Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Susan M E Smith"'
Autor:
Juan A De La Cruz, Thota Ganesh, Becky A Diebold, Weiping Cao, Amelia Hofstetter, Neetu Singh, Amrita Kumar, James McCoy, Priya Ranjan, Susan M E Smith, Suryaprakash Sambhara, J David Lambeth, Shivaprakash Gangappa
Publikováno v:
PLoS ONE, Vol 16, Iss 7, p e0254632 (2021)
Superoxide radicals and other reactive oxygen species (ROS) are implicated in influenza A virus-induced inflammation. In this in vitro study, we evaluated the effects of TG6-44, a novel quinazolin-derived myeloperoxidase-specific ROS inhibitor, on in
Externí odkaz:
https://doaj.org/article/80b3ccda96934ff1811aa0a4c2c44104
Autor:
Juan D Rodriguez, Saddef Haq, Tsvetan Bachvaroff, Kristine F Nowak, Scott J Nowak, Deri Morgan, Vladimir V Cherny, Maredith M Sapp, Steven Bernstein, Andrew Bolt, Thomas E DeCoursey, Allen R Place, Susan M E Smith
Publikováno v:
PLoS ONE, Vol 12, Iss 2, p e0171594 (2017)
In 1972, J. Woodland Hastings and colleagues predicted the existence of a proton selective channel (HV1) that opens in response to depolarizing voltage across the vacuole membrane of bioluminescent dinoflagellates and conducts protons into specialize
Externí odkaz:
https://doaj.org/article/8c009d1f01134b1790ccb4fb16c5f50f
Publikováno v:
The Journal of Eukaryotic Microbiology
Bioluminescence in dinoflagellates is controlled by HV1 proton channels. Database searches of dinoflagellate transcriptomes and genomes yielded hits with sequence features diagnostic of all confirmed HV1, and show that HV1 is widely distributed in th
Autor:
Dipak K, Ghosh, Michael A, Holliday, Clayton, Thomas, J Brice, Weinberg, Susan M E, Smith, John C, Salerno
Publikováno v:
The Journal of biological chemistry. 281(20)
Mammalian nitric-oxide synthases are large modular enzymes that evolved from independently expressed ancestors. Calmodulin-controlled isoforms are signal generators; calmodulin activates electron transfer from NADPH through three reductase domains to
Publikováno v:
Biochemistry. 44(11)
A study of bovine endothelial nitric oxide synthase by Fourier transform infrared (FTIR) spectroscopy in the 1000-2500 cm(-)(1) range is reported. Binding of CO to the reduced enzyme gives two heme(II)-CO nu(C)(-)(O) stretches (1927 and 1904 cm(-)(1)
Publikováno v:
Biochemistry. 41(26)
Improvements in sensitivity and data processing of Fourier transform infrared (FTIR) spectroscopy enable it to be used to detect changes in protein structure at the atomic level. This paper reports a study of neuronal nitric oxide synthase (nNOS) by
Publikováno v:
Oxygen Homeostasis and Its Dynamics ISBN: 9784431684787
Nitric oxide synthases are large modular enzymes that produce NO and citrulline from arginine at the expense of NADPH and O2. We have modeled the reductase region, which corresponds roughly to the C-terminal half of the molecule, using the available
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6a2f5a3b93fb04502b8a5ace25e28434
https://doi.org/10.1007/978-4-431-68476-3_36
https://doi.org/10.1007/978-4-431-68476-3_36
Publikováno v:
Antioxidants, Vol 10, Iss 6, p 890 (2021)
The reactive oxygen species (ROS)-producing enzyme NADPH oxidase (NOX) was first identified in the membrane of phagocytic cells. For many years, its only known role was in immune defense, where its ROS production leads to the destruction of pathogens
Externí odkaz:
https://doaj.org/article/0cee703184d640f583a2021081b2cfb9