Zobrazeno 1 - 10
of 25
pro vyhledávání: '"R N, Armstrong"'
Publikováno v:
Hydrology and Earth System Sciences, Vol 23, Pp 4891-4907 (2019)
Land surface evaporation has considerable spatial variability that is not captured by point-scale estimates calculated from meteorological data alone. Knowing how evaporation varies spatially remains an important issue for improving parameterisations
Externí odkaz:
https://doaj.org/article/810778d47a19488e9f2e7e11f2dc73fa
Publikováno v:
Chemical Research in Toxicology. 14:1107-1117
Glutathione (GSH) transferases are generally involved in the detoxication of xenobiotic chemicals. However, conjugation can also activate compounds and result in DNA modification. Activation of 1,2-dihaloethanes (BrCH(2)CH(2)Br, BrCH(2)CH(2)Cl, and C
Autor:
Shu-ou Shan, R. N. Armstrong
Publikováno v:
Journal of Biological Chemistry. 269:32373-32379
Isoenzymes 3-3 and 4-4 of the mu class glutathione S-transferases share 77% sequence identity but have distinctly different catalytic properties. Analysis of the crystal structure of isoenzyme 3-3 in complex with the diastereomeric products of the ad
Publikováno v:
Journal of Biological Chemistry. 268:11508-11511
The participation of the hydroxyl group of tyrosine 115 in the catalytic mechanism of isoenzyme 3-3 of rat glutathione (GSH) S-transferase is implicated by x-ray crystallographic analysis of a product complex and confirmed by comparison of the cataly
Publikováno v:
Journal of Biological Chemistry. 267:4296-4299
The role of the hydroxyl group of tyrosine 6 in the catalytic mechanism of isoenzyme 3-3 of rat glutathione S-transferase has been examined by x-ray crystallography and site-specific replacement of the residue with phenylalanine and evaluation of the
Publikováno v:
Journal of Biological Chemistry. 266:19475-19479
To test the proposition that a histidine residue is essential in the catalytic mechanism of glutathione S-transferase, rat liver isoenzyme 3-3 specifically labeled with [ring-2-13C]histidine was prepared. The 13C NMR spectrum of the labeled enzyme re
Autor:
S, Shan, R N, Armstrong
Publikováno v:
The Journal of biological chemistry. 269(51)
Isoenzymes 3-3 and 4-4 of the mu class glutathione S-transferases share 77% sequence identity but have distinctly different catalytic properties. Analysis of the crystal structure of isoenzyme 3-3 in complex with the diastereomeric products of the ad
Autor:
J H, Ploemen, W W, Johnson, S, Jespersen, D, Vanderwall, B, van Ommen, J, van der Greef, P J, van Bladeren, R N, Armstrong
Publikováno v:
The Journal of biological chemistry. 269(43)
The mode of inactivation of glutathione S-transferase isoenzyme 3-3 from rat by the active site-directed inhibitor 2-(S-glutathionyl)-3,5,6-trichloro-1,4-benzoquinone (GSTCBQ) has been investigated by a combination of site-specific mutagenesis and ma
Autor:
R N, Armstrong
Publikováno v:
Advances in enzymology and related areas of molecular biology. 69
Publikováno v:
The Journal of biological chemistry. 268(16)
The participation of the hydroxyl group of tyrosine 115 in the catalytic mechanism of isoenzyme 3-3 of rat glutathione (GSH) S-transferase is implicated by x-ray crystallographic analysis of a product complex and confirmed by comparison of the cataly