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<svg xmlns="http://www.w3.org/2000/svg" xmlns:xlink="http://www.w3.org/1999/xlink" style="overflow:visible;enable-background:new 0 0 431.413 43.583" viewBox="0 0 362.094 362.089" preserveAspectRatio="xMidYMid meet" zoomAndPan="magnify" width="362.094" height="362.089" contentScriptType="text/ecmascript" contentStyleType="text/css" version="1.0"><defs><linearGradient xmlns:xlink="http://www.w3.org/1999/xlink" id="color2" gradientUnits="objectBoundingBox" gradientTransform="" x1="0%" y1="0%" x2="100%" y2="0%" spreadMethod="pad"><stop style="stop-color:#000000;stop-opacity:1;" offset="0%"></stop></linearGradient><linearGradient xmlns:xlink="http://www.w3.org/1999/xlink" id="color3" gradientUnits="objectBoundingBox" gradientTransform="" x1="0%" y1="0%" x2="100%" y2="0%" spreadMethod="pad"><stop style="stop-color:#0000ff;stop-opacity:1;" offset="0%"></stop></linearGradient><linearGradient xmlns:xlink="http://www.w3.org/1999/xlink" id="stroke1" gradientUnits="objectBoundingBox" gradientTransform="" x1="0%" y1="0%" x2="100%" y2="0%" spreadMethod="pad"><stop style="stop-color:#808080;stop-opacity:1;" offset="0%"></stop></linearGradient><linearGradient xmlns:xlink="http://www.w3.org/1999/xlink" id="stroke2" gradientUnits="objectBoundingBox" gradientTransform="" x1="0%" y1="0%" x2="100%" y2="0%" spreadMethod="pad"><stop style="stop-color:#008000;stop-opacity:1;" offset="0%"></stop></linearGradient><linearGradient xmlns:xlink="http://www.w3.org/1999/xlink" id="stroke3" gradientUnits="objectBoundingBox" gradientTransform="" x1="0%" y1="0%" x2="100%" y2="0%" spreadMethod="pad"><stop style="stop-color:#00ff00;stop-opacity:1;" offset="0%"></stop></linearGradient><linearGradient xmlns:xlink="http://www.w3.org/1999/xlink" id="color1" gradientUnits="objectBoundingBox" gradientTransform="" x1="0%" y1="0%" x2="100%" y2="0%" spreadMethod="pad"><stop style="stop-color:#DD1C7E;stop-opacity:1;" offset="0%"></stop></linearGradient></defs><g><path fill="url(#XMLID_2_)" d="M347.41,145.592c19.58,19.581,19.58,51.325,0,70.905L216.497,347.406 c-19.58,19.576-51.326,19.576-70.904,0L14.685,216.497c-19.58-19.581-19.58-51.325,0-70.905L145.592,14.68 c19.579-19.573,51.324-19.573,70.904,0L347.41,145.592z"></path><g><path d="M147.401,28.39L28.395,147.401c-18.551,18.551-18.551,48.736,0,67.287l119.006,119.009 c18.551,18.547,48.736,18.547,67.288,0l119.01-119.009c8.987-8.985,13.937-20.934,13.937-33.643s-4.949-24.658-13.937-33.644l0,0 L214.689,28.39C196.137,9.844,165.951,9.843,147.401,28.39z M150.229,330.869L31.223,211.86c-16.991-16.991-16.991-44.639,0-61.631 L150.229,31.218c16.992-16.987,44.64-16.987,61.632,0l119.01,119.01c8.231,8.231,12.765,19.175,12.765,30.816 s-4.533,22.584-12.765,30.815l-119.01,119.009C194.868,347.856,167.22,347.856,150.229,330.869z"></path></g></g><g><path style="fill:url(#color1);stroke:none;" d="M67.66,227.26 c38.149-33.786,104.903-59.965,163.419-40.252l-8.939,50.335l83.449-53.662L245.36,86.73l-7.273,49.991 C153.513,131.339,102.871,167.523,67.66,227.26z"></path></g><defs><linearGradient xmlns:xlink="http://www.w3.org/1999/xlink" id="XMLID_2_" gradientUnits="userSpaceOnUse" x1="181.0469" y1="-4.882813e-004" x2="181.0469" y2="362.0894"><stop style="stop-color:#FFFFFF" offset="0"></stop><stop style="stop-color:#FFF8ED" offset="0.0424"></stop><stop style="stop-color:#FDE2B2" offset="0.1921"></stop><stop style="stop-color:#FCCF7F" offset="0.3414"></stop><stop style="stop-color:#FBC055" offset="0.4869"></stop><stop style="stop-color:#FAB435" offset="0.6279"></stop><stop style="stop-color:#F9AB1E" offset="0.7631"></stop><stop style="stop-color:#F9A610" offset="0.8898"></stop><stop style="stop-color:#F9A40B" offset="1"></stop></linearGradient></defs></svg> PMID: 17405910 association of single LPS molecules with plasmaderived LPS-binding protein (LBP)

PMID: 17405910 one LPS bound to one LBP, the so formed protein–glycolipid complex is recognized, with high specificity, by CD14

PMID: 17405910, 11034352 activation of TLR4, which is thought to initiate intracellular signaling upon association with a CD14 molecule that is occupied by an LPS–LBP complex.

