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Open AccessJournal ArticleDOI

Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine).

O.W. Griffith, +1 more
- 25 Aug 1979 - 
- Vol. 254, Iss: 16, pp 7558-7560
TLDR
The findings support the conclusion that the S-alkyl moiety of the sulfoximine binds at the enzyme site that normally binds the acceptor amino acid and increases in a manner which is parallel to those of the corresponding isosteric accepter amino acid substrates, i.e. glycine, alanine, and alpha-aminobutyrate.
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This article is published in Journal of Biological Chemistry.The article was published on 1979-08-25 and is currently open access. It has received 1626 citations till now. The article focuses on the topics: Buthionine sulfoximine.

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Journal ArticleDOI

Targeting cancer cells by ROS-mediated mechanisms: a radical therapeutic approach?

TL;DR: It is argued that modulating the unique redox regulatory mechanisms of cancer cells might be an effective strategy to eliminate these cells.
Journal ArticleDOI

Selective modification of glutathione metabolism

TL;DR: Modifications of glutathione metabolism may be achieved by administration of selective enzyme inhibitors, and also by giving compounds that increase glutATHione synthesis, which are useful in chemotherapy and radiation therapy and in protecting cells against the toxic effects of drugs, other foreign compounds, and oxygen.
Journal ArticleDOI

Glutathione in plants: an integrated overview.

TL;DR: How alterations in glutathione status, such as those observed during stress, may participate in signal transduction cascades are discussed and how these alterations are integrated to fine-tune photorespiratory and respiratory metabolism and to modulate phytohormone signalling pathways.
Journal ArticleDOI

Metabolite Profiling Identifies a Key Role for Glycine in Rapid Cancer Cell Proliferation

TL;DR: Glycine consumption and expression of the mitochondrial glycine biosynthetic pathway was identified as strongly correlated with rates of proliferation across cancer cells, and higher expression of this pathway was associated with greater mortality in breast cancer patients.
References
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Journal ArticleDOI

gamma-Glutamylcysteine synthetase. Further purification, "half of the sites" reactivity, subunits, and specificity.

TL;DR: Gamma-glutamylcysteine synthetase was obtained from rat liver by an improved method involving chromatography on Sepharose-aminohexyl-ATP to a specific activity of about 1600 units/mg, or approximately twice that previously obtained; it is thus the most active preparation of this enzyme thus far isolated as mentioned in this paper.
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