PMID: 16920490 IFN-gamma binds to the IFN-gamma receptor.

PMID: 16920490, 1698311, 10359581 In the case of LPS, efficient ligand recognition requires the signalling receptor TLR4, as well as the CD14 co-receptor (Wright et al., 1990) and MD-2 accessory molecule

PMID: 16920490, 1698311, 10359581 n the case of LPS, efficient ligand recognition requires the signalling receptor TLR4, as well as the CD14 co-receptor (Wright et al., 1990) and MD-2 accessory molecule

PMID: 16920490, 14993454 Full signal transduction requires a number of signalling adaptors, including MyD88 and the adaptors of the MyD88-independent pathway, TRAM (also called TIRP, TICAM2) and TRIF (also known as TICAM1) (reviewed in Vogel et al., 2003)

PMID: 16920490, 14993454 Full signal transduction requires a number of signalling adaptors, including MyD88 and the adaptors of the MyD88-independent pathway, TRAM (also called TIRP, TICAM2) and TRIF (also known as TICAM1) (reviewed in Vogel et al., 2003)

PMID: 16920490, 14993454 Full signal transduction requires a number of signalling adaptors, including MyD88 and the adaptors of the MyD88-independent pathway, TRAM (also called TIRP, TICAM2) and TRIF (also known as TICAM1) (reviewed in Vogel et al., 2003)

PMID: 16920490, 11130078 CpG DNA signalling is mediated by the TLR9 signalling receptor

PMID: 16920490, 11130078 CpG DNA signalling is mediated by the TLR9 signalling receptor (Hemmi et al., 2000), and unlike TLR4, the MyD88 signalling adaptor mediates all known downstream responses (Schnare et al., 2000).

PMID: 16920490, 15928677 LPS induces expression of negative regulators of key adaptor/signalling molecules (e.g. IRAK-M and SOCS1 that target IRAKs, ST2L that sequesters MyD88 and MAL) (Liew et al., 2005).

PMID: 16920490, 15928677, 11870615, 12811837, 10453004 LPS induces expression of negative regulators of key adaptor/signalling molecules (e.g. IRAK-M and SOCS1 that target IRAKs, ST2L that sequesters MyD88 and MAL) (Liew et al., 2005). Both LPS and IFN¦Ã induced expression of these SOCS proteins (SOCS1 and SOCS3), and LPS pre-treatment inhibited some functions of IFN¦Ã signalling via the activities of these proteins (Crespo et al., 2002; Dalpke et al., 2003; Stoiber et al., 1999

PMID: 16920490 Induction of Tlr9 mRNA by IFN¦Ã in BMM was largely dependent on the presence of CSF-1 that suppressed Tlr9 expression (manuscript in preparation).

PMID: 16920490, 11964313, 12811837,7999637, 11672593, 12831455 IFN¦Ã stimulation induced Tlr2, Tlr4, and Tlr6 mRNAs, upregulated expression of TLR2 and TLR4 protein at the cell surface, and increased resulting LPS-binding ability of macrophages

PMID: 16920490 Induction of Tlr9 mRNA by IFN¦Ã in BMM was largely dependent on the presence of CSF-1 that suppressed Tlr9 expression (manuscript in preparation).

PMID: 16920490, 10725699 LPS downregulates surface expression of the signalling receptor TLR4, and its accessory molecule, MD-2 (Nomura et al., 2000).

PMID: 16920490, 10725699 LPS downregulates surface expression of the signalling receptor TLR4, and its accessory molecule, MD-2 (Nomura et al., 2000).

