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10.1177/1753425914550426 http://scihub22266oqcxt.onion/10.1177/1753425914550426 C4452626!4452626 !25394365     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25394365 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Innate+Immun 2015 ; 21 (5 ): 490-503 Nephropedia Template TP {{tp|p=25394365 |t=2015. Anti-endotoxic activity and structural basis for human MD-2·TLR4 antagonism of tetraacylated lipid A mimetics based on ?GlcN(1?1)?GlcN scaffold |pdf=|usr=}}{{25394365 }} gab.com Text Anti-endotoxic activity and structural basis for human MD-2·TLR4 antagonism of tetraacylated lipid A mimetics based on GlcN(1 1) GlcN scaffold JO: Innate Immun http://www.kidney.de/pget.php?&tw=1&pmid=25394365 #FOAvip Interfering with LPS binding by the co-receptor protein myeloid differentiation factor 2 (MD-2) represents a useful approach for down-regulation of MD-2·TLR4-mediated innate immune signaling, which is implicated in the pathogenesis of a variety of human diseases, including sepsis syndrome. The antagonistic activity of a series of novel synthetic tetraacylated bis-phosphorylated glycolipids based on the ?GlcN(1?1)?GlcN scaffold was assessed in human monocytic macrophage-like cell line THP-1, dendritic cells and human epithelial cells. Two compounds were shown to inhibit efficiently the LPS-induced inflammatory signaling by down-regulation of the expression of TNF-?, IL-6, IL-8, IL-10 and IL-12 to background levels. The binding of the tetraacylated by (R)-3-hydroxy-fatty acids (2?×?C12, 2?×?C14), 4,4'-bisphosphorylated ?GlcN(1?1)?GlcN-based lipid A mimetic DA193 to human MD-2 was calculated to be 20-fold stronger than that of Escherichia coli lipid A. Potent antagonistic activity was related to a specific molecular shape induced by the ?,?(1?1)-diglucosamine backbone. 'Co-planar' relative arrangement of the GlcN rings was inflicted by the double exo-anomeric conformation around both glycosidic torsions in the rigid ?,?(1?1) linkage, which was ascertained using NOESY NMR experiments and confirmed by molecular dynamics simulation. In contrast to the native lipid A ligands, the binding affinity of ?GlcN(1?1)?GlcN-based lipid A mimetics to human MD-2 was independent on the orientation of the diglucosamine backbone of the synthetic antagonist within the binding pocket of hMD-2 (rotation by 180°) allowing for two equally efficient binding modes as shown by molecular dynamics simulation. Twit Text FOAVip Anti-endotoxic activity and structural basis for human MD-2·TLR4 antagonism of tetraacylated lipid A mimetics based on GlcN(1 1) GlcN scaffold ????Innate Immun http://www.kidney.de/pget.php?&tw=1&pmid=25394365 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25394365 #FOAvip English Wikipedia <ref>{{Cite pmid|25394365 }}</ref> Anti-endotoxic activity and structural basis for human MD-2·TLR4 antagonism of tetraacylated lipid A mimetics based on ?GlcN(1?1)?GlcN scaffold #MMPMID25394365 Garate JA ; Stöckl J ; Fernández-Alonso Mdel C ; Artner D ; Haegman M ; Oostenbrink C ; Jiménez-Barbero J ; Beyaert R ; Heine H ; Kosma P ; Zamyatina A Innate Immun 2015[Jul]; 21 (5 ): 490-503 PMID25394365 show ga Interfering with LPS binding by the co-receptor protein myeloid differentiation factor 2 (MD-2) represents a useful approach for down-regulation of MD-2·TLR4-mediated innate immune signaling, which is implicated in the pathogenesis of a variety of human diseases, including sepsis syndrome. The antagonistic activity of a series of novel synthetic tetraacylated bis-phosphorylated glycolipids based on the ?GlcN(1?1)?GlcN scaffold was assessed in human monocytic macrophage-like cell line THP-1, dendritic cells and human epithelial cells. Two compounds were shown to inhibit efficiently the LPS-induced inflammatory signaling by down-regulation of the expression of TNF-?, IL-6, IL-8, IL-10 and IL-12 to background levels. The binding of the tetraacylated by (R)-3-hydroxy-fatty acids (2?×?C12, 2?×?C14), 4,4'-bisphosphorylated ?GlcN(1?1)?GlcN-based lipid A mimetic DA193 to human MD-2 was calculated to be 20-fold stronger than that of Escherichia coli lipid A. Potent antagonistic activity was related to a specific molecular shape induced by the ?,?(1?1)-diglucosamine backbone. 'Co-planar' relative arrangement of the GlcN rings was inflicted by the double exo-anomeric conformation around both glycosidic torsions in the rigid ?,?(1?1) linkage, which was ascertained using NOESY NMR experiments and confirmed by molecular dynamics simulation. In contrast to the native lipid A ligands, the binding affinity of ?GlcN(1?1)?GlcN-based lipid A mimetics to human MD-2 was independent on the orientation of the diglucosamine backbone of the synthetic antagonist within the binding pocket of hMD-2 (rotation by 180°) allowing for two equally efficient binding modes as shown by molecular dynamics simulation. |Binding Sites [MESH] |Cell Line [MESH] |Cytokines/biosynthesis [MESH] |Dendritic Cells/drug effects/metabolism [MESH] |Endotoxins/*antagonists & inhibitors [MESH] |Epithelial Cells/drug effects [MESH] |Escherichia coli/chemistry [MESH] |Glucosamine/chemistry/pharmacology [MESH] |Humans [MESH] |Immunity, Innate/immunology [MESH] |Lipid A/*analogs & derivatives/chemistry/*pharmacology [MESH] |Lipopolysaccharides/metabolism [MESH] |Lymphocyte Antigen 96/*antagonists & inhibitors/chemistry/metabolism [MESH] |Molecular Conformation [MESH] |Signal Transduction/physiology [MESH]Anti-endotoxic activity and structural basis for human MD-2·TLR4 antag(epmc).pdf DeepDyve Pubget Overpricing