Results 211 to 220 of about 127,735 (256)
Some of the next articles are maybe not open access.
2000
Abstract The glutathione transferases (GSTs) are a family of multi-functional proteins which act as enzymes and also as binding proteins in detoxification processes (1-5). GSTs catalyse the nucleophilic attack of the sulfur atom of reduced glutathione by electrophilic groups in a second substrate. Most GSTs are located in the cytosol,
openaire +1 more source
Abstract The glutathione transferases (GSTs) are a family of multi-functional proteins which act as enzymes and also as binding proteins in detoxification processes (1-5). GSTs catalyse the nucleophilic attack of the sulfur atom of reduced glutathione by electrophilic groups in a second substrate. Most GSTs are located in the cytosol,
openaire +1 more source
Detoxication reactions of glutathione and glutathione transferases
Xenobiotica, 1986(1986). Detoxication reactions of glutathione and glutathione transferases. Xenobiotica: Vol. 16, No. 10-11, pp. 957-973.
openaire +2 more sources
Glutathione Transferase: New Model for Glutathione Activation
Chemistry – A European Journal, 2008AbstractGlutathione transferases are enzymes of the cellular detoxification system that metabolize a vast spectrum of xenobiotic and endobiotic toxic compounds. They are homodimers or heterodimers and each monomer has an active center composed of a G‐site in which glutathione (GSH) binds and an H‐site for the electrophilic substrate.
Daniel F A R, Dourado +3 more
openaire +2 more sources
The Role of Glutathione and Glutathione Transferases in Chemical Cardnogenesi
Critical Reviews in Biochemistry and Molecular Biology, 1990(1990). The Role of Glutathione and Glutathione Transferases in Chemical Cardnogenesi. Critical Reviews in Biochemistry and Molecular Biology: Vol. 25, No. 1, pp. 47-70.
Brian Coles +2 more
openaire +2 more sources
Mammalian Cytosolic Glutathione Transferases
Current Protein & Peptide Science, 2008Glutathione Transferases (GSTs) are crucial enzymes in the cell detoxification process catalyzing the nucleophilic attack of glutathione (GSH) on toxic electrophilic substrates and producing a less dangerous compound. GSTs studies are of great importance since they have been implicated in the development of drug resistance in tumoral cells and are ...
Daniel F A R, Dourado +2 more
openaire +2 more sources
Human glutathione S-transferases
International Journal of Biochemistry, 19941. Multiple forms of glutathione S-transferase (GST) isoenzymes present in human tissues are dimers of subunits belonging to three distinct gene families namely alpha, mu and pi. Only the subunits within each class hybridize to give active dimers. 2.
Y C, Awasthi, R, Sharma, S S, Singhal
openaire +2 more sources
Marine Glutathione S-Transferases
Marine Biotechnology, 2007The aquatic environment is generally affected by the presence of environmental xenobiotic compounds. One of the major xenobiotic detoxifying enzymes is glutathione S-transferase (GST), which belongs to a family of multifunctional enzymes involved in catalyzing nucleophilic attack of the sulfur atom of glutathione (gamma-glutamyl-cysteinylglycine) to an
Brian, Blanchette +2 more
openaire +2 more sources
Glutathione S-Transferases - A Review
Current Medicinal Chemistry, 1999Abstract: The Glutathione S-transferases (GSTs) form a group of multi-gene isoenzymes involved in the cellular detoxification of both xenobiotic and endobiotic compounds. GSTs have been divided into a number of subclasses, alpha (α), mu {μ), pi (π), and theta (θ).
A E, Salinas, M G, Wong
openaire +2 more sources
Glutathione transferases and neurodegenerative diseases
Neurochemistry International, 2015There is substantial agreement that the unbalance between oxidant and antioxidant species may affect the onset and/or the course of a number of common diseases including Parkinson's and Alzheimer's diseases. Many studies suggest a crucial role for oxidative stress in the first phase of aging, or in the pathogenesis of various diseases including ...
MAZZETTI, ANNA PAOLA +3 more
openaire +3 more sources
Drosophila Glutathione S‐Transferases
2005The Drosophila glutathione S-transferases (GSTs; EC2.5.1.18) comprise a host of cytosolic proteins that are encoded by a gene superfamily and a homolog of the human microsomal GST. Biochemical studies of certain recombinant GSTs have linked their enzymatic functions to important substrates such as the pesticide DDT and 4-hydroxynonenal, a reactive ...
Chen-Pei D, Tu, Bünyamin, Akgül
openaire +2 more sources