Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Donald J. Wolff"'
Autor:
Donald J. Wolff, Christopher M. Barbieri, Stephen R. Wilson, David I. Schuster, Christine F. Richardson
Publikováno v:
Archives of Biochemistry and Biophysics. 399:130-141
C(60)-Fullerene trisamine adducts inhibit neuronal nitric oxide synthase and calcineurin phosphatase activities in a manner completely reversible by calmodulin. As measured by difference spectroscopy, D(3)-trisamine and C(3)-semiamine fullerene adduc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6dd2866ea6f7e3fc975188c0b5f3c1ae
https://doi.org/10.1006/abbi.2002.2766
https://doi.org/10.1006/abbi.2002.2766
Publikováno v:
Archives of Biochemistry and Biophysics. 375:183-194
N(omega)propyl-l-arginine (NPA) and S-ethyl-N-[4-(trifluoromethyl)phenyl]isothiourea (TFMPITU) inhibit selectively the neuronal nitric oxide (NO) synthase (nNOS) isoform. In the presence of Ca(2+) and calmodulin (CaM), NPA and TFMPITU produce a time-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d7b8160869200d94b3fc9d2af22dd04
https://doi.org/10.1006/abbi.1999.1658
https://doi.org/10.1006/abbi.1999.1658
Autor:
Donald J. Wolff, Ruslana Bryk
Publikováno v:
Pharmacology & Therapeutics. 84:157-178
Nitric oxide synthase (NOS) (EC 1.14.13.39) is a homodimeric cytochrome P450 monooxygenase analog that generates nitric oxide (NO) from the amino acid L-arginine. Enzymatically produced NO acts as an intracellular messenger in neuronal networks, bloo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2a24901539f45b182c764faf1c2cf74
https://doi.org/10.1016/s0163-7258(99)00030-3
https://doi.org/10.1016/s0163-7258(99)00030-3
Autor:
Andrew L. Salzman, Donald J. Wolff, Salvatore Cuzzocrea, Andrew Lubeskie, Csaba Szabó, Basilia Zingarelli, Garry J. Southan, Douglas S. Gauld
Publikováno v:
Biochemical Pharmacology. 54:409-417
Guanidines, amidines, S-alkylisothioureas, and other compounds containing the amidine function (-C(=NH)NH2) have been described as inhibitors of the generation of nitric oxide (NO) by NO synthase (NOS). Here we report on the inhibition of the activit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf665f5ed0f890e7080670cb7cd5d7d3
https://doi.org/10.1016/s0006-2952(97)00196-2
https://doi.org/10.1016/s0006-2952(97)00196-2
Publikováno v:
Archives of Biochemistry and Biophysics. 338:73-82
As measured at 100 μ m extracellular arginine, aminoguanidine produced a time- and concentration-dependent inactivation of nitric oxide (NO) synthesis by cytokine-induced RAW cells. Inactivation obeyed first-order kinetics and occurred at a maximal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1ff23a8c43803ee68b4bd747361b5d97
https://doi.org/10.1006/abbi.1996.9811
https://doi.org/10.1006/abbi.1996.9811
Autor:
Donald J. Wolff
Publikováno v:
Emerging Therapeutic Targets. 1:29-32
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::96be01d15b411d02dac4f0b5ed4fbe86
https://doi.org/10.1517/14728222.1.1.29
https://doi.org/10.1517/14728222.1.1.29
Autor:
Garry J. Southan, Donald J. Wolff, Timothy C. Gahman, Venkat Bhat, Andrew L. Salzman, Csaba Szabó, Ruslana Bryk, Basilia Zingarelli
Publikováno v:
British Journal of Pharmacology. 118:1659-1668
1. Guanidines, amidines, S-alkylisothioureas, and recently, mercaptoalkylguanidines have been described as inhibitors of the generation of nitric oxide (NO) from L-arginine by NO synthases (NOS). We have recently demonstrated that guanidinoethyldisul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da8a860848a0e3aa1debac24b4af0535
https://doi.org/10.1111/j.1476-5381.1996.tb15589.x
https://doi.org/10.1111/j.1476-5381.1996.tb15589.x
Autor:
Andrew Lubeskie, Donald J. Wolff
Publikováno v:
Archives of Biochemistry and Biophysics. 325:227-234
Diaminoguanidine (DAG) and NG-amino-L-arginine each produced a time- and concentration-dependent inactivation of the citrulline-forming activity of all three NOS isoforms. DAG inactivates both the NADPH-oxidase and the citrulline-forming activities o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b5b07406ba03d6fbc17494be41252475
https://doi.org/10.1006/abbi.1996.0028
https://doi.org/10.1006/abbi.1996.0028
Publikováno v:
Archives of Biochemistry and Biophysics. 314:360-366
Citrulline formation by the Ca 2+ CaM-dependent nitric oxide synthase of bovine endothelium is inhibited reversibly by 7-nitroindazole, 1-phenylimidazole, and imidazole. As measured at 0.67 μM (6R)-5,6,7,8-tetrahydrobiopterin (BH 4 ), IC 50 values o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e495ca6c025d630d7ff537c68f29a264
https://doi.org/10.1006/abbi.1994.1454
https://doi.org/10.1006/abbi.1994.1454
Autor:
B.J. Gribin, Donald J. Wolff
Publikováno v:
Archives of Biochemistry and Biophysics. 311:300-306
Citrulline formation by Ca(2+)-calmodulin (CaM)-dependent nitric oxide synthase from bovine brain is inhibited reversibly by indazole, 5-nitro-, 6-nitro-, and 7-nitroindazole with IC50 values of 2.3 mM, 1.15 mM, 40 microM, and 2.5 microM, respectivel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::572717ddcac2fe1430dd4667212beded
https://doi.org/10.1006/abbi.1994.1241
https://doi.org/10.1006/abbi.1994.1241