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Cited by 818

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Structural basis for signal transduction by the Toll/interleukin-1 receptor domains

Xu, Yingwu, Tao, Xiao, Shen, Baohe, Horng, Tiffany, Medzhitov, Ruslan, Manley, James L., Tong, Liang·2000·Nature
DOI 10.1038/35040600
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Research works printed but not linked: 28

  1. Hoffmann, J. A., Kafatos, F. C., Janeway, C. A. Jr & Ezekowitz, R. A. B. Phylogenetic perspectives in innate immunity. Science 284, 1313–1318 (1999). · DOI · Paper page
  2. Kopp, E. B. & Medzhitov, R. The Toll-receptor family and control of innate immunity. Curr. Opin. Immunol. 11, 13–18 (1999). · DOI · Paper page
  3. Anderson, K. V. Toll signaling pathways in the innate immune response. Curr. Opin. Immunol. 12, 13–19 ( 2000). · DOI · Paper page
  4. Gay, N. J. & Keith, F. J. Drosophila Toll and IL-1 receptor. Nature 351, 355– 356 (1991). · DOI · Paper page
  5. Poltorak, A. et al. Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: mutations in Tlr4 gene. Science 282, 2085 –2088 (1998). · DOI · Paper page
  6. Underhill, D. M. et al. The Toll-like receptor 2 is recruited to macrophage phagosomes and discriminates between pathogens. Nature 401, 811–815 (1999). · DOI · Paper page
  7. Muzio, M., Ji, J., Feng, P. & Dixit, V. M. IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling. Science 278, 1612–1615 ( 1997). · DOI · Paper page
  8. Wesche, H., Henzel, W. J., Shilinglaw, W., Li, S. & Cao, Z. MyD88, an adapter that recruits IRAK to the IL-1 receptor complex. Immunity 7, 837–847 (1997). · DOI · Paper page
  9. Medzhitov, R. et al. MyD88 is an adaptor protein in the hToll/IL-1 receptor family signaling pathways. Mol. Cell 2, 253– 258 (1998). · DOI · Paper page
  10. Burns, K. et al. MyD88, an adapter protein involved in interleukin-1 signaling. J. Biol. Chem. 273, 12203– 12209 (1998). · DOI · Paper page
  11. Eck, M. J., Schoelson, S. E. & Harrison, S. C. Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck. Nature 362, 87–91 (1993). · DOI · Paper page
  12. Mitcham, J. L. et al. T1/ST2 signaling establishes it as a member of an expanding interleukin-1 receptor family. J. Biol. Chem. 271, 5777–5783 (1996). · DOI
  13. Burns, K. et al. Tollip, a new component of the IL-1RI pathway, links IRAK to the IL-1 receptor. Nature Cell Biol. 2, 346–351 (2000). · DOI · Paper page
  14. Norris, J. L. & Manley, J. L. Selective nuclear transport of the Drosophila morphogen dorsal can be established by a signaling pathway involving the transmembrane protein Toll and protein kinase A. Genes Dev. 6, 1654–1667 (1992). · DOI
  15. Slack, J. L. et al. Identification of two major sites in the type I interleukin-1 receptor cytoplasmic region responsible for coupling to pro-inflammatory signaling pathways. J. Biol. Chem. 275, 4670– 4678 (2000). · DOI · Paper page
  16. Huang, B., Eberstadt, M., Olejniczak, E. T., Meadows, R. P. & Fesik, S. W. NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain. Nature 384, 638–641 (1996). · DOI · Paper page
  17. Shen, B. & Manley, J. L. Phosphorylation modulates direct interactions between the Toll receptor, Pelle kinase and Tube. Development 125, 4719–4728 (1998). · DOI
  18. Du, X., Poltorak, A., Silva, M. & Beutler, B. Analysis of Tlr4-mediated LPS signal transduction in macrophages by mutational modification of the receptor. Blood Cells Mol. Dis. 25, 328– 338 (1999). · DOI
  19. Rock, F. L., Hardiman, G., Timans, J. C., Kastelein, R. A. & Bazan, J. F. A family of human receptors structurally related to Drosophila Toll. Proc. Natl Acad. Sci. USA 95, 588–593 (1998). · DOI · Paper page
  20. Stock, J. B., Stock, A. M. & Mottonen, J. M. Signal transduction in bacteria. Nature 344, 395–400 ( 1990). · DOI · Paper page
  21. Otwinowski, Z. & Minor, W. processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307–326 ( 1997). · DOI · Paper page
  22. Hendrickson, W. A. Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254, 51– 58 (1991). · DOI · Paper page
  23. Furey, W. & Swaminathan, S. PHASES-95: A program package for processing and analyzing diffraction data from macromolecules. Methods Enzymol. 277, 590–620 (1997). · DOI · Paper page
  24. Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110–119 (1991). · DOI · Paper page
  25. Brunger, A. et al. Crystallography & NMR System: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905–921 (1998). · DOI · Paper page
  26. Tong, L. Combined molecular replacement. Acta Crystallogr. A 52, 905–921 (1998).
  27. Carson, M. Ribbon models of macromolecules. J. Mol. Graph. 5, 103–106 (1987). · DOI · Paper page
  28. Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281–296 (1991). · DOI

Cited by

Metadata

Authors
Xu, Y., Tao, X., Shen, B., Horng, T., Medzhitov, R., Manley, J. L., & Tong, L.
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
2000-11
Volume
408
Issue
6808
Pages
111-115
ISSN
  • 0028-0836 (ISSN-L)
  • 1476-4687
DOI
10.1038/35040600
OpenAlex
W2147038697
Cited by
818
References
1
FWCI
11.70
Type
journal article
Language
en
Open access
closed
Licence
www.springer.com/tdm (tdm)

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