NSC 131114
NSC 131114 structure
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Common Name | NSC 131114 | ||
|---|---|---|---|---|
| CAS Number | 24425-56-7 | Molecular Weight | 391.48300 | |
| Density | 1.254g/cm3 | Boiling Point | 748.5ºC at 760 mmHg | |
| Molecular Formula | C16H29N3O6S | Melting Point | 200-202ºC(lit.) | |
| MSDS | Chinese USA | Flash Point | 406.5ºC | |
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Quantitation of protein S-glutathionylation by liquid chromatography-tandem mass spectrometry: correction for contaminating glutathione and glutathione disulfide.
Anal. Biochem. 469 , 54-64, (2014) Protein S-glutathionylation is a posttranslational modification that links oxidative stimuli to reversible changes in cellular function. Protein-glutathione mixed disulfide (PSSG) is commonly quantified by reduction of the disulfide and detection of the resul... |
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Effects of ONO-6950, a novel dual cysteinyl leukotriene 1 and 2 receptors antagonist, in a guinea pig model of asthma.
Eur. J. Pharmacol. 765 , 242-8, (2015) We assessed in this study the anti-asthmatic effects of ONO-6950, a novel cysteinyl leukotriene 1 (CysLT1) and 2 (CysLT2) receptors dual antagonist, in normal and S-hexyl glutathione (S-hexyl GSH)-treated guinea pigs, and compared these effects to those of mo... |
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Glutathionylation and Reduction of Methacrolein in Tomato Plants Account for Its Absorption from the Vapor Phase.
Plant Physiol. 169 , 1744-54, (2015) A large portion of the volatile organic compounds emitted by plants are oxygenated to yield reactive carbonyl species, which have a big impact on atmospheric chemistry. Deposition to vegetation driven by the absorption of reactive carbonyl species into plants... |
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Crystal structures of the yeast prion Ure2p functional region in complex with glutathione and related compounds.
Biochemistry 40(45) , 13564-73, (2001) The [URE3] phenotype in yeast Saccharomyces cerevisiae is due to an altered prion form of Ure2p, a protein involved in nitrogen catabolism. To understand possible conformational changes at the origin of prion propagation, we previously solved the crystal stru... |
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Crystallographic and thermodynamic analysis of the binding of S-octylglutathione to the Tyr 7 to Phe mutant of glutathione S-transferase from Schistosoma japonicum.
Biochemistry 44 , 1174-1183, (2005) Glutathione S-transferases are a family of multifunctional enzymes involved in the metabolism of drugs and xenobiotics. Two tyrosine residues, Tyr 7 and Tyr 111, in the active site of the enzyme play an important role in the binding and catalysis of substrate... |
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Modulating catalytic activity by unnatural amino acid residues in a GSH-binding loop of GST P1-1.
J. Mol. Biol. 376(3) , 811-26, (2008) The loop following helix alpha2 in glutathione transferase P1-1 has two conserved residues, Cys48 and Tyr50, important for glutathione (GSH) binding and catalytic activity. Chemical modification of Cys48 thwarts the catalytic activity of the enzyme, and mutat... |
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Plasmodium falciparum glutathione S-transferase--structural and mechanistic studies on ligand binding and enzyme inhibition.
Protein Sci. 15(2) , 281-9, (2006) Glutathione S-transferase of the malarial parasite Plasmodium falciparum (PfGST) represents a novel class of GST isoenzymes. Since the architecture of the PfGST substrate binding site differs significantly from its human counterparts and there is only this on... |
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Thermodynamic description of the effect of the mutation Y49F on human glutathione transferase P1-1 in binding with glutathione and the inhibitor S-hexylglutathione.
J. Biol. Chem. 278(47) , 46938-48, (2003) The thermodynamics of binding of both the substrate glutathione (GSH) and the competitive inhibitor S-hexylglutathione to the mutant Y49F of human glutathione S-transferase (hGST P1-1), a key residue at the dimer interface, has been investigated by isothermal... |
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Macrophage migration inhibitory factor interactions with glutathione and S-hexylglutathione.
J. Biol. Chem. 273(24) , 14877-84, (1998) Macrophage migration inhibitory factor (MIF) has been reported to interact with glutathione and S-hexylglutathione and to possess glutathione S-transferase activity. However, contrary to these reports, a recent NMR study concluded that MIF shows no affinity f... |
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The three-dimensional structure of an avian class-mu glutathione S-transferase, cGSTM1-1 at 1.94 A resolution.
J. Mol. Biol. 278(1) , 239-52, (1998) Glutathione S-transferase cGSTM1-1, an avian class-mu enzyme with high sequence identity with rGSTM3-3, was expressed heterologously in Escherichia coli. The three-dimensional structure of this protein that co-crystallized with an inhibitor, S-hexylglutathion... |