PMID: 12106783 LPS is bound by CD14 and/or CD11/18 at the cell surface and facilitates an interaction with the TLR4-MD2 complex.

PMID: 12106783 The CD14-independent cluster able to bind to LPS and represented by Hsp70, Hsp-90, CXCR4, and GDF5 may also contribute to LPS-induced TNF-¦Á production by as yet unknown mechanism(s).

PMID: 12106783 Induction of a panel of inflammatory genes including COX-2, IL-12 p35, IL-12 p40, TNF-¦Á, IP-10, IRF-1, and ICSBP by low concentrations of LPS required both CD14 and TLR4.

PMID: 12106783 E. coli LPS and the TLR2 agonists, lipoarabinomannan (LAM) and soluble tuberculosis factor (STF), rapidly activated mitogen activated (MAP) kinases, as well as NF-¦ÊB and AP-1 transactivation.

PMID: 12106783 E. coli LPS and the TLR2 agonists, lipoarabinomannan (LAM) and soluble tuberculosis factor (STF), rapidly activated mitogen activated (MAP) kinases, as well as NF-¦ÊB and AP-1 transactivation.

PMID: 12106783, 9200483, 7535339, 9820516 CD18 in complex with CD11b or CD11c, activates signaling cascades leading to NF-¦ÊB translocation.

PMID: 12106783 IFN-¦Ã, IL-12 p40, and MCP-5 were induced only by E. coli LPS. Induction of a panel of inflammatory genes including COX-2, IL-12 p35, IL-12 p40, TNF-¦Á, IP-10, IRF-1, and ICSBP by low concentrations of LPS required both CD14 and TLR4.

PMID: 12106783 IFN-¦Ã, IL-12 p40, and MCP-5 were induced only by E. coli LPS.

PMID: 12106783 IFN-¦Ã, IL-12 p40, and MCP-5 were induced only by E. coli LPS

PMID: 12106783 E. coli LPS and the TLR2 agonists, lipoarabinomannan (LAM) and soluble tuberculosis factor (STF), rapidly activated mitogen activated (MAP) kinases, as well as NF-¦ÊB and AP-1 transactivation.

PMID: 12106783 E. coli LPS and the TLR2 agonists, lipoarabinomannan (LAM) and soluble tuberculosis factor (STF), rapidly activated mitogen activated (MAP) kinases, as well as NF-¦ÊB and AP-1 transactivation.

PMID: 12106783, 1698311, 7534290, 7534291 soluble form (sCD14) or a glycosylphosphatidylinositol (GPI)-linked form (mCD14) on myeloid lineage cells bound enterobacterial LPS with high affinity.

PMID: 12106783 Activation of DC through TLR2 also led to preferential induction of IL-8 and p19/IL-23.

PMID: 12106783 Activation of DC through TLR2 also led to preferential induction of IL-8 and p19/IL-23.

PMID: 12106783, 9751057 LPS binding ability of TLRs revealed that 3H-labeled LPS bound TLR2. However, the kinetics of association was slow and the Kd low (500?700 nM).

PMID: 12106783 Induction of a panel of inflammatory genes including COX-2, IL-12 p35, IL-12 p40, TNF-¦Á, IP-10, IRF-1, and ICSBP by low concentrations of LPS required both CD14 and TLR4.

PMID: 12106783 Induction of a panel of inflammatory genes including COX-2, IL-12 p35, IL-12 p40, TNF-¦Á, IP-10, IRF-1, and ICSBP by low concentrations of LPS required both CD14 and TLR4.

PMID: 12106783 Induction of a panel of inflammatory genes including COX-2, IL-12 p35, IL-12 p40, TNF-¦Á, IP-10, IRF-1, and ICSBP by low concentrations of LPS required both CD14 and TLR4.

PMID: 12106783 Induction of a panel of inflammatory genes including COX-2, IL-12 p35, IL-12 p40, TNF-¦Á, IP-10, IRF-1, and ICSBP by low concentrations of LPS required both CD14 and TLR4.

PMID: 12106783 Induction of a panel of inflammatory genes including COX-2, IL-12 p35, IL-12 p40, TNF-¦Á, IP-10, IRF-1, and ICSBP by low concentrations of LPS required both CD14 and TLR4.

PMID: 12106783 Stimulation of cells with LPS or other inflammatory stimuli leads to the activation of the I¦ÊB kinase complex (IKK).

PMID: 12106783 In addition to NF-¦ÊB, LPS also activates MAP kinases, including JNK-1/2, ERK-1/2, and p38, in macrophages.

PMID: 12106783 LPS is bound by CD14 and/or CD11/18 at the cell surface and facilitates an interaction with the TLR4-MD2 complex.

PMID: 12106783 Stimulation of cells with LPS or other inflammatory stimuli leads to the activation of the I¦ÊB kinase complex (IKK), which phosphorylates I¦ÊB on two N-terminal serine residues.

PMID: 12106783 Phosphorylated I¦ÊB becomes a substrate for ubiquitin ligase and finally undergoes degradation by the 26S proteasome.

PMID: 12106783 Phosphorylated I¦ÊB becomes a substrate for ubiquitin ligase and finally undergoes degradation by the 26S proteasome.

PMID: 12106783 Released NF-¦ÊB then moves to the nucleus, where it activates the transcription of many ¦ÊB-dependent genes, including TNF-¦Á and I¦ÊB¦Á.

