User menu

Engineering Allosteric Regulation into Biological Catalysts

Bibliographic reference Fastrez, Jacques. Engineering Allosteric Regulation into Biological Catalysts. In: ChemBioChem : a European journal of chemical biology, Vol. 10, no. 18, p. 2824-2835 (2009)
Permanent URL http://hdl.handle.net/2078.1/34295
  1. Monod J., Jacob F., General Conclusions: Teleonomic Mechanisms in Cellular Metabolism, Growth, and Differentiation, 10.1101/sqb.1961.026.01.048
  2. Fenton, Trends Biochem. Sci., 33, 420 (2008)
  3. Kuriyan, Nature, 450, 983 (2007)
  4. Monod, J. Mol. Biol., 12, 88 (1965)
  5. Koshland, Biochemistry, 5, 365 (1966)
  6. M. Eigen, Nobel Symp. 1967, 5, 333–369.
  7. Cooper, Eur. Biophys. J., 11, 103 (1984)
  8. Goodey, Nat. Chem. Biol., 4, 474 (2008)
  9. Cui, Protein Sci., 17, 1295 (2008)
  10. Gunasekaran, Proteins, 57, 433 (2004)
  11. Hilser, Proc. Natl. Acad. Sci. USA, 95, 9903 (1998)
  12. Hardy, Curr. Opin. Struct. Biol., 14, 706 (2004)
  13. Süel, Nat. Struct. Biol., 10, 59 (2003)
  14. Ota, J. Mol. Biol., 351, 345 (2005)
  15. Brüschweiler, J. Am. Chem. Soc., 131, 3063 (2009)
  16. Smith, Chem. Rev., 97, 391 (1997)
  17. Binz, Nat. Biotechnol., 23, 1257 (2005)
  18. Fedor, Annu. Rev. Biophys., 38, 271 (2009)
  19. Fiammengo, Curr. Opin. Biotechnol., 16, 614 (2005)
  20. Cech, Science, 289, 878 (2000)
  21. Lipscomb, Adv. Enzymol. Relat. Areas Mol. Biol. Vol. 68, 67 (1994)
  22. Wales, J. Mol. Biol., 294, 1387 (1999)
  23. Cunin, J. Mol. Biol., 294, 1401 (1999)
  24. Komiyama, Nature, 373, 244 (1995)
  25. Pawlyk, Proc. Natl. Acad. Sci. USA, 99, 11115 (2002)
  26. Luque, Proteins, 4, 63 (2000)
  27. Dang, Proc. Natl. Acad. Sci. USA, 93, 10653 (1996)
  28. Page, J. Mol. Biol., 378, 666 (2008)
  29. Perona, Biochemistry, 34, 1489 (1995)
  30. Ikeda, J. Biol. Chem., 275, 9150 (2000)
  31. Santamaría, J. Biol. Chem., 277, 1210 (2002)
  32. Safo, Acta Crystallogr., D58, 634 (2002)
  33. Pargellis, Nat. Struct. Biol., 9, 268 (2002)
  34. Lawrence, Chem. Biol., 15, 586 (2008)
  35. Matsumura, Science, 243, 792 (1989)
  36. Higaki, Biochemistry, 29, 8582 (1990)
  37. McGrath, Biochemistry, 32, 1914 (1993)
  38. Tanaka, Biosci. Biotechnol. Biochem., 64, 2008 (2000)
  39. Browner, Nat. Struct. Biol., 1, 327 (1994)
  40. Mandecki, Protein Eng., 4, 801 (1991)
  41. Brennan, Proc. Natl. Acad. Sci. USA, 92, 5783 (1995)
  42. Benito, J. Biol. Chem., 271, 21251 (1996)
  43. Feliu, FEBS Lett., 438, 267 (1998)
  44. Ferrer-Miralles, J. Biol. Chem., 276, 40087 (2001)
  45. Blouse, J. Biol. Chem., 284, 4647 (2009)
  46. Saghatelian, J. Am. Chem. Soc., 125, 344 (2003)
