The Relative Influence of Metal Ion Binding Sites in the I-like Domain and the Interface with the Hybrid Domain on Roll… (2025)

1. JianFeng Chen
2. Junichi Takagi
3. Can Xie
4. Tsan Xiao
5. Bing-Hao Luo
6. Timothy A. Springer

1. Hynes, Cell, № 110, с. 673
   https://doi.org/10.1016/S0092-8674(02)00971-6
2. Takagi, Immunol. Rev., № 186, с. 141
   https://doi.org/10.1034/j.1600-065X.2002.18613.x
3. Kim, Science, № 301, с. 1720
   https://doi.org/10.1126/science.1084174
4. Giancotti, Science, № 285, с. 1028
   https://doi.org/10.1126/science.285.5430.1028
5. Takagi, Cell, № 110, с. 599
   https://doi.org/10.1016/S0092-8674(02)00935-2
6. Vinogradova, Cell, № 110, с. 587
   https://doi.org/10.1016/S0092-8674(02)00906-6
7. Takagi, EMBO J., № 22, с. 4607
   https://doi.org/10.1093/emboj/cdg445
8. Xiao, T., Takagi, J., Wang, J.-h., Coller, B. S., and Springer, T. A. (2004) 432, 59–67
   https://doi.org/10.1038/nature02976
9. Luo, Proc. Natl. Acad. Sci. U. S. A., № 100, с. 2403
   https://doi.org/10.1073/pnas.0438060100
10. Luo, J. Biol. Chem., № 279, с. 27466
    https://doi.org/10.1074/jbc.M404354200
11. Mould, J. Biol. Chem., № 278, с. 17028
    https://doi.org/10.1074/jbc.M213139200
12. Luo, J. Biol. Chem., № 279, с. 10215
    https://doi.org/10.1074/jbc.M312732200
13. Yang, Proc. Natl. Acad. Sci. U. S. A., № 101, с. 2333
    https://doi.org/10.1073/pnas.0307291101
14. Springer, с. 29
15. Chen, Nat. Struct. Biol., № 10, с. 995
    https://doi.org/10.1038/nsb1011
16. de Chateau, Biochemistry, № 40, с. 13972
    https://doi.org/10.1021/bi011582f
17. Berlin, Cell, № 80, с. 413
    https://doi.org/10.1016/0092-8674(95)90491-3
18. Xiong, Science, № 296, с. 151
    https://doi.org/10.1126/science.1069040
19. Xiong, Science, № 294, с. 339
    https://doi.org/10.1126/science.1064535
20. Lazarovits, J. Immunol., № 133, с. 1857
    https://doi.org/10.4049/jimmunol.133.4.1857
21. Schweighoffer, J. Immunol., № 151, с. 717
    https://doi.org/10.4049/jimmunol.151.2.717
22. Tidswell, J. Immunol., № 159, с. 1497
    https://doi.org/10.4049/jimmunol.159.3.1497
23. Lu, J. Biol. Chem., № 273, с. 15138
    https://doi.org/10.1074/jbc.273.24.15138
24. Luo, PLoS Biol., № 2, с. 776
25. Lawrence, Cell, № 65, с. 859
    https://doi.org/10.1016/0092-8674(91)90393-D
26. Salas, J. Biol. Chem., № 277, с. 50255
    https://doi.org/10.1074/jbc.M209822200
27. Brunger, Acta Crystallogr. Sect. D, № 54, с. 905
    https://doi.org/10.1107/S0907444998003254
28. Holzmann, EMBO J., № 8, с. 1735
    https://doi.org/10.1002/j.1460-2075.1989.tb03566.x
29. Teixido, J. Biol. Chem., № 267, с. 1786
    https://doi.org/10.1016/S0021-9258(18)46014-0
30. Parker, J. Biol. Chem., № 268, с. 7028
    https://doi.org/10.1016/S0021-9258(18)53141-0
31. Hemler, Immunol. Rev., № 114, с. 45
    https://doi.org/10.1111/j.1600-065X.1990.tb00561.x
32. Sanchez-Madrid, Eur. J. Immunol., № 16, с. 1343
    https://doi.org/10.1002/eji.1830161106
33. McIntyre, J. Biol. Chem., № 264, с. 13745
    https://doi.org/10.1016/S0021-9258(18)80063-1
34. Bednarczyk, J. Biol. Chem., № 267, с. 25274
    https://doi.org/10.1016/S0021-9258(19)74036-8
35. Bergeron, Biochem. J., № 373, с. 475
    https://doi.org/10.1042/bj20021630
36. Mould, J. Biol. Chem., № 278, с. 39993
    https://doi.org/10.1074/jbc.M304627200
37. Salas, Immunity, № 20, с. 393
    https://doi.org/10.1016/S1074-7613(04)00082-2

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