PMID: 12106783 In addition to NF-¦ÊB, LPS also activates MAP kinases, including JNK-1/2, ERK-1/2, and p38, in macrophages.

PMID: 12106783 In addition to NF-¦ÊB, LPS also activates MAP kinases, including JNK-1/2, ERK-1/2, and p38, in macrophages.

PMID: 12106783 In addition to NF-¦ÊB, LPS also activates MAP kinases, including JNK-1/2, ERK-1/2, and p38, in macrophages.

PMID: 12106783 In addition to NF-¦ÊB, LPS also activates MAP kinases, including JNK-1/2, ERK-1/2, and p38, in macrophages.

PMID: 12106783 The CD14-independent cluster able to bind to LPS and represented by Hsp70, Hsp-90, CXCR4, and GDF5 may also contribute to LPS-induced TNF-¦Á production by as yet unknown mechanism(s). Induction of a panel of inflammatory genes including COX-2, IL-12 p35, IL-12 p40, TNF-¦Á, IP-10, IRF-1, and ICSBP by low concentrations of LPS required both CD14 and TLR4. Released NF-¦ÊB then moves to the nucleus, where it activates the transcription of many ¦ÊB-dependent genes, including TNF-¦Á and I¦ÊB¦Á. MAP kinases have been shown to be important for both TNF-¦Á and IL-1 synthesis

PMID: 12106783 Released NF-¦ÊB then moves to the nucleus, where it activates the transcription of many ¦ÊB-dependent genes, including TNF-¦Á and I¦ÊB¦Á.

PMID: 12106783 LPS is bound by CD14 and/or CD11/18 at the cell surface and facilitates an interaction with the TLR4-MD2 complex.

PMID: 12106783 Induction of a panel of inflammatory genes including COX-2, IL-12 p35, IL-12 p40, TNF-¦Á, IP-10, IRF-1, and ICSBP by low concentrations of LPS required both CD14 and TLR4. MAP kinases have been shown to be important for both TNF-¦Á and IL-1 synthesis

PMID: 12106783 Induction of a panel of inflammatory genes including COX-2, IL-12 p35, IL-12 p40, TNF-¦Á, IP-10, IRF-1, and ICSBP by low concentrations of LPS required both CD14 and TLR4. MAP kinases have been shown to be important for both TNF-¦Á and IL-1 synthesis

PMID: 12106783 Induction of a panel of inflammatory genes including COX-2, IL-12 p35, IL-12 p40, TNF-¦Á, IP-10, IRF-1, and ICSBP by low concentrations of LPS required both CD14 and TLR4. MAP kinases have been shown to be important for both TNF-¦Á and IL-1 synthesis

PMID: 12106783 Induction of a panel of inflammatory genes including COX-2, IL-12 p35, IL-12 p40, TNF-¦Á, IP-10, IRF-1, and ICSBP by low concentrations of LPS required both CD14 and TLR4. MAP kinases have been shown to be important for both TNF-¦Á and IL-1 synthesis

PMID: 12106783 Induction of a panel of inflammatory genes including COX-2, IL-12 p35, IL-12 p40, TNF-¦Á, IP-10, IRF-1, and ICSBP by low concentrations of LPS required both CD14 and TLR4. MAP kinases have been shown to be important for both TNF-¦Á and IL-1 synthesis

PMID: 12106783 E. coli LPS and the TLR2 agonists, lipoarabinomannan (LAM) and soluble tuberculosis factor (STF), rapidly activated mitogen activated (MAP) kinases, as well as NF-¦ÊB and AP-1 transactivation.

PMID: 12106783 E. coli LPS and the TLR2 agonists, lipoarabinomannan (LAM) and soluble tuberculosis factor (STF), rapidly activated mitogen activated (MAP) kinases, as well as NF-¦ÊB and AP-1 transactivation.

PMID: 12106783, 9200483, 7535339, 9820516 CD18 in complex with CD11b or CD11c, activates signaling cascades leading to NF-¦ÊB translocation.

PMID: 12106783 E. coli LPS and the TLR2 agonists, lipoarabinomannan (LAM) and soluble tuberculosis factor (STF), rapidly activated mitogen activated (MAP) kinases, as well as NF-¦ÊB and AP-1 transactivation.

PMID: 12106783 Nod 1 binds to 3H?LPS and activates NF-¦ÊB in a TLR4-independent fashion.

PMID: 12106783, 2462607 CD11b/CD18 (Mac-1) and CD11c/CD18, obligate heterodimers share a common molecule, CD18, which was shown to be necessary for LPS binding on the surface of cells expressing integrins.

PMID: 12106783, 2462607 CD11b/CD18 (Mac-1) and CD11c/CD18, obligate heterodimers share a common molecule, CD18, which was shown to be necessary for LPS binding on the surface of cells expressing integrins.

PMID: 12106783 E. coli LPS and the TLR2 agonists, lipoarabinomannan (LAM) and soluble tuberculosis factor (STF), rapidly activated mitogen activated (MAP) kinases, as well as NF-¦ÊB and AP-1 transactivation.

PMID: 12106783 LPS can also be internalized through an as yet unknown mechanism.

PMID: 12106783 LPS can also be internalized through an as yet unknown mechanism, and may bind to intracellular Nod1.