- S-
Glutathionylation is the
posttranslational modification of
protein cysteine residues by the
addition of glutathione, the most
abundant and important...
-
stems from the
reversible glutathionylation of the E2-lipoac acid
domain of
Oxoglutarate dehydrogenase.
Glutathionylation, a form of post-translational...
-
regulation of
cellular thiol proteins under oxidative stress by
protein S-
glutathionylation, a redox-regulated post-translational
thiol modification. The general...
- (proteostasis)
through S-
glutathionylation of ER
resident proteins,
including PDI and BiP. GSTP
leads to S-
glutathionylation of
binding immunoglobulin...
-
CoAlation (Protein-S-SCoA),
which plays a
similar role to
protein S-
glutathionylation by
preventing the
irreversible oxidation of the
thiol group of cysteine...
- UMP),
usually to
tyrosine propionylation pyroglutamate formation S-
glutathionylation S-nitrosylation S-sulfenylation (aka S-sulphenylation), reversible...
-
thought that the
primary function of Grx2 is to
catalyse reversible glutathionylation of
proteins with GSH in
cellular redox regulation including the response...
- "The role of
glutathione S-transferase P in
signaling pathways and S-
glutathionylation in cancer". Free
Radical Biology & Medicine. 51 (2): 299–313. doi:10...
-
which contains GRX-like domains;
these domains play a role in the S-
glutathionylation of
proteins and may be
involved in
actin organization in hair cells...
- cell function. Additionally, Tew and
colleagues investigated how S-
glutathionylation of the
protein BiP,
mediated by GSTP,
contributes to
acquired resistance...
