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- W2176481039 endingPage "1362" @default.
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- W2176481039 abstract "Precise functioning and fine-tuning of Toll-like receptor 4 (TLR4) signaling is a critical requirement for the smooth functioning of the innate immune system, since aberrant TLR4 activation causes excessive production of pro-inflammatory cytokines and interferons. This can result in life threatening conditions such as septic shock and other inflammatory disorders. The TRIF-related adaptor molecule (TRAM) adaptor protein is unique to the TLR4 signaling pathway and abrogation of TRAM-mediated TLR4 signaling is a promising strategy for developing therapeutics aimed at disrupting TRAM interactions with other components of the TLR4 signaling complex. The VIPER motif from the vaccinia virus-producing protein, A46 has been reported to disrupt TRAM-TLR4 interactions. We have exploited this information, in combination with homology modeling and docking approaches, to identify a potential binding site on TRAM lined by the BB loop and αC helix. Virtual screening of commercially available small molecules targeting the binding site enabled to short-list 12 small molecules to abrogate TRAM-mediated TLR4 signaling. Molecular dynamics and molecular mechanics calculations have been performed for the analysis of these receptor-ligand interactions." @default.
- W2176481039 created "2016-06-24" @default.
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- W2176481039 creator A5040360818 @default.
- W2176481039 creator A5059972450 @default.
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- W2176481039 date "2015-09-02" @default.
- W2176481039 modified "2023-10-16" @default.
- W2176481039 title "An<i>in silico</i>approach towards the identification of novel inhibitors of the TLR-4 signaling pathway" @default.
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- W2176481039 doi "https://doi.org/10.1080/07391102.2015.1079243" @default.
- W2176481039 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26264972" @default.
- W2176481039 hasPublicationYear "2015" @default.
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