disruption 14 5.00 Very Low Very Low Very Low
Cancer 7 5.00 Very Low Very Low Very Low
Hemorrhage 7 5.00 Very Low Very Low Very Low
Necrosis 7 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Evidence derived from in vitro experiments has indicated that whereas the TLR4/MD-2 complex requires CD14 for the activation of MyD88-dependent signaling by S-LPS [14], the main form of LPS produced by most gram-negative bacteria, it does not require CD14 for activation by R-LPS.
MD-2 Binding (complex) of TLR4
1) Confidence 0.10 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2855719 Disease Relevance 0.15 Pain Relevance 0.04
These data indicate that the TLR4/MD-2 complex requires CD14 for the activation of MyD88-dependent signaling by S-LPS, but not by R-LPS.
MD-2 Binding (complex) of TLR4
2) Confidence 0.10 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2855719 Disease Relevance 0.39 Pain Relevance 0.11
These data indicate that the TLR4/MD-2 complex requires CD14 for the activation of MyD88-dependent signaling by S-LPS, but not by R-LPS.
MD-2 Binding (complex) of TLR4
3) Confidence 0.10 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2855719 Disease Relevance 0.39 Pain Relevance 0.11
Evidence derived from in vitro experiments has indicated that whereas the TLR4/MD-2 complex requires CD14 for the activation of MyD88-dependent signaling by S-LPS [14], the main form of LPS produced by most gram-negative bacteria, it does not require CD14 for activation by R-LPS.
MD-2 Binding (complex) of TLR4
4) Confidence 0.10 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2855719 Disease Relevance 0.15 Pain Relevance 0.04
Binding of LPS to the TLR4/MD-2 complex is facilitated by LPS binding protein (LBP) and CD14 [1].
MD-2 Binding (Binding) of LPS
5) Confidence 0.09 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2855719 Disease Relevance 0.24 Pain Relevance 0.22
LPS is bound by MD-2 within the TLR4/MD-2 complex [3] and subsequent conformational changes in TLR4 lead to reorganization of its cytoplasmic domain, enabling the recruitment of the adaptors MyD88 and Toll/interleukin 1 receptor domain-containing adaptor inducing interferon beta (TRIF) [4].
MD-2 Binding (bound) of LPS
6) Confidence 0.09 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2855719 Disease Relevance 0.25 Pain Relevance 0.19
LPS is bound by MD-2 within the TLR4/MD-2 complex [3] and subsequent conformational changes in TLR4 lead to reorganization of its cytoplasmic domain, enabling the recruitment of the adaptors MyD88 and Toll/interleukin 1 receptor domain-containing adaptor inducing interferon beta (TRIF) [4].
MD-2 Binding (bound) of LPS
7) Confidence 0.09 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2855719 Disease Relevance 0.25 Pain Relevance 0.19

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