Selenoprotein W is a glutathione-dependent antioxidant in vivo (Q27863315)

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Tae Soo Kim

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Youn Wook Chung

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Byeong Jae Lee

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Ick Young Kim

Protein oxidation in aging, disease, and oxidative stress

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language of work or name

English

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publication date

24 April 2002

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517

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issue

1-3

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page(s)

225-8

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cites work

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The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution

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The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm.

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Selenoprotein P in human plasma as an extracellular phospholipid hydroperoxide glutathione peroxidase. Isolation and enzymatic characterization of human selenoprotein p

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Selenoprotein W of rat muscle binds glutathione and an unknown small molecular weight moiety

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Purification, characterization, and glutathione binding to selenoprotein W from monkey muscle

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Responsiveness of selenoproteins to dietary selenium

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Mitochondrial glutathione modulates TNF-alpha-induced endothelial cell dysfunction

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Increased induction of apoptosis in mononuclear cells of a glucose-6-phosphate dehydrogenase deficient patient

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Overexpression of catalase in cytosolic or mitochondrial compartment protects HepG2 cells against oxidative injury

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Tissue distribution and influence of selenium status on levels of selenoprotein W.

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Selenium influences tissue levels of selenoprotein W in sheep.

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Dietary selenium increases selenoprotein W levels in rat tissues.

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Determination of glutathione and glutathione disulfide in biological samples

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