  47. Kobe, Nature, 402, 373 (1999)
  48. Yousef, Proc. Natl. Acad. Sci. USA, 101, 11583 (2004)
  49. Krishna, Proc. Natl. Acad. Sci. USA, 102, 1053 (2005)
  50. Lee, Science, 322, 438 (2008)
  51. Fastrez, Mol. Biotechnol., 7, 37 (1997)
  52. Legendre, Nat. Biotechnol., 17, 67 (1999)
  53. Legendre, Protein Sci., 11, 1506 (2002)
  54. Mathonet, Protein Sci., 15, 2323 (2006)
  55. Hamers-Casterman, Nature, 363, 446 (1993)
  56. Mathonet, Protein Sci., 15, 2335 (2006)
  57. Savard, Biochemistry, 45, 11414 (2006)
  58. Guntas, J. Mol. Biol., 336, 263 (2004)
  59. Guntas, Chem. Biol., 11, 1483 (2004)
  60. Kim, Arch. Biochem. Biophys., 446, 44 (2006)
  61. Guntas, Proc. Natl. Acad. Sci. USA, 102, 11224 (2005)
  62. Looger, Nature, 423, 185 (2003)
  63. Marvin, Proc. Natl. Acad. Sci. USA, 98, 4955 (2001)
  64. Liang, Protein Sci., 16, 929 (2007)
  65. Edwards, Nucleic Acids Res., 36, 78 (2008)
  66. Paulus, Annu. Rev. Biochem., 69, 447 (2000)
  67. Buskirk, Proc. Natl. Acad. Sci. USA, 101, 10505 (2004)
  68. Yuen, J. Am. Chem. Soc., 128, 8939 (2006)
  69. Skretas, Protein Sci., 14, 523 (2005)
  70. Famulok, Chem. Rev., 107, 3715 (2007)
  71. Liu, Chem. Rev., 109, 1948 (2009)
  72. Sassanfar, Nature, 364, 550 (1993)
  73. Tuschl, Proc. Natl. Acad. Sci. USA, 90, 6991 (1993)
  74. Long, Proc. Natl. Acad. Sci. USA, 91, 6977 (1994)
  75. Tang, Chem. Biol., 4, 453 (1997)
  76. Tang, Nucleic Acids Res., 26, 4214 (1998)
  77. Araki, Nucleic Acids Res., 26, 3379 (1998)
  78. Soukup, Proc. Natl. Acad. Sci. USA, 96, 3584 (1999)
  79. Koizumi, Nat. Struct. Biol., 6, 1062 (1999)
  80. Jose, Nucleic Acids Res., 29, 1631 (2001)
  81. Hall, Biosens. Bioelectron., 22, 1939 (2007)
  82. Hartig, Nat. Biotechnol., 20, 717 (2002)
  83. Walter, Nat. Struct. Biol., 6, 544 (1999)
  84. Bock, Nature, 355, 564 (1992)
  85. Najafi-Shoushtari, Blood Cells Mol. Dis., 38, 19 (2007)
  86. Najafi-Shoushtari, Nucleic Acids Res., 32, 3212 (2004)
  87. Najafi-Shoushtari, RNA, 11, 1514 (2005)
  88. Robertson, Nucleic Acids Res., 28, 1751 (2000)
  89. Amontov, Nucleic Acids Res., 34, 5032 (2006)
  90. Liu, Proc. Natl. Acad. Sci. USA, 104, 2056 (2007)
  91. Liu, Angew. Chem., 119, 7731 (2007)
  92. Angew. Chem. Int. Ed. 2007, 46, 7587–7590.
  93. Yen, Nature, 431, 471 (2004)
  94. Winkler, Nature, 428, 281 (2004)
  95. Zhao, Curr. Opin. Struct. Biol., 7, 480 (1997)
  96. Breaker, RNA, 9, 949 (2003)
  97. Swain, Curr. Opin. Struct. Biol., 16, 102 (2006)
  98. Gianneschi, Angew. Chem., 116, 5619 (2004)
  99. Angew. Chem. Int. Ed. 2004, 43, 5503–5507 (and references therein).