Subrata Adak
Department of Immunology
Lerner Research Institute
Cleveland Clinic
Cleveland
USA
Name/email consistency: high
- Cloning, expression, and characterization of a nitric oxide synthase protein from Deinococcus radiodurans. Adak, S., Bilwes, A.M., Panda, K., Hosfield, D., Aulak, K.S., McDonald, J.F., Tainer, J.A., Getzoff, E.D., Crane, B.R., Stuehr, D.J. Proc. Natl. Acad. Sci. U.S.A. (2002)
- Direct evidence for nitric oxide production by a nitric-oxide synthase-like protein from Bacillus subtilis. Adak, S., Aulak, K.S., Stuehr, D.J. J. Biol. Chem. (2002)
- A conserved flavin-shielding residue regulates NO synthase electron transfer and nicotinamide coenzyme specificity. Adak, S., Sharma, M., Meade, A.L., Stuehr, D.J. Proc. Natl. Acad. Sci. U.S.A. (2002)
- Neuronal nitric-oxide synthase mutant (Ser-1412 --> Asp) demonstrates surprising connections between heme reduction, NO complex formation, and catalysis. Adak, S., Santolini, J., Tikunova, S., Wang, Q., Johnson, J.D., Stuehr, D.J. J. Biol. Chem. (2001)
- Chimeras of nitric-oxide synthase types I and III establish fundamental correlates between heme reduction, heme-NO complex formation, and catalytic activity. Adak, S., Aulak, K.S., Stuehr, D.J. J. Biol. Chem. (2001)
- Molecular basis for hyperactivity in tryptophan 409 mutants of neuronal NO synthase. Adak, S., Wang, Q., Stuehr, D.J. J. Biol. Chem. (2000)
- Arginine conversion to nitroxide by tetrahydrobiopterin-free neuronal nitric-oxide synthase. Implications for mechanism. Adak, S., Wang, Q., Stuehr, D.J. J. Biol. Chem. (2000)