PMID: 16920490, 11964313, 15324355, 12761135,12831455 Numerous reports document the IFN¦Ã-dependent induction of the CD14 co-receptor and MD-2 accessory molecule, which aid in LPS signalling

PMID: 16920490, 12831455, 12761135, 15324355 ,11964313 Numerous reports document the IFN¦Ã-dependent induction of the CD14 co-receptor and MD-2 accessory molecule, which aid in LPS signalling

PMID: 16920490, 11964313, 15324355, 12761135, 12831455 12032143 Additionally, IFN¦Ã upregulated the expression of MyD88 (Bosisio et al., 2002; Mochizuki et al., 2004; Tamai et al., 2003) and IRAK1 (Adib-Conquy and Cavaillon, 2002), which participate in TLR signalling pathways.

PMID: 16920490,12032143 Additionally, IFN¦Ã upregulated the expression of MyD88 and IRAK1

PMID: 16920490, 12811837, 10453004, 11870615 Both LPS and IFN¦Ã induced expression of these SOCS proteins (SOCS1 and SOCS3), and LPS pre-treatment inhibited some functions of IFN¦Ã signalling via the activities of these proteins (Crespo et al., 2002; Dalpke et al., 2003; Stoiber et al., 1999).

PMID: 16920490, 11870615, 10453004, 12811837 Both LPS and IFN¦Ã induced expression of these SOCS proteins (SOCS1 and SOCS3), and LPS pre-treatment inhibited some functions of IFN¦Ã signalling via the activities of these proteins (Crespo et al., 2002; Dalpke et al., 2003; Stoiber et al., 1999).

PMID: 16920490, 10453004, 12811837, 11870615 Both LPS and IFN¦Ã induced expression of these SOCS proteins (SOCS1 and SOCS3), and LPS pre-treatment inhibited some functions of IFN¦Ã signalling via the activities of these proteins (Crespo et al., 2002; Dalpke et al., 2003; Stoiber et al., 1999

PMID: 16920490, 12831455, 11672593, 7999637, 12811837, 11964313 IFN¦Ã stimulation induced Tlr2, Tlr4, and Tlr6 mRNAs, upregulated expression of TLR2 and TLR4 protein at the cell surface, and increased resulting LPS-binding ability of macrophages

PMID: 16920490, 15928677 LPS induces expression of negative regulators of key adaptor/signalling molecules (e.g. IRAK-M and SOCS1 that target IRAKs, ST2L that sequesters MyD88 and MAL) (Liew et al., 2005).

PMID: 16920490, 12811837, 12686553 Signalling initiated by a number of TLR agonists (e.g. LPS, CpG DNA, lipotechoic acid) induced STAT1 S727 phosphorylation, via activation of p38 MAPK pathways (

PMID: 16920490, 15928677 LPS induces expression of negative regulators of key adaptor/signalling molecules (e.g. IRAK-M and SOCS1 that target IRAKs, ST2L that sequesters MyD88 and MAL) (Liew et al., 2005).

PMID: 16920490, 9864217 IFN¦Ã pre-treatment of RAW264.7 cells promoted LPS-induced NF-¦ÊB activation and DNA binding kinetics, as well as causing more rapid degradation of the NF-¦ÊB inhibitor, I¦ÊB¦Á (Held et al., 1999)

PMID: 16920490, 9864217 IFN¦Ã pre-treatment of RAW264.7 cells promoted LPS-induced NF-¦ÊB activation and DNA binding kinetics, as well as causing more rapid degradation of the NF-¦ÊB inhibitor, I¦ÊB¦Á (Held et al., 1999)

PMID: 16920490, 9864217 IFN¦Ã pre-treatment of RAW264.7 cells promoted LPS-induced NF-¦ÊB activation and DNA binding kinetics, as well as causing more rapid degradation of the NF-¦ÊB inhibitor, I¦ÊB¦Á

PMID: 16920490 IFN¦Ã also influenced the activity of another key LPS-induced transcription factor, AP-1, in human monocytes.

