Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase

Nature

Volumn 351, Issue 6329, 1991, Pages 714-718

  Bredt, David S ^a   Hwang, Paul M ^a   Glatt, Charles E ^a   Lowenstein, Charles ^a   Reed, Randall R ^a,b   Snyder, Solomon H ^a  

^a DEPARTMENT OF PATHOLOGY   (United States)

^b JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME P450 REDUCTASE; NITRIC OXIDE SYNTHASE;

ARTICLE; BLOOD VESSEL; BRAIN; CYTOTOXICITY; MACROPHAGE; PHOSPHORYLATION; PRIORITY JOURNAL;

AMINO ACID OXIDOREDUCTASES; AMINO ACID SEQUENCE; ANIMAL; BASE SEQUENCE; BINDING SITES; CALMODULIN; CELL LINE; CEREBELLUM; CLONING, MOLECULAR; COMPARATIVE STUDY; DNA; FLAVIN MONONUCLEOTIDE; FLAVIN-ADENINE DINUCLEOTIDE; GENE EXPRESSION; HUMAN; MOLECULAR SEQUENCE DATA; NADP; NADPH-FERRIHEMOPROTEIN REDUCTASE; NITRIC-OXIDE SYNTHASE; PHOSPHORYLATION; RATS; RNA, MESSENGER; SEQUENCE HOMOLOGY, NUCLEIC ACID; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.; TISSUE DISTRIBUTION; TRANSFECTION;

EID: 0025802065     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/351714a0     Document Type: Article

References (48)

1. Moncada, S., Palmer, R. M. J. & Higgs, E. A. Biochem. Pharmal. 38, 1709-1713 (1989).
2. Furchgott, R. F. & Vanhoutte, P. M. FASEB J. 3, 2007-2018 (1988).
3. Ignarro, L. J. A. Rev. Pharmal. Tox. 30, 535-560 (1990).
4. Hibbs, J. B., Jr., Vavrin, Z. & Taintor, R. R. J. Immun. 138, 550-565 (1987).
5. Bredt, D. S. & Snyder, S. H. Proc. natn. Acad. Sci. U.S.A. 86, 9030-9033 (1989).
6. Garthwaite, J., Garthwaite G., Palmer, R. M. J. & Moncada, S. Eur. J. Pharmacol. 172, 413-416 (1989).
7. Bredt, D. S., Hwang, P. M. & Snyder, S. H. Nature 347, 768-770 (1990).
8. Bult, H. et al. Nature 345, 346-347 (1990).
9. Gillespie, J. S., Liu, X. & Martin, W. Br. J. Pharmac. 98, 1080-1082 (1989).
10. Ramagopal, M. W. & Leighton, H. J. Eur. J. Pharmac. 174, 297-299 (1989).
11. Arnold, W. P., Mittal, C. K., Katsuki, S. & Murad, F. Proc. natn. Acad. Sci. U.S.A. 74, 3203-3207 (1977).
12. Bredt, D. S. & Snyder, S. H. Proc. natn. Acad. Sci. U.S.A. 87, 682-685 (1990).
13. Marietta, M. A., Yoon. P. S. Iyengar, R., Leaf C. D. & Wishnok, J. S. Biochemistry 27, 8706-8711 (1988).
14. Palmer, R. J. M. & Moncada, S. Biochem. biophys. Res. Commun. 158, 348-352 (1989).
15. Kwon, N. S. et al. J. biol. Chem. 265, 13442-13445 (1990).
16. Iyanagi, T. & Mason, H. S. Biochemistry 12, 2297-2308 (1973).
17. Kozak, M. Nucleic Acids Res. 15, 8125-8148 (1987).
18. Snyder, S. H. & Bredt, D. S. Trends pharmacol. Sci. 12, 125-128 (1991).
19. O’Neil, K. T. & DeGrado, W. F. Trends biol. Sci. 15, 59-64 (1990).
20. Kemp, B. E. & Pearson, R. B. Trends biol. Sci. 15, 342-346 (1990).
21. Porter, T. D. & Kasper, C. B. Biochemistry 25, 1682-1687 (1986).
22. Porter, T. D. & Kasper, C. B. Proc. natn. Acad. Sci. U.S.A. 82, 973-977. (1985).
23. Ostrowski, J. et al. J. biol. Chem. 27, 15796-15808 (1989).
24. Newman, B. J. & Gray, J. C. Pl. molec. Biol. 10, 511-520 (1988).
25. Helms, L. F., King, G. D. & Swenson, R. P. Biochem. biophys. Res. Commun. 168, 809-817 (1990).
26. Yabusaki, Y., Murakami, H. & Ohkawa, H. J. Biochem. 103, 1004-1010 (1988).
27. Tayeh, M. A. & Marietta, M. A. J. biol. Chem. 264, 19654-19658 (1989).
28. Kwon, N. S., Nathan C. F. & Stuehr, D. J. J. biol. Chem. 264, 20496-20501 (1989).
29. Mayer, B., John, M. & Bohme, E. FEBS Lett. 277, 215-219 (1990).
30. Nathan, C. F. & Stuehr, D. J. J. natn. Cancer Inst 82, 726-728 (1990).
31. Yui, Y. et al. J. biol. Chem. 266, 3369-3371 (1991).
32. Lu, A. Y. H., Junk, K. W. & Coon, M. J. J. biol. Chem. 244, 3714-3721 (1969).
33. Kapitulnik, J., Gelboin, H. V., Guengerich, F. P. & Jacobowitz, D. M. Neuroscience 20, 829-833 (1987).
34. Warner, M., Kohler, C., Hansson, T. & Gustafsson, J. A. J. Neurochem. 50, 1057-1065 (1988).
35. Haglund, L., Kohler, C., Haaparanta, T., Goldstein, M. & Gustafsson, J. Nature 307, 259-262 (1984).
36. Nakane, M., Ichikawa, M. & Deguchi, T. Brain Res. 273, 9-15 (1983).
37. Dawson, T. M., Bredt, D. S., Fotuhi, M., Hwang, P. M. & Snyder, S. H. Proc. natn. Acad. Sci. US.A. (in the press).
38. Thomas, E. & Pearse, A. G. E. Acta Neuropath. 3, 238-249 (1964).
39. Beal, M. F. et al. Nature 321, 168-171 (1989).
40. Koh, J. -Y., Peters, S. & Choi, D. W. Science 234, 73-76 (1986).
41. Ferrante, R. J. et al. Science 230, 561-563 (1985).
42. Vemura, Y., Kowall, N. W. & Beal, M. F. Ann. Neurol. 27, 620-625 (1990).
43. Dawson, V. L., Dawson, T. M., London, E. D., Bredt, D. S. & Snyder, S. H. Proc. natn. Acad. Sci. U.S.A. (in the press).
44. Pritchett, D. B. et al. Science 242, 1306-1308 (1988).
45. Schultz, G. & Bohme, E. Methods of Enzymatic Analysis 3rd edn Vol 4 (eds Bergmeyer, H. V., Bergmeyer, J. & Grabl, M.) 379-389 (Verlag Chemie, Deerbeach, Florida, 1983).
46. Davis, L. G., Dibner, M. D. & Batley, J. F. Basic Methods in Molecular Biology, 130-135 (Elsevier, New York, 1986).
47. Ross, C. A., MacCumber, M. W., Glatt, C. A. & Snyder, S. H. Proc. natn. Acad. Sci. U.S.A. 86, 2923-2927 (1989).
48. Mizukawa, K., Vincent, S. R., McGeer, P. L. & McGeer, E. G. J. comp. Neurol. 279, 281-311 (1989).