Zobrazeno 1 - 10
of 55
pro vyhledávání: '"Ramasamy, Somasundaram"'
Publikováno v:
In Nitric Oxide 2011 24(2):102-109
Autor:
Rifkind, Joseph M., Nagababu, Enika, Barbiro-Michaely, Efrat, Ramasamy, Somasundaram, Pluta, Ryszard M., Mayevsky, Avraham
Publikováno v:
In Nitric Oxide 2007 16(4):448-456
Publikováno v:
In Nitric Oxide 2006 15(1):20-29
Autor:
Ramasamy, Somasundaram1, Haque, Mohammad Mahfuzul1, Gangoda, Mahinda2, Stuehr, Dennis J.1 stuehrd@ccf.org
Publikováno v:
FEBS Journal. Dec2016, Vol. 283 Issue 24, p4491-4501. 11p.
Autor:
Nagababu, Enika ‡, Ramasamy, Somasundaram ‡, Abernethy, Darrell R. §, Rifkind, Joseph M. ‡, ¶
Publikováno v:
In Journal of Biological Chemistry 21 November 2003 278(47):46349-46356
Autor:
Rifkind, Joseph M., Abugo, O.O., Nagababu, Enika, Ramasamy, Somasundaram, Demehin, Andrew, Jayakumar, Rajadas
Publikováno v:
In Advances in Cell Aging and Gerontology 2002 11:283-307
Autor:
Michael K. Johnson, Masakazu Hirasawa, Megha Bhalla, David B. Knaff, Ramasamy Somasundaram, Jatindra N. Tripathy, James P. Allen
Publikováno v:
Molecular Plant. 2(3):407-415
A series of site-directed mutants of the ferredoxin-dependent spinach nitrite reductase has been characterized and several amino acids have been identified that appear to be involved in the interaction of the enzyme with ferredoxin. In a complementar
Publikováno v:
The Journal of biological chemistry. 286(45)
Nitric-oxide synthases (NOS) are heme-thiolate enzymes that generate nitric oxide (NO) from l-arginine. Mammalian and bacterial NOSs contain a conserved tryptophan (Trp) that hydrogen bonds with the heme-thiolate ligand. We mutated Trp66 to His and P
Autor:
Ramasamy Somasundaram, David B. Knaff, Michael K. Johnson, Frederik Sommer, Sabeeha S. Merchant, Jatindra N. Tripathy, James P. Allen, Masakazu Hirasawa, Matthew Nestander, Masoud Zabet-Moghaddam, Mahima Kruthiventi, Jung Sung Chung
Publikováno v:
Photosynthesis research. 103(2)
The ferredoxin-dependent nitrite reductase from the green alga Chlamydomonas reinhardtii has been cloned, expressed in Escherichia coli as a His-tagged recombinant protein, and purified to homogeneity. The spectra, kinetic properties and substrate-bi
Akademický článek
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