Results 301 to 310 of about 508,182 (337)
Some of the next articles are maybe not open access.
Glutathione peroxidase and oxidative stress
Toxicology Letters, 1995In this study, overexpression of the cDNA for the major cytoplasmic glutathione peroxidase isoenzyme, GSH Peroxidase 1 (GSHPx-1), in human MCF-7 breast cancer cells has been shown to significantly increase the tolerance of these cells to oxidative stress produced by hydrogen peroxide or by the redox cycling of the quinone-containing anticancer agent ...
openaire +2 more sources
Glutathione Peroxidase 4 and Ferroptosis
2016Glutathione peroxidase 4 (Gpx4) is one of eight members of the mammalian glutathione peroxidase family of enzymes. Gpx4 is unique due to its capacity to efficiently reduce phospholipid hydroperoxides. Additionally, it has been recognized that Gpx4 governs a novel form of non-apoptotic cell death, named ferroptosis.
Friedmann Angeli, J.P.F. +2 more
openaire +2 more sources
Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase.
Journal of Laboratory and Clinical Medicine, 1967D. Paglia, W. N. Valentine
semanticscholar +1 more source
1981
Publisher Summary This chapter presents a procedure for the preparation of glutathione peroxidase, which is regarded as a major protective system against endogenously and exogenously induced lipid peroxidation. Two types of methods are used for determining the activity of glutathione peroxidase.
openaire +1 more source
Publisher Summary This chapter presents a procedure for the preparation of glutathione peroxidase, which is regarded as a major protective system against endogenously and exogenously induced lipid peroxidation. Two types of methods are used for determining the activity of glutathione peroxidase.
openaire +1 more source
1993
Glutathione peroxidases are considered essential for the prevention of lipid peroxidation in biomembranes (1). Whereas the “classical” tetrameric Glutathione peroxidases (GPX) only reduce hydroperoxy fatty acids previously cleaved from phospholipids by phospholipases, a monomeric variant called phospholipid hydroperoxide glutathione peroxidase (PHGPX ...
R. Brigelius-Flohé +5 more
openaire +1 more source
Glutathione peroxidases are considered essential for the prevention of lipid peroxidation in biomembranes (1). Whereas the “classical” tetrameric Glutathione peroxidases (GPX) only reduce hydroperoxy fatty acids previously cleaved from phospholipids by phospholipases, a monomeric variant called phospholipid hydroperoxide glutathione peroxidase (PHGPX ...
R. Brigelius-Flohé +5 more
openaire +1 more source
Assays of glutathione peroxidase.
Methods in Enzymology, 1984L. Flohé, W. Günzler
semanticscholar +1 more source
Selenium: Biochemical Role as a Component of Glutathione Peroxidase
Science, 1973J. T. Rotruck +5 more
semanticscholar +1 more source
1985
Publisher Summary Glutathione peroxidases catalyze the reduction of hydroperoxides (ROOH) by glutathione (GSH). “R” may be an aliphatic or aromatic organic group or, simply, hydrogen. The products are H 2 O, an alcohol (ROH), and glutathione disulfide (GSSG).
openaire +1 more source
Publisher Summary Glutathione peroxidases catalyze the reduction of hydroperoxides (ROOH) by glutathione (GSH). “R” may be an aliphatic or aromatic organic group or, simply, hydrogen. The products are H 2 O, an alcohol (ROH), and glutathione disulfide (GSSG).
openaire +1 more source
Selenium: biochemical role as a component of glutathione peroxidase.
Science, 2009J. T. Rotruck +5 more
semanticscholar +1 more source
Glutathione peroxidase activity in selenium-deficient rat liver.
Biochemical and Biophysical Research Communications - BBRC, 1976R. Lawrence +3 more
semanticscholar +1 more source

