ArticleProceedings of the National Academy of Sciences of the United States of America2009
Structural basis for the multiple interactions of the MyD88 TIR domain in TLR4 signaling.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.
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Who cites it
101 citing papers in PubMed.
- Review
- Roles of TIR domain-containing adaptor protein in tumor: Inflammation and immune regulation via toll-like receptor signaling.The Journal of international medical research · 2026Review
- MyD88 self-assembles into supramolecular filaments to amplify NF-κB signaling.Fundamental research · 2026Article
- Zfand5 terminates TLR3/4 signaling and necroptosis by targeting TRIF to the proteasome for degradation.Cell death & disease · 2026Article
- Structural Mechanism of Receptor-Triggered MyD88 Oligomeric Assembly in Innate Immune Signaling.Nature communications · 2026Article
- Protective effect of hesperetin against myelosuppression and splenic inflammation via modulating TLR4/MYD88/NF-κB signaling: molecular docking and experimental validation.Frontiers in pharmacology · 2026Article
- Tissue macrophages: origin, heterogenity, biological functions, diseases and therapeutic targets.Signal transduction and targeted therapy · 2025Review
- In silico analysis of Triphala-derived polyphenols as inhibitors of TIR-TIR homodimerization in the inflammatory pathway.Frontiers in bioinformatics · 2025Article
- Acetylation of TIR domains in the TLR4-Mal-MyD88 complex regulates immune responses in sepsis.The EMBO journal · 2024Article
- Review
- Targeting Myeloid Differentiation Primary Response Protein 88 (MyD88) and Galectin-3 to Develop Broad-Spectrum Host-Mediated Therapeutics against SARS-CoV-2.International journal of molecular sciences · 2024Review
- Ammonia transporter RhBG initiates downstream signaling and functional responses by activating NFκB.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- TIR domains of TLR family-from the cell culture to the protein sample for structural studies.PloS one · 2024Article
- Microbial Pathogenesis in the Era of Spatial Omics.Infection and immunity · 2023Review
- Lipopolysaccharide detection by the innate immune system may be an uncommon defence strategy used in nature.Open biology · 2022Review
- Article
- A Structural Perspective on Calprotectin as a Ligand of Receptors Mediating Inflammation and Potential Drug Target.Biomolecules · 2022Review
- Integrating Network Pharmacology and Experimental Validation to Explore the Key Mechanism of Gubitong Recipe in the Treatment of Osteoarthritis.Computational and mathematical methods in medicine · 2022Article
- Article
- Modulation of Toll-like receptor 1 intracellular domain structure and activity by ZnCommunications biology · 2021Article
41 more citing papers are in PubMed but not listed here.
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9 authors.
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Abstract
Myeloid differentiating factor 88 (MyD88) and MyD88 adaptor-like (Mal) are adaptor molecules critically involved in the Toll-like receptor (TLR) 4 signaling pathway. While Mal has been proposed to serve as a membrane-sorting adaptor, MyD88 mediates signal transduction from activated TLR4 to downstream components. The Toll/Interleukin-1 receptor (TIR) domain of MyD88 is responsible for sorting and signaling via direct or indirect TIR-TIR interactions between Mal and TLR4. However, the molecular mechanisms involved in multiple interactions of the TIR domain remain unclear. The present study describes the solution structure of the MyD88 TIR domain. Reporter gene assays revealed that 3 discrete surface sites in the TIR domain of MyD88 are important for TLR4 signaling. Two of these sites were shown to mediate direct binding to the TIR domain of Mal. Interestingly, Mal-TIR, but not MyD88-TIR, directly binds to the cytosolic TIR domain of TLR4. These observations suggested that the heteromeric assembly of TIR domains of the receptor and adaptors constitutes the initial step of TLR4 intracellular signal transduction.
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