PMID: 16920490, 11972023, 10975834, 9649436 In the case of TLR4, LPS treatment following IFN¦Ã exposure increased the percentage of STAT1 molecules phosphorylated on both Y701 and S727, and subsequent STAT1 DNA-binding activity relative to IFN¦Ã treatment alone

PMID: 16920490, 12667213, 9568729 IFN¦Ã signalling induced Inos mRNA via STAT1, but induction was maximal only when the Inos promoter NF-¦ÊB sites were occupied following TLR ligation

PMID: 16920490, 2498530 IFN-gamma stimulation induces Ifn-beta mRNA.

PMID: 16920490, 11964313, 12811837, 7999637, 1167259 IFN¦Ã stimulation induced Tlr2, Tlr4, and Tlr6 mRNAs, upregulated expression of TLR2 and TLR4 protein at the cell surface, and increased resulting LPS-binding ability of macrophages

PMID: 16920490, 15928677 LPS induces expression of negative regulators of key adaptor/signalling molecules (e.g. IRAK-M and SOCS1 that target IRAKs, ST2L that sequesters MyD88 and MAL) (Liew et al., 2005).

PMID: 16920490, 9864217 IFN¦Ã pre-treatment of RAW264.7 cells promoted LPS-induced NF-¦ÊB activation and DNA binding kinetics, as well as causing more rapid degradation of the NF-¦ÊB inhibitor, I¦ÊB¦Á (Held et al., 1999)

PMID: 16920490, 12811837, 12686553 Signalling initiated by a number of TLR agonists (e.g. LPS, CpG DNA, lipotechoic acid) induced STAT1 S727 phosphorylation, via activation of p38 MAPK pathways

PMID: 16920490, 12811837, 12686553 Signalling initiated by a number of TLR agonists (e.g. LPS, CpG DNA, lipotechoic acid) induced STAT1 S727 phosphorylation, via activation of p38 MAPK pathways

PMID: 16920490, 12811837, 12686553 Signalling initiated by a number of TLR agonists (e.g. LPS, CpG DNA, lipotechoic acid) induced STAT1 S727 phosphorylation, via activation of p38 MAPK pathways

PMID: 16920490, 12811837, 12686553 Signalling initiated by a number of TLR agonists (e.g. LPS, CpG DNA, lipotechoic acid) induced STAT1 S727 phosphorylation, via activation of p38 MAPK pathways

PMID: 16920490, 10975834, 9649436 In the case of TLR4, LPS treatment following IFN¦Ã exposure increased the percentage of STAT1 molecules phosphorylated on both Y701 and S727, and subsequent STAT1 DNA-binding activity relative to IFN¦Ã treatment alone

PMID: 16920490, 10975834, 9649436 In the case of TLR4, LPS treatment following IFN¦Ã exposure increased the percentage of STAT1 molecules phosphorylated on both Y701 and S727, and subsequent STAT1 DNA-binding activity relative to IFN¦Ã treatment alone

PMID: 16920490, 11972023, 10975834, 9649436 STAT1 is phosphorylated at both sites following IFN¦Ã exposure; the IFN¦Ã receptor/JAK complex directly mediates Y701 phosphorylation, whereas S727 phosphorylation occurs via a separate pathway involving Ca(2+)/calmodulin-dependent kinase II

PMID: 16920490, 16816106 Recent studies from our laboratory showed that Hdac1 mRNA was induced by LPS in BMM and that HDACs acted as negative feedback regulators of a sub-set of LPS-inducible genes, including Cox2

PMID: 16920490, 12831455, 11672593, 7999637, 12811837, 11964313 IFN¦Ã stimulation induced Tlr2, Tlr4, and Tlr6 mRNAs, upregulated expression of TLR2 and TLR4 protein at the cell surface, and increased resulting LPS-binding ability of macrophages

PMID: 16920490, 16816106 Recent studies from our laboratory showed that Hdac1 mRNA was induced by LPS in BMM and that HDACs acted as negative feedback regulators of a sub-set of LPS-inducible genes, including Cox2

PMID: 16920490, 14645718, 16481475 Further, STAT1 and HDAC1 physically interact (Nusinzon and Horvath, 2003) and STAT1 is an acetylated protein