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Analogies and surprising differences between recombinant nitric oxide synthase-like proteins from Staphylococcus aureus and Bacillus anthracis in their interactions with l-arginine analogs and iron ligands.
Salard I, Mercey E, Rekka E, Boucher JL, Nioche P, Mikula I, Martasek P, Raman CS, Mansuy D. Salard I, et al. Among authors: martasek p. J Inorg Biochem. 2006 Dec;100(12):2024-33. doi: 10.1016/j.jinorgbio.2006.09.017. Epub 2006 Sep 28. J Inorg Biochem. 2006. PMID: 17084900
Implications for isoform-selective inhibitor design derived from the binding mode of bulky isothioureas to the heme domain of endothelial nitric-oxide synthase.
Raman CS, Li H, Martásek P, Babu BR, Griffith OW, Masters BS, Poulos TL. Raman CS, et al. Among authors: martasek p. J Biol Chem. 2001 Jul 13;276(28):26486-91. doi: 10.1074/jbc.M102255200. Epub 2001 Apr 30. J Biol Chem. 2001. PMID: 11331290 Free article.
Isothioureas are potent NOS inhibitors, and the structures of the endothelial NOS heme domain complexed with isothioureas bearing small S-alkyl substituents have been determined (Li, H., Raman, C.S., Martasek, P., Kral, V., Masters, B.S.S., and Poulos, T.L. (2000) J …
Isothioureas are potent NOS inhibitors, and the structures of the endothelial NOS heme domain complexed with isothioureas bearing small S-al …
275 results