Protocol for detecting protein S-glutathionylation in Arabidopsis thaliana under oxidative stress using a non-transgenic chemical toolkit [PDF]
Summary: Protein S-glutathionylation is a redox-sensitive post-translational modification that regulates proteostasis and signaling during oxidative stress. However, its in vivo detection is challenging due to labile disulfide bonds and ex vivo oxidation
Shuai Zhao, Xiaoyuan Chen, Wei Wang
doaj +2 more sources
Redox-dependent protein S-glutathionylation governs azacitidine sensitivity and resistance in AML [PDF]
Disruption of redox metabolism is a hallmark of drug-resistant cancer cells, representing a major obstacle to the effective treatment of acute myeloid leukemia (AML).
Dušan Nemes +5 more
doaj +2 more sources
The discovery that cardiac sarcomere proteins are substrates for S-glutathionylation and that this post-translational modification correlates strongly with diastolic dysfunction led to new concepts regarding how levels of oxidative stress affect the ...
Paola C. Rosas, R. John Solaro
doaj +3 more sources
Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation [PDF]
S-glutathionylation and S-nitrosylation are reversible post-translational modifications on the cysteine thiol groups of proteins, which occur in cells under physiological conditions and oxidative/nitrosative stress both spontaneously and enzymatically ...
Elena Kalinina, Maria Novichkova
doaj +4 more sources
S-Glutathionylation of Cryptic Cysteines Enhances Titin Elasticity by Blocking Protein Folding [PDF]
SummaryThe giant elastic protein titin is a determinant factor in how much blood fills the left ventricle during diastole and thus in the etiology of heart disease.
Solaro, R. John +19 more
core +5 more sources
Protein S-glutathionylation and platelet anti-aggregating activity of disulfiram
Blood platelets are central to haemostasis, and reactions in platelets involving sulfhydryl groups play important roles in platelet function. Reduced glutathione (GSH) plays an important role in platelet aggregation and glutathione-depleting chemicals ...
D. Giustarini +11 more
core +5 more sources
Protein S-glutathionylation stimulate adipogenesis by stabilizing C/EBPβ in 3T3L1 cells. [PDF]
Watanabe Y +8 more
europepmc +2 more sources
Measurement of S-glutathionylated proteins by HPLC [PDF]
AbstractS-glutathionylated proteins (GSSP), i.e., protein-mixed disulfides with glutathione (GSH), are considered a suitable biomarker of oxidative stress. In fact, they occur within cells at low level and their concentration increases markedly under pro-oxidant conditions.
Giustarini, Daniela +3 more
openaire +5 more sources
ROS-Driven STAT1 S-Glutathionylation Sustains IFNγ Signaling and Pro-Inflammatory Microglial Polarization [PDF]
Oxidative stress is a major driver of neuroinflammation, yet the molecular redox mechanisms that shape microglial activation remain incompletely defined.
Martina Brattini +8 more
doaj +2 more sources
Increased Protein S-Glutathionylation in Leber's Hereditary Optic Neuropathy (LHON). [PDF]
Leber’s hereditary optic neuropathy (LHON, MIM#535000) is the most common form of inherited optic neuropathies and mitochondrial DNA-related diseases. The pathogenicity of mutations in genes encoding components of mitochondrial Complex I is well established, but the underlying pathomechanisms of the disease are still unclear.
Zhou L +13 more
europepmc +5 more sources

