- S-
Glutathionylation is the
posttranslational modification of
protein cysteine residues by the
addition of glutathione, the most
abundant and important...
-
regulation of
cellular thiol proteins under oxidative stress by
protein S-
glutathionylation, a redox-regulated post-translational
thiol modification. The general...
-
stems from the
reversible glutathionylation of the E2-lipoac acid
domain of
Oxoglutarate dehydrogenase.
Glutathionylation, a form of post-translational...
-
CoAlation (Protein-S-SCoA),
which plays a
similar role to
protein S-
glutathionylation by
preventing the
irreversible oxidation of the
thiol group of cysteine...
- (proteostasis)
through S-
glutathionylation of ER
resident proteins,
including PDI and BiP. GSTP
leads to S-
glutathionylation of
binding immunoglobulin...
- (UMP)),
usually to
tyrosine propionylation pyroglutamate formation S-
glutathionylation S-nitrosylation S-sulfenylation (aka S-sulphenylation), reversible...
-
photosynthetic organisms:
emerging functions for
glutaredoxins and
glutathionylation" (PDF). Annu Rev
Plant Biol. 59: 143–66. doi:10.1146/annurev.arplant...
- cell function. Additionally, Tew and
colleagues investigated how S-
glutathionylation of the
protein BiP,
mediated by GSTP,
contributes to
acquired resistance...
-
photosynthetic organisms:
emerging functions for
glutaredoxins and
glutathionylation" (PDF).
Annual Review of
Plant Biology. 59: 143–66. doi:10.1146/annurev...
- (2006). "A
novel role for
human sulfiredoxin in the
reversal of
glutathionylation".
Cancer Res. 66 (13): 6800–6. doi:10.1158/0008-5472.CAN-06-0484....
