Zobrazeno 1 - 10
of 35
pro vyhledávání: '"D J, Stuehr"'
Publikováno v:
Biochemical Society Transactions. 33:1399-1403
The conditions of the cellular microenvironment in complex multicellular organisms fluctuate, enforcing permanent adaptation of cells at multiple regulatory levels. Covalent post-translational modifications of proteins provide the short-term response
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b3aa94f92c3f977df817223be6ef5bd
https://doi.org/10.1042/bst0331399
https://doi.org/10.1042/bst0331399
Publikováno v:
American Journal of Physiology-Cell Physiology. 260:C910-C916
Although nitric oxide (.N = O) biosynthesis is inducible in rat hepatocytes (HC), the physiological significance of .N = O production by these cells is unknown. Short exposure of HC to authentic .N = O led to a concentration-dependent inhibition of m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b82ec644a22172173bc10cbc0cb94b1
https://doi.org/10.1152/ajpcell.1991.260.5.c910
https://doi.org/10.1152/ajpcell.1991.260.5.c910
Publikováno v:
The Journal of Immunology. 145:940-944
Macrophage deactivating factor (MDF) and three members of the transforming growth factor-beta family (TGF-beta 1, -beta 2, and -beta 3) blocked the ability of IFN-gamma to induce release of reactive nitrogen intermediates from mouse peritoneal macrop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::04546e52226531feb6ae7bf2699530cc
https://doi.org/10.4049/jimmunol.145.3.940
https://doi.org/10.4049/jimmunol.145.3.940
Autor:
Jean-Luc Boucher, L. Casse, P. Camus, D. J. Stuehr, Kjetil Ask, Marie-Agnès Sari, Yves Michel Frapart, Sylvie Dijols, C. Giroud, K.S. Kim, Daniel Mansuy
Publikováno v:
Chemical Research in Toxicology
Chemical Research in Toxicology, American Chemical Society, 2003, 16, pp.1547-1554
Chemical Research in Toxicology, American Chemical Society, 2003, 16, pp.1547-1554
Nitric oxide synthases (NOSs) are flavohemeproteins that catalyze the oxidation of l-arginine to l-citrulline with formation of the widespread signal molecule NO. Beside their fundamental role in NO biosynthesis, these enzymes are also involved in th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8be6b54e3748373f068d1ccacde35ac
https://hal.science/hal-00095869
https://hal.science/hal-00095869
Publikováno v:
The Journal of biological chemistry. 275(43)
We studied catalysis by tetrahydrobiopterin (H4B)-free neuronal nitric-oxide synthase (nNOS) to understand how heme and H4B participate in nitric oxide (NO) synthesis. H4B-free nNOS catalyzed Arg oxidation to N(omega)-hydroxy-l-Arg (NOHA) and citrull
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3608af5764ef41880cd667ecd4d65535
https://pubmed.ncbi.nlm.nih.gov/10945985
https://pubmed.ncbi.nlm.nih.gov/10945985
Publikováno v:
The Journal of biological chemistry. 274(32)
The nNOS reductase domain is homologous to cytochrome P450 reductase, which contains two conserved clusters of acidic residues in its FMN module that play varied roles in its electron transfer reactions. To study the role of nNOS reductase domain clu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::cf301cbfaaedfc1a928e7a814df6abbb
https://pubmed.ncbi.nlm.nih.gov/10428800
https://pubmed.ncbi.nlm.nih.gov/10428800
Publikováno v:
The Journal of biological chemistry. 273(35)
Endothelial nitric-oxide synthase (eNOS) is targeted to caveoli through interaction with caveolin-1 (cav-1). cav-1 binding to a consensus site in the eNOS oxygenase domain is proposed to antagonize calmodulin (CaM) binding and thereby inhibit eNOS ni
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::72e73423532ea508557a0bfbdbfdfcb4
https://pubmed.ncbi.nlm.nih.gov/9712842
https://pubmed.ncbi.nlm.nih.gov/9712842
Publikováno v:
The Journal of biological chemistry. 273(30)
Cytokine-inducible nitric-oxide (NO) synthase (iNOS) contains an oxygenase domain that binds heme, tetrahydrobiopterin, and L-arginine, and a reductase domain that binds FAD, FMN, calmodulin, and NADPH. Dimerization of two oxygenase domains allows el
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5fc13b4c02b5e94aff91b8a4f7517521
https://pubmed.ncbi.nlm.nih.gov/9668073
https://pubmed.ncbi.nlm.nih.gov/9668073
Publikováno v:
The Journal of biological chemistry. 272(28)
Nitric oxide synthases (NOS) are hemeproteins that catalyze oxidation of L-arginine to nitric oxide (NO) and citrulline. The NOS heme iron is expected to participate in oxygen activation during catalysis, but its interactions with O2 are not characte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::be01cf4ebcf4839a2023e7c372d6ebb0
https://pubmed.ncbi.nlm.nih.gov/9211873
https://pubmed.ncbi.nlm.nih.gov/9211873
Autor:
R, Gachhui, A, Presta, D F, Bentley, H M, Abu-Soud, R, McArthur, G, Brudvig, D K, Ghosh, D J, Stuehr
Publikováno v:
The Journal of biological chemistry. 271(34)
Rat neuronal NO synthase (nNOS) is comprised of a flavin-containing reductase domain and a heme-containing oxygenase domain. Calmodulin binding to nNOS increases the rate of electron transfer from NADPH into its flavins, triggers electron transfer fr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ab5ee2e24cf3c658ed4ad8ab9fcfa43e
https://pubmed.ncbi.nlm.nih.gov/8702805
https://pubmed.ncbi.nlm.nih.gov/8702805