Results 181 to 190 of about 8,445 (200)
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Glutathionylation of proteins by glutathione disulfide S-oxide
Biochemical Pharmacology, 2002Aqueous solution of S-nitrosoglutathione (GSNO) underwent spontaneous chemical transformation that generated several glutathione derivatives including glutathione sulfonic acid (GSO3H), glutathione disulfide S-oxide (GS(O)SG), glutathione disulfide S-dioxide, and glutathione disulfide.
Kuo-Ping, Huang, Freesia L, Huang
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Glutathionylation regulates IkappaB.
Biochemical and biophysical research communications, 2008Although there has been considerable interest in the regulation of NFkappaB activation by glutathionylation, the possibility of IkappaB as a target for glutathionylation has not been investigated. We now report that Cys(189) of IkappaB alpha is a target for S-glutathionylation. This modification is reversed by thiols such as dithiothreitol and GSH. The
In Sup, Kil +2 more
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Measurement of Mixed Disulfides Including Glutathionylated Proteins
2010Mixed disulfides between protein cysteines and low-molecular-weight thiol cysteine or glutathione lead to the formation of cysteinylated proteins or glutathionylated proteins. These types of posttranslational modification are of great importance in the so-called redox regulation, by which changes in the redox state of the cell regulate a number of ...
PRIORA R. +4 more
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Thioltransferase is a specific glutathionyl mixed-disulfide oxidoreductase
Biochemistry, 1993To study the substrate specificity and mechanism of thioltransferase (TTase) catalysis, we have used 14C- and 35S-radiolabeled mixed disulfides of cysteine and glutathione (GSH) with various cysteine-containing proteins. These protein mixed disulfide substrates were incubated with glutathione, glutathione disulfide (GSSG) reductase, and NADPH in the ...
S A, Gravina, J J, Mieyal
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Regulation of protein function by glutathionylation.
Free radical research, 2005The main function of reduced glutathione (GSH) is to protect from oxidative stress as a reactive oxygen scavenger. However, in the context of redox regulation, the ratio between GSH and its oxidized form (GSSG) determines the redox state of redox-sensitive cysteines in some proteins and, thus, acts as a signaling system.
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Oxidized GAPDH transfers S-glutathionylation to a nuclear protein Sirtuin-1 leading to apoptosis
Free Radical Biology and Medicine, 2021Syed Husain Mustafa Rizvi +2 more
exaly
Analysis of glutathionylated proteins
Plant and Cell Physiology Supplement, 2003Ito, Hisashi +2 more
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Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation
Molecules, 2021Elena Kalinina, Maria Novichkova
exaly