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PMID: 15051069, 7537731 LPS-binding protein (LBP), a 60 kDa serum glycoprotein that binds to the lipid A moiety of LPS with a dissociation constant of 3.5 nM

PMID: 15051069 LBP removes LPS from the outer membrane and forms complexes consisting of LPS, LBP and soluble CD14 (sCD14).

PMID: 15051069 These complexes deliver LPS to membrane CD14 for LPS signaling.

PMID: 15051069 Toll-like receptor (TLR) 4 associates itself with MD-2 in the endoplasmic reticulum (ER) with the aid of a chaperone gp96. PMID: 15051069, 11593030 Association between human MD-2 and TLR4 occurs in the endoplasmic reticulum (ER).

PMID: 15051069 LPS bound to CD14 is transferred to Toll-like receptor (TLR) 4–MD-2, which undergoes oligomerization and triggers a signal. PMID: 15051069, 14517279 A lipid A antagonist, E5531, was shown to block LPS interaction with TLR4–MD-2 probably through direct interaction with TLR4–MD-2.

PMID: 15051069 LPS bound to CD14 is transferred to Toll-like receptor (TLR) 4–MD-2, which undergoes oligomerization and triggers a signal.

PMID: 15051069 The TIR domain of MyD88 is important for interaction with the cytoplasmic domain of TLR4.

PMID: 15051069 The death domain of MyD88 recruits members of the (IL)-1 receptor-associated kinases (IRAKs), IRAK1 and IRAK4.

PMID: 15051069 The death domain of MyD88 recruits members of the (IL)-1 receptor-associated kinases (IRAKs), IRAK1 and IRAK4.

PMID: 15051069, 11960013 IRAK4 is able to phosphorylate IRAK1.

PMID: 15051069 IRAK4 is able to phosphorylate IRAK1 [32], which together interact with TRAF6 (TNF receptor-associated factor 6).

indirect

PMID: 15051069, 12791976 TRAF6 can also lead to the activation of the IκBα kinase complex (IKK)the phosphorylation and subsequent degradation of IκBα, and finally the activation of NF-κBs

indirect

PMID: 15051069 This then leads to the activation of mitogen-activated protein kinases (MAPKs), such as p38s, ERKs (extracellular signal-regulated kinases) and JNK (c-Jun N-terminal kinase).

indirect

PMID: 15051069 This then leads to the activation of mitogen-activated protein kinases (MAPKs), such as p38s, ERKs (extracellular signal-regulated kinases) and JNK (c-Jun N-terminal kinase).

indirect

PMID: 15051069 This then leads to the activation of mitogen-activated protein kinases (MAPKs), such as p38s, ERKs (extracellular signal-regulated kinases) and JNK (c-Jun N-terminal kinase).

PMID: 15051069, 12791976 TRAF6 can also lead to the activation of the IκBα kinase complex (IKK)the phosphorylation and subsequent degradation of IκBα, and finally the activation of NF-κBs

PMID: 15051069, 12791976 TRAF6 can also lead to the activation of the IκBα kinase complex (IKK)the phosphorylation and subsequent degradation of IκBα, and finally the activation of NF-κBs.

PMID: 15051069, 12791976 TRAF6 can also lead to the activation of the IκBα kinase complex (IKK)the phosphorylation and subsequent degradation of IκBα, and finally the activation of NF-κBs.

PMID: 15051069, 12471095, 14556004 Two TIR-containing adaptor molecules, TIR domain-containing adaptor-inducing interferon (IFN)-β (TRIF, also known as TICAM-1) and TRIF-related adaptor molecule (TRAM), are demonstrated to work in concert to activate MyD88-independent activation of IFN regulatory factor 3 (IRF3), leading to the induction of IFN α/β.

PMID: 15051069, 12471095, 14556004 Two TIR-containing adaptor molecules, TIR domain-containing adaptor-inducing interferon (IFN)-β (TRIF, also known as TICAM-1) and TRIF-related adaptor molecule (TRAM), are demonstrated to work in concert to activate MyD88-independent activation of IFN regulatory factor 3 (IRF3), leading to the induction of IFN α/β.

indirect

indirect

PMID: 15051069, 12471095, 14556004 Two TIR-containing adaptor molecules, TIR domain-containing adaptor-inducing interferon (IFN)-β (TRIF, also known as TICAM-1) and TRIF-related adaptor molecule (TRAM), are demonstrated to work in concert to activate MyD88-independent activation of IFN regulatory factor 3 (IRF3), leading to the induction of IFN α/β.

indirect

PMID: 15051069 The MyD88-independent pathway also activates NF-κB transcription factors.

indirect

PMID: 15051069 The MyD88-independent pathway also activates NF-κB transcription factors.

PMID: 15051069, 12471095, 14556004 Two TIR-containing adaptor molecules, TIR domain-containing adaptor-inducing interferon (IFN)-β (TRIF, also known as TICAM-1) and TRIF-related adaptor molecule (TRAM), are demonstrated to work in concert to activate MyD88-independent activation of IFN regulatory factor 3 (IRF3), leading to the induction of IFN α/β.

PMID: 15051069, 12471095, 14556004 Two TIR-containing adaptor molecules, TIR domain-containing adaptor-inducing interferon (IFN)-β (TRIF, also known as TICAM-1) and TRIF-related adaptor molecule (TRAM), are demonstrated to work in concert to activate MyD88-independent activation of IFN regulatory factor 3 (IRF3), leading to the induction of IFN α/β.

PMID: 15051069, 12471095, 14556004 Two TIR-containing adaptor molecules, TIR domain-containing adaptor-inducing interferon (IFN)-β (TRIF, also known as TICAM-1) and TRIF-related adaptor molecule (TRAM), are demonstrated to work in concert to activate MyD88-independent activation of IFN regulatory factor 3 (IRF3), leading to the induction of IFN α/β.

PMID: 15051069, 12471095, 14556004 Two TIR-containing adaptor molecules, TIR domain-containing adaptor-inducing interferon (IFN)-β (TRIF, also known as TICAM-1) and TRIF-related adaptor molecule (TRAM), are demonstrated to work in concert to activate MyD88-independent activation of IFN regulatory factor 3 (IRF3), leading to the induction of IFN α/β.

PMID: 15051069 Toll-like receptor (TLR) 4 associates itself with MD-2 in the endoplasmic reticulum (ER) with the aid of a chaperone gp96 and then undergoes N-linked glycosylation in the Golgi apparatus before cell surface expression.

PMID: 15051069 Toll-like receptor (TLR) 4 associates itself with MD-2 in the endoplasmic reticulum (ER) with the aid of a chaperone gp96 and then undergoes N-linked glycosylation in the Golgi apparatus before cell surface expression. PMID: 15051069, 12738639 Human MD-2 is required for human TLR4 glycosylation at residue positions Asn526 and Asn575, without which human TLR4 cannot get to the cell surface, even with MD-2 association.

PMID: 15051069, 12738639 Human MD-2 is required for human TLR4 glycosylation at residue positions Asn526 and Asn575, without which human TLR4 cannot get to the cell surface, even with MD-2 association.

PMID: 15051069, 11500507 Human recombinant soluble MD-2 was shown to interact with LPS at an apparent dissociation constant of 65 nM, which is similar to the dissociation constant for binding of LPS to CD14 (30–74 nM).

PMID: 15051069, 7897216, 9686597, 11521060 Molecular cloning of MD-2 was preceded by the identification of radioproteictive105 (RP105) and associated MD-1.

PMID: 15051069 RP105–MD-1 is a structurally related complex and has a role in the B cell response to LPS.