Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran.

By Ho Min Kim, B. Park, Jung-In Kim, Sung Eun Kim, Judong Lee, Se Cheol Oh, P. Enkhbayar, N. Matsushima, Hayyoung Lee, O. Yoo and 1 more. Cell, 2007

1,194 citations recorded by the source corpus.

Subfields: Cancer Research, Immunology, Microbiology

View Paper: https://www.semanticscholar.org/paper/6ef1f33227d883bfa86e1801daaccb3ddd69d2e1

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In Cancer Research

1. Shizuo Akira
2. Luke A. O'Neill
3. Jonathan C. Kagan
4. Taro Kawai
5. G. Barton
6. Himanshu Kumar
7. R. Medzhitov
8. K. Takeda

In Immunology

1. Shizuo Akira
2. Taro Kawai
3. Jonathan C. Kagan
4. Luke A. O'Neill
5. G. Barton
6. Himanshu Kumar
7. R. Medzhitov
8. Jie-Oh Lee

In Microbiology

1. Shizuo Akira
2. Taro Kawai
3. G. Barton
4. Jonathan C. Kagan
5. R. Medzhitov

Citations in the corpus

• Pathogen Recognition by the Innate Immune System (2011, background): “Therefore, lipid A activates the TLR4 signaling pathway, but Eritoran does not [13, 14].”
• The interleukin‐1 receptor/Toll‐like receptor superfamily: 10 years of progress (2008, background): “A structure for the LPS antagonist eritoran bound to MD2 in complex with TLR4 has also been solved (64).”
• Variation in Microbiome LPS Immunogenicity Contributes to Autoimmunity in Humans. (2016, neutral): “Specifically, the lipid A domain of LPS is responsible for immune signaling through recognition and activation of the Toll-like receptor 4 (TLR4) complex (Kim et al., 2007); as such, structural changes in lipid A impact recognition by TLR4 and influence multiple facets of microbial ecology (Cullen e”
• Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like receptor 6 heterodimer. (2009, methodology): “Recently, the extracellular domains of several TLRs with and without bound ligands have been crystallized and their structures have been reported (Bell et al., 2005; Choe et al., 2005; Jin et al., 2007; Kim et al., 2007b; Liu et al., 2008; Park et al., 2009).”
• The Structural Biology of Toll-Like Receptors (2011, background): “To facilitate crystallization and structure determination the LRR-CT and the last one or two LRRs of TLRs 1, 2, and 6 were replaced by corresponding regions of a hagfish VLR (Table 2) (Kim et al., 2007).”
• Tenascin-C is an endogenous activator of Toll-like receptor 4 that is essential for maintaining inflammation in arthritic joint disease (2009, background): “Crystallization of the TLR4 ectodomain, MD-2 and the LPS analog eritoran in complex supports data that LPS does not bind TLR4 directl”