| PubMed |
Abstract |
RScore(About this table) |
| 5163097 |
Okawa H, Casida JE: Glutathione S-transferases liberate hydrogen cyanide from organic thiocyanates. Biochem Pharmacol. 1971 Jul;20(7):1708-11.
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6(0,0,1,1) |
Details |
| 4331266 |
Okawa H, Casida JE: Glutathione S-transferases liberate hydrogen cyanide from organic thiocyanates. Biochem Pharmacol. 1971 Jul;20(7):1708-11.
|
6(0,0,1,1) |
Details |
| 12191880 |
Leng G, Lewalter J: Polymorphism of glutathione S-transferases and susceptibility to acrylonitrile and dimethylsulfate in cases of intoxication. Toxicol Lett. 2002 Aug 5;134(1-3):209-17.
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2(0,0,0,2) |
Details |
| 3556837 |
Freeman JJ, Hayes EP: The metabolism of acetonitrile to cyanide by isolated rat hepatocytes. . Fundam Appl Toxicol. 1987 Feb;8(2):263-71.
The metabolism of saturated nitriles, including acetonitrile, has been assumed to occur by a cytochrome P-450-dependent oxidation at the alpha-carbon, yielding a cyanohydrin intermediate which may spontaneously degrade to hydrogen cyanide and an aldehyde.
Since acetonitrile is structurally similar to iodomethane, a substrate for glutathione (GSH) S-transferases, we hypothesized that the metabolism of acetonitrile to cyanide might also occur by a nucleophilic substitution reaction involving GSH. |
1(0,0,0,1) |
Details |