PMID: 17405910 TLR4 signaling depends on the presence of MD2, a secretory glycoprotein that associates with TLR4.

PMID: 17405910 Subsequent to the association of MyD88 with TLR4, MyD88 recruits the IL-1 receptor-associated kinase 1 (IRAK1).

PMID: 17405910 Subsequent to the association of MyD88 with TLR4, MyD88 recruits the IL-1 receptor-associated kinase 1 (IRAK1).

PMID: 17405910 Phosphorylation of IRAK1 by IRAK4 and other kinases results in the dissociation of IRAK1 from TLR4.

PMID: 17405910 Phosphorylated IRAK1 associates, in the cytosol, with tumor necrosis factor receptor (TNFR)-associated factor 6 (TRAF6).

PMID: 17405910 Phosphorylation of IRAK1 by IRAK4 and other kinases results in the dissociation of IRAK1 from TLR4.

Indirect

PMID: 17405910 TRAF6, a RING domain-containing E3 ubiquitin ligase, activates mitogen-activated protein kinase kinase kinases (MAP3K), transforming growth factor beta (TGF-beta)-activating kinase 1 (TAK1), mitogen-activated protein kinase/extracellular signal-regulated kinase kinase kinase (MEKK3, and apoptosis signal-regulating kinase 1 (ASK1).

Indirect

PMID: 17405910 TRAF6, a RING domain-containing E3 ubiquitin ligase, activates mitogen-activated protein kinase kinase kinases (MAP3K), transforming growth factor beta (TGF-beta)-activating kinase 1 (TAK1), mitogen-activated protein kinase/extracellular signal-regulated kinase kinase kinase (MEKK3, and apoptosis signal-regulating kinase 1 (ASK1).

Indirect

PMID: 17405910 TRAF6, a RING domain-containing E3 ubiquitin ligase, activates mitogen-activated protein kinase kinase kinases (MAP3K), transforming growth factor beta (TGF-beta)-activating kinase 1 (TAK1), mitogen-activated protein kinase/extracellular signal-regulated kinase kinase kinase (MEKK3, and apoptosis signal-regulating kinase 1 (ASK1).

Indirect

PMID: 17405910 MAP3K family (T1, TAK1; M3, MEKK3; A1, ASK1) which, in turn, activate Jnk (J), IKK (I), and p38 (p).

Indirect

PMID: 17405910 MAP3K family (T1, TAK1; M3, MEKK3; A1, ASK1) which, in turn, activate Jnk (J), IKK (I), and p38 (p).

Indirect

PMID: 17405910 MAP3K family (T1, TAK1; M3, MEKK3; A1, ASK1) which, in turn, activate Jnk (J), IKK (I), and p38 (p).

PMID: 17405910 Subsequent activation of cJun N-terminal kinase (Jnk), I-kappaB kinase (IKK) complex (consisting of alpha, beta and gamma subunits), and p38, leads to phosphorylation of cJun, I-kappaB, and ATF2, respectively.

PMID: 17405910 Subsequent activation of cJun N-terminal kinase (Jnk), I-kappaB kinase (IKK) complex (consisting of alpha, beta and gamma subunits), and p38, leads to phosphorylation of cJun, I-kappaB, and ATF2, respectively.

Indirect

PMID: 17405910 Subsequent activation of cJun N-terminal kinase (Jnk), I-kappaB kinase (IKK) complex (consisting of alpha, beta and gamma subunits), and p38, leads to phosphorylation of cJun, I-kappaB, and ATF2, respectively.

PMID: 17405910 Phosphorylated I-kappaB is ubiquitinated and degraded by the 26S proteosome, leaving the p65-p50 dimer (NF-kappaB), which is now free to translocate to the nucleus.

PMID: 17405910 Phosphorylated I-kappaB is ubiquitinated and degraded by the 26S proteosome, leaving the p65-p50 dimer (NF-kappaB), which is now free to translocate to the nucleus.

PMID: 17405910, 15356101 The generation of ROS appears to result from a direct activation of membrane-bound NADPH oxidase 4 by TLR4.

