Biologically relevant chemical properties of peroxymonophosphate ({double bond, long}O3POOH)

Bioorganic and Medicinal Chemistry Letters

Volumn 19, Issue 1, 2009, Pages 218-221

  LaButti, Jason N ^a   Gates, Kent S ^a  

^a UNIVERSITY OF MISSOURI   (United States)

Author keywords

Protein tyrosine phosphatase; Signal transduction

Indexed keywords

HYDROGEN PEROXIDE; PEROXYMONOPHOSPHATE; PROTEIN TYROSINE PHOSPHATASE; UNCLASSIFIED DRUG;

ARTICLE; ENZYME INACTIVATION; MASS SPECTROMETRY; PHOSPHORUS NUCLEAR MAGNETIC RESONANCE; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS;

ANIMALS; DRUG STABILITY; HYDROGEN PEROXIDE; PHOSPHATES; PROTEIN TYROSINE PHOSPHATASES;

EID: 57749090147     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2008.10.133     Document Type: Article

References (34)

1. Rhee S.G. Science 312 (2006) 1882
2. Lambeth J.D., Kawahara T., and Diebold B. Free Radical Biol. Med. 43 (2007) 319
3. Denu J.M., and Tanner K.G. Biochemistry 37 (1998) 5633
4. Sivaramakrishnan S., Keerthi K., and Gates K.S. J. Am. Chem. Soc. 127 (2005) 10830
5. Xu D., Rovira I.I., and Finkel T. Dev. Cell 2 (2002) 251
6. den Hertog J., Groen A., and van der Wijk T. Arch. Biochem. Biophys. 434 (2005) 11
7. Alonso A., Sasin J., Bottini N., Friedberg I., Ostermann A., Godzik A., Hunter T., Dixon J.E., and Mustelin T. Cell 117 (2004) 699
8. Hunter T. Cell 100 (2000) 113
9. Tonks N.K. Nat. Rev. Cell. Biol. 7 (2006) 833
10. Salmeen A., Anderson J.N., Myers M.P., Meng T.-C., Hinks J.A., Tonks N.K., and Barford D. Nature 423 (2003) 769
11. van Montfort R.L.M., Congreeve M., Tisi D., Carr R., and Jhoti H. Nature 423 (2003) 773
12. Mahedev K., Zilbering A., Zhu L., and Goldstein B.J. J. Biol. Chem. 276 (2001) 21938
13. Meng T.-C., Fukada T., and Tonks N.K. Mol. Cell 9 (2002) 387
14. Stone J.R. Arch. Biochem. Biophys. 422 (2004) 119
15. Ushio-Fukai M. Science STKE 349 (2006) 1
16. Chen K., Kirber M.T., Yang Y., and Keaney J.F.J. J. Cell Biol. 181 (2008) 1129
17. LaButti J.N., Chowdhury G., Reilly T.J., and Gates K.S. J. Am. Chem. Soc. 129 (2007) 5320
18. Knowles J.R. Annu. Rev. Biochem. 49 (1980) 877
19. Hershlag D., and Jencks W.P. J. Am. Chem. Soc. 112 (1990) 1951
20. Battaglia C.J., and Edward J.O. Inorg. Chem. 4 (1965) 552
21. Griffith W.P., Powell R.D., and Skapski A.C. Polyhedron 7 (1988) 1305
22. 31P NMR, see:. Lerman C.L., and Cohn M. J. Biol. Chem. 255 (1980) 8756
23. Zhu T., Chang H.-m., and Kadla J.F. Can. J. Chem. 81 (2003) 156
24. Miller E.W., Tulyanthan O., Isacoff E.Y., and Chang C.J. Nat. Chem. Biol. 3 (2007) 263
25. Secco F., and Venturini M. J. Chem. Soc., Dalton Trans. (1976) 1410
26. Halliwell B., and Gutteridge J.M.C. Methods Enzymol. 186 (1990) 1
27. Zhao B., and Chasteen N.D. Anal. Biochem. 349 (2006) 262
28. Winterbourn C.C., and Metodiewa D. Free Radical Biol. Med. 27 (1999) 322
29. Richardson D.E., Regino C.A.S., Yao H., and Johnson J.V. Free Radical Biol. Med. 35 (2003) 1538
30. Thenraja D., Subramaniam P., and Srinivasan C. Tetrahedron 58 (2002) 4283
31. Ghanem R., Carmona C., Muñoz M.A., Guardado P., and Balón M. J. Chem. Soc., Perkin Trans. 2 (1996) 2197
32. Suthakaran R., Rajagopal S., and Srinivasan C. Tetrahedron 57 (2001) 1369
33. Hara I., Ichise N., Kojima K., Kondo H., Ohgiya S., Matsuyama H., and Yumoto I. Biochemistry 46 (2007) 11
34. Pichorner H., Jessner G., and Ebermann R. Arch. Biochem. Biophys. 300 (1993) 258