Myricetin as a Potential Adjuvant in Chemotherapy: Studies on the Inhibition of Human Glutathione Transferase A1-1.

Glutathione transferases (GSTs) are a family of Phase II detoxification enzymes that are involved in the development of multi-drug resistance (MDR) phenomena toward chemotherapeutic agents. GST inhibitors are considered candidate compounds able to chemomodulate and reverse MDR. The natural flavonoid myricetin (MYR) has been shown to exhibit a wide range of pharmacological functions, including antitumor activity.

The Interaction of Human Glutathione Transferase GSTA1-1 with Reactive Dyes.

Human glutathione transferase A1-1 (hGSTA1-1) contributes to developing resistance to anticancer drugs and, therefore, is promising in terms of drug-design targets for coping with this phenomenon. In the present study, the interaction of anthraquinone and diazo dichlorotriazine dyes (DCTD) with hGSTA1-1 was investigated. The anthraquinone dye Procion blue MX-R (PBMX-R) appeared to interact with higher affinity and was selected for further study.

The Interaction of the Flavonoid Fisetin with Human Glutathione Transferase A1-1.

Glutathione transferases (GSTs) are a family of Phase II detoxification enzymes that are involved in the development of the multidrug resistance (MDR) mechanism in cancer cells and therefore affect the clinical outcome of cancer chemotherapy. The discovery of nontoxic natural compounds as inhibitors for GSTs is a promising approach for chemosensitizing and reversing MDR. Fisetin (7,3',4'-flavon-3-ol) is a plant flavonol present in many plants and fruits.

The Pleiotropic Function of Human Sirtuins as Modulators of Metabolic Pathways and Viral Infections.

Sirtuins (SIRTs) are nicotinamide adenine dinucleotide-dependent histone deacetylases that incorporate complex functions in the mechanisms of cell physiology. Mammals have seven distinct members of the SIRT family (SIRT1-7), which play an important role in a well-maintained network of metabolic pathways that control and adapt the cell to the environment, energy availability and cellular stress. Until recently, very few studies investigated the role of SIRTs in modulating viral infection and progeny.

Probing the Role of the Conserved Arg174 in Formate Dehydrogenase by Chemical Modification and Site-Directed Mutagenesis.

The reactive adenosine derivative, adenosine 5'--[S-(4-hydroxy-2,3-dioxobutyl)]-thiophosphate (AMPS-HDB), contains a dicarbonyl group linked to the purine nucleotide at a position equivalent to the pyrophosphate region of NAD. AMPS-HDB was used as a chemical label towards formate dehydrogenase (FDH). AMPS-HDB reacts covalently with FDH, leading to complete inactivation of the enzyme activity.

The Interaction of the Microtubule Targeting Anticancer Drug Colchicine with Human Glutathione Transferases.

Background: Glutathione transferases (GSTs) are a family of Phase II detoxification enzymes that have been shown to be involved in the development of multi-drug resistance (MDR) mechanism toward chemotherapeutic agents. GST inhibitors have, therefore, emerged as promising chemosensitizers to manage and reverse MDR. Colchicine (COL) is a classical antimitotic, tubulin-binding agent (TBA) which is being explored as anticancer drug.

Development of Enzybiotics: The Ph28 Gene of Phage PH15 Is a Two-Domain Endolysin.

Given the worldwide increase in antibiotic resistant bacteria, bacteriophage derived endolysins represent a very promising new alternative class of antibacterials in the fight against infectious diseases. Endolysins are able to degrade the prokaryotic cell wall, and therefore have potential to be exploited for biotechnological and medical purposes. is a Gram-positive multidrug-resistant (MDR) bacterium of human skin.

Copper-induced oxidative cleavage of glutathione transferase F1-1 from Zea mays.

Study of the interaction of glutathione transferase F1-1 from Zea mays (ZmGSTF1-1) with Cu(II), in the presence of ascorbate showed that the enzyme was rapidly inactivated. The inactivation was time and Cu(II) concentration dependent. The rate of inactivation showed non-linear dependence on Cu(II) concentration, indicating that a reversible complex with the enzyme (K 84.

Ligand-induced glutathione transferase degradation as a therapeutic modality: Investigation of a new metal-mediated affinity cleavage strategy for human GSTP1-1.

Glutathione transferases (GST, EC. 2.5.

Biochemical characterization and immobilization of Erwinia carotovoral-asparaginase in a microplate for high-throughput biosensing of l-asparagine.

l-Asparaginases (l-ASNase, E.C. 3.

Delineation of the structural and functional role of Arg111 in GSTU4-4 from Glycine max by chemical modification and site-directed mutagenesis.

The structural and functional role of Arg111 in GSTU4-4 from Glycine max (GmGSTU4-4) was studied by chemical modification followed by site-directed mutagenesis. The arginine-specific reagent 2,3-butanedione (BTD) inactivates the enzyme in borate buffer at pH8.0, with pseudo-first-order saturation kinetics.