IndraLab

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TLR4 binds NAMPT. 17 / 18
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"Furthermore, visfatin has been associated with the innate immune receptor toll-like receptor 4 (TLR4), which plays a key role in cartilage and bone inflammatory and catabolic responses."
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"This is in keeping with both the SPR results, showing that the protein strongly binds to the receptor in the absence of MD2, and the docking results, revealing that NAMPT interacts with TLR4 in its concave surface, similarly to MD2 ( xref )."
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"Our analysis of the structure of the MD-2 and LPS complex, however, indicates that LPS binding to TLR4 maps to the protruding region of NAMPT and PBEF (S402-N412), suggesting that NAMPT and PBEF may intrinsically adopt a conformation capable of direct TLR4 binding and activation."
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"The minimized model for the NAMPT–TLR4 complex ( xref ) confirms the role of the NAMPT-positive patches, showing the presence of stabilizing electrostatic interactions between Lys residues 48, 68, 71, 73 and TLR4 negatively charged carboxylic moieties ( xref )."
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"NAMPT binds TLR4 in a concentration-dependent manner, with an equilibrium dissociation constant (K D ) of about 18 nM ( xref and xref )."
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"Our group recently confirmed the binding of eNAMPT to TLR4 in macrophage cellular model ( xref ), performing surface plasmon resonance (SPR) under the same conditions previously established for the NAMPT-TLR4 interaction ( xref )."
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"Furthermore, the extracellular binding of NAMPT to toll-like receptor 4 (TLR4) results in NF-κB phosphorylation and activation, providing information on protein functionality [ xref ]."
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"To further gain insights into NAMPT–TLR4 interaction we performed molecular docking between TLR4 homodimer and NAMPT homodimer."
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"Furthermore, the extracellular binding of NAMPT to toll like receptor 4 (TLR4) results in NF-kappaB phosphorylation and activation, providing information on protein functionality [XREF_BIBR]."
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"Using an integrated approach combining bioinformatics and functional and structural analyses, we investigated the interaction between NAMPT and TLR4 at the molecular level."
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"To shed light on the molecular NAMPT–TLR4 interaction, we started from the evidence that bacterial NAMPT does not act as a cytokine ( xref )."
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"Finally, the involvement of the two loops in receptor binding was supported by NAMPT-TLR4 docking simulations."
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"The kinetics of the binding of wild-type and mutated NAMPT to biosensor-tethered TLR4 was analyzed."
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"Molecular docking studies on NAMPT–TLR4 interaction."
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"Here, we have analyzed the kinetics of the NAMPT–TLR4 complex formation by assessing the direct binding of NAMPT to immobilized TLR4."
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"Molecular Insights Into The Interaction Between Human Nicotinamide Phosphoribosyltransferase and Toll-Like Receptor 4."
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"The extracellular form of NAMPT (eNAMPT) binds TLR4, triggering an inflammatory response and so acting as a damage-induced molecular marker."
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