Sort   by:  
 Page size 
ProteomicsS-glutathionylation proteome profiling of Streptococcus mutans
S-glutathionylation is an important post-translational modification (PTM) process that targets the protein cysteine thiol by the addition of glutathione (GSH). This modification can prevent proteolysis from over-oxidation of protein cysteine residue during the condition of oxidative or nitrosative s...
ORGANISM(S): Streptococcus mutans UA159 
2020-07-14 | PXD019564 | Pride
S-glutathionylation  streptococcus mutans  post-translational modification 
ProteomicsMass-spectroscopic quantification of CHAC1-regulated protein cysteine S-glutathionylation
S-glutathionylation is an important post-translational modification of a cysteine residue of target protein. We applied a quantitative redox proteomics approach to identify the specific cysteine residues as targets of S-glutathionylation. Using this approach, we profiled CHAC1-associated changes in ...
ORGANISM(S): Mus Musculus 
2024-03-12 | PXD050569 |
ProteomicsAlterations of protein S-glutathionylation modification in macrophages under oxidative conditions
S-glutathionylation is an important regulatory posttranslational modification of protein cysteine (Cys) thiols, yet the role of specific cysteine residues as targets of modification is poorly understood. To identify the specific molecular targets and pathways of Grx1 that are susceptible to redox-de...
ORGANISM(S): Mus musculus (Mouse) 
2021-11-01 | PXD027965 | Pride
Bmdm S-glutathionylation Lc–ms/ms 
UnknownProtein S-glutathionylation in malaria parasites.
Not available
S-EPMC4932784 | biostudies-literature
UnknownS-glutathionylation regulates inflammatory activities of S100A9.
Not available
S-EPMC2863208 | biostudies-literature
UnknownProtein phosphatase PP2Cα S-glutathionylation regulates cell migration.
Not available
S-EPMC11530597 | biostudies-literature
UnknownAllosteric Control of a Plant Receptor Kinase through S-Glutathionylation.
Not available
S-EPMC5768518 | biostudies-literature
UnknownA novel approach for predicting protein S-glutathionylation.
Not available
S-EPMC7489215 | biostudies-literature
UnknownProtein thiyl radical mediates S-glutathionylation of complex I.
Not available
S-EPMC3418477 | biostudies-literature
ProteomicsQuantitative Profiling of Protein S-Glutathionylation during Nanoparticle-Induced Oxidative Stress
Quantitative profiling of protein s-glutathionylation (SSG) reveals redox-dependent regulation of macrophage function during nanoparticle-induced oxidative stress
ORGANISM(S): Mus musculus (Mouse) 
2016-08-02 | PXD003356 | Pride
Glutathionylation Ssg Macrophage Redox Nanoparticle 
Sort   by:  
 Page size