Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
First Independent Research Support & Transition (FIRST) Awards (R29)
Project #
1R29CA053914-01
Application #
3460126
Study Section
Biochemistry Study Section (BIO)
Project Start
1991-01-01
Project End
1991-02-28
Budget Start
1991-01-01
Budget End
1991-02-28
Support Year
1
Fiscal Year
1991
Total Cost
Indirect Cost
Name
Weill Medical College of Cornell University
Department
Type
Schools of Medicine
DUNS #
201373169
City
New York
State
NY
Country
United States
Zip Code
10065
Hannibal, Luciana; Page, Richard C; Haque, Mohammad Mahfuzul et al. (2015) Dissecting structural and electronic effects in inducible nitric oxide synthase. Biochem J 467:153-65
Sabat, Joseph; Egawa, Tsuyoshi; Lu, Changyuan et al. (2013) Catalytic intermediates of inducible nitric-oxide synthase stabilized by the W188H mutation. J Biol Chem 288:6095-106
Nagpal, Latika; Haque, Mohammad M; Saha, Amit et al. (2013) Mechanism of inducible nitric-oxide synthase dimerization inhibition by novel pyrimidine imidazoles. J Biol Chem 288:19685-97
Haque, Mohammad Mahfuzul; Fadlalla, Mohammed A; Aulak, Kulwant S et al. (2012) Control of electron transfer and catalysis in neuronal nitric-oxide synthase (nNOS) by a hinge connecting its FMN and FAD-NADPH domains. J Biol Chem 287:30105-16
Wang, Zhi-Qiang; Tejero, Jesús; Wei, Chin-Chuan et al. (2012) Arg375 tunes tetrahydrobiopterin functions and modulates catalysis by inducible nitric oxide synthase. J Inorg Biochem 108:203-15
Tejero, Jesus; Biswas, Ashis; Haque, Mohammad Mahfuzul et al. (2011) Mesohaem substitution reveals how haem electronic properties can influence the kinetic and catalytic parameters of neuronal NO synthase. Biochem J 433:163-74
Hannibal, Luciana; Somasundaram, Ramasamy; Tejero, Jesús et al. (2011) Influence of heme-thiolate in shaping the catalytic properties of a bacterial nitric-oxide synthase. J Biol Chem 286:39224-35
Ghosh, Arnab; Chawla-Sarkar, Mamta; Stuehr, Dennis J (2011) Hsp90 interacts with inducible NO synthase client protein in its heme-free state and then drives heme insertion by an ATP-dependent process. FASEB J 25:2049-60
Tejero, Jesús; Haque, Mohammad Mahfuzul; Durra, Deborah et al. (2010) A bridging interaction allows calmodulin to activate NO synthase through a bi-modal mechanism. J Biol Chem 285:25941-9
Tejero, Jesús; Hannibal, Luciana; Mustovich, Anthony et al. (2010) Surface charges and regulation of FMN to heme electron transfer in nitric-oxide synthase. J Biol Chem 285:27232-40

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