<p><b>Copyright information:</b></p><p>Taken from "Glutathionylation of beta-actin via a cysteinyl sulfenic acid intermediary"</p><p>http://www.biomedcentral.com/1471-2091/8/26</p><p>BMC Biochemistry 2007;8():26-26.</p><p>Published online 10 Dec 2007</p><p>PMCID:PMC2228301.</p><p></p> indicated samples were incubated with (i) 1 mM DTT, after which 1 mM GSSG (A) or GSH (B) was added (ii) and a second incubation with 1 mM DTT was performed (iii)
ABSTRACT Glutathione (GSH) is an important intracellular peptide with multiple functions ranging fro...
138 p.Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1992.Cyanohydroxybutene (CHB; 200 ...
Protein-glutathione mixed disulfide formation was investigated in vitro by exposure of human platele...
<p><b>Copyright information:</b></p><p>Taken from "Glutathionylation of beta-actin via a cysteinyl s...
Many proteins, including actin, are targets for S-glutathionylation, the reversible formation of mix...
Glutathione (GSH) is the most abundant antioxidant in living organisms. It is a small tripeptide com...
Glutathionylated actin was detected as described in Methods. Densitometric analysis of the obtained ...
: Protein glutathionylation is a post-translational modification consisting of the formation of a mi...
S-glutathionylation, the reversible formation of mixed disulphides of cysteinyl residues in target p...
In this study we investigated the molecular mechanism of glutathionylation on isolated human cardiac...
S-glutathionylation, the reversible formation of mixed disulphides of cysteinyl residues in target p...
Glutathione disulfide (GSSG) accumulates in cells under an increased oxidant load, which occurs duri...
Glutathione disulfide (GSSG) accumulates in cells under an increased oxidant load, which occurs duri...
S-glutathionylation involves the reversible formation of a mix disulphide-bridge between specific cy...
ABSTRACT Glutathione (GSH) is an important intracellular peptide with multiple functions ranging fro...
138 p.Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1992.Cyanohydroxybutene (CHB; 200 ...
Protein-glutathione mixed disulfide formation was investigated in vitro by exposure of human platele...
<p><b>Copyright information:</b></p><p>Taken from "Glutathionylation of beta-actin via a cysteinyl s...
Many proteins, including actin, are targets for S-glutathionylation, the reversible formation of mix...
Glutathione (GSH) is the most abundant antioxidant in living organisms. It is a small tripeptide com...
Glutathionylated actin was detected as described in Methods. Densitometric analysis of the obtained ...
: Protein glutathionylation is a post-translational modification consisting of the formation of a mi...
S-glutathionylation, the reversible formation of mixed disulphides of cysteinyl residues in target p...
In this study we investigated the molecular mechanism of glutathionylation on isolated human cardiac...
S-glutathionylation, the reversible formation of mixed disulphides of cysteinyl residues in target p...
Glutathione disulfide (GSSG) accumulates in cells under an increased oxidant load, which occurs duri...
Glutathione disulfide (GSSG) accumulates in cells under an increased oxidant load, which occurs duri...
S-glutathionylation involves the reversible formation of a mix disulphide-bridge between specific cy...
ABSTRACT Glutathione (GSH) is an important intracellular peptide with multiple functions ranging fro...
138 p.Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1992.Cyanohydroxybutene (CHB; 200 ...
Protein-glutathione mixed disulfide formation was investigated in vitro by exposure of human platele...