Indirect

PMID: 17405910, 15356101 The generation of ROS appears to result from a direct activation of membrane-bound NADPH oxidase 4 by TLR4.

PMID: 17405910, 9564042 ASK1 can only be activated by TRAF6 if the associated thioredoxin (TrX) is displaced from TRAF6.

Indirect

PMID: 17405910, 15864310 This dissociation depends on the formation of ROS.

PMID: 17405910, 12062447, 12062447 TIRAP, another TLR4 adapter protein appears to be involved in the activation of interferon regulatory factor 3 (IRF3), a transcription factor, which induces the type I interferon gene, and further evidence suggests that this activation is mediated by a double-stranded RNA responsive protein kinase (PKR).

PMID: 17405910, 12062447, 12062447 TIRAP, another TLR4 adapter protein appears to be involved in the activation of interferon regulatory factor 3 (IRF3), a transcription factor, which induces the type I interferon gene, and further evidence suggests that this activation is mediated by a double-stranded RNA responsive protein kinase (PKR).

PMID: 17405910 Phosphorylated I-kappaB is ubiquitinated and degraded by the 26S proteosome, leaving the p65-p50 dimer (NF-kappaB), which is now free to translocate to the nucleus.

PMID: 17405910 Apart from MyD88 and TIRAP, additional TLR4 adapter proteins have been identified.

PMID: 17405910, 12062447, 15029200, 16006187 TIRAP, another TLR4 adapter protein appears to be involved in the activation of interferon regulatory factor 3 (IRF3), a transcription factor, which induces the type I interferon gene, and further evidence suggests that this activation is mediated by a double-stranded RNA responsive protein kinase (PKR).

Indirect

PMID: 17405910, 16006187 TIR domain-containing adapter inducing interferon (TRIF) and TRIF-related adapter molecule (TRAM), both involved in the activation of IRF3 and IRF7.

PMID: 17405910, 9820516 macrophages express several other LPS receptors, for example, CD11b/CD18

PMID: 17405910, 1852209 macrophages express several other LPS receptors, for example, CD11b/CD18, class A macrophage scavenger receptor (MSR)

PMID: 17405910, 1852209 MSR acts as a scavenger for LPS, that is, rather than eliciting a proinflammatory response, the MSR–LPS complex is internalized and LPS is partially degraded.

PMID: 17405910, 16021602 NOD-1 and -2 agonists also act in synergy with LPS to stimulate cytokine production.

PMID: 17405910, 15275964 Cationic proteins, e.g., protamines and CAP37, associate with LPS and bind to cellular surfaces.

PMID: 17405910 Heparin exerts its anticoagulant effect through binding to AT III and thrombin. Apart from its interaction with proteins of the coagulation pathway, heparin binds to LBP and displaces LPS

PMID: 17405910, 14550561 LPS is bound and neutralized by poly-L-histidine.

PMID: 17405910, 9564042 ASK1 can only be activated by TRAF6 if the associated thioredoxin (TrX) is displaced from TRAF6.

PMID: 17405910 MAP3K family (T1, TAK1; M3, MEKK3; A1, ASK1) which, in turn, activate Jnk (J), IKK (I), and p38 (p).

PMID: 17405910 MAP3K family (T1, TAK1; M3, MEKK3; A1, ASK1) which, in turn, activate Jnk (J), IKK (I), and p38 (p).

PMID: 17405910 MAP3K family (T1, TAK1; M3, MEKK3; A1, ASK1) which, in turn, activate Jnk (J), IKK (I), and p38 (p).

PMID: 17405910 MAP3K family (T1, TAK1; M3, MEKK3; A1, ASK1) which, in turn, activate Jnk (J), IKK (I), and p38 (p).

PMID: 17405910 MAP3K family (T1, TAK1; M3, MEKK3; A1, ASK1) which, in turn, activate Jnk (J), IKK (I), and p38 (p).

PMID: 17405910 MAP3K family (T1, TAK1; M3, MEKK3; A1, ASK1) which, in turn, activate Jnk (J), IKK (I), and p38 (p).

PMID: 17405910, 15356101 The generation of ROS appears to result from a direct activation of membrane-bound NADPH oxidase 4 by TLR4.

PMID: 17405910, 12062447, 12062447 TIRAP, another TLR4 adapter protein appears to be involved in the activation of interferon regulatory factor 3 (IRF3), a transcription factor, which induces the type I interferon gene, and further evidence suggests that this activation is mediated by a double-stranded RNA responsive protein kinase (PKR).

PMID: 17405910, 12062447, 15029200, 16006187 TIR domain-containing adapter inducing interferon (TRIF) and TRIF-related adapter molecule (TRAM), both involved in the activation of IRF3 and IRF7.