Results 11 to 20 of about 6,885 (176)
Isotopically Labeled Clickable Glutathione to Quantify Protein S‐Glutathionylation [PDF]
ChemBioChem, 2020 AbstractProtein S‐glutathionylation is one of the important cysteine oxidation events that regulate various redox‐mediated biological processes. Despite several existing methods, there are few proteomic approaches to identify and quantify specific cysteine residues susceptible to S‐glutathionylation.
Young-Hoon Ahn
exaly +6 more sources
An In Vitro Study of Protein S-Glutathionylation by Members of the CLIC Protein Family [PDF]
BiomoleculesIncreasing evidence points to members of the chloride intracellular ion channel (CLIC) protein family performing a variety of functions within cells—classifying them as moonlighting proteins—and serving as natural cellular antioxidant protective agents ...
Wendy El Khoury +4 more
doaj +4 more sources
Immunoprecipitation methods to identify S-glutathionylation in target proteins
MethodsX, 2019 S-glutathionylation is a reversible post-translational modification of proteins that generate a mixed disulfide between glutathione to thiolate anion of cysteine residues in target proteins. In the last ten years, S-glutathionylation has been extensively
Elena Butturini +3 more
doaj +4 more sources
The effect of oxidant and the non-oxidant alteration of cellular thiol concentration on the formation of protein mixed-disulfides in HEK 293 cells. [PDF]
PLoS ONE, 2008 Cellular molecules possess various mechanisms in responding to oxidant stress. In terms of protein responses, protein S-glutathionylation is a unique post-translational modification of protein reactive cysteines forming disulfides with glutathione ...
Jasen Lee Gilge +2 more
doaj +3 more sources
Prediction of S-glutathionylation sites based on protein sequences. [PDF]
PLoS ONE, 2013 S-glutathionylation, the reversible formation of mixed disulfides between glutathione(GSH) and cysteine residues in proteins, is a specific form of post-translational modification that plays important roles in various biological processes, including ...
Chenglei Sun +4 more
doaj +4 more sources
Increased Protein S-Glutathionylation in Leber's Hereditary Optic Neuropathy (LHON). [PDF]
Int J Mol Sci, 2020 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 +6 more sources
Protein S-glutathionylation: a regulatory device from bacteria to humans
Trends in Biochemical Sciences, 2009 S-Glutathionylation is the specific post-translational modification of protein cysteine residues by the addition of the tripeptide glutathione, the most abundant and important low-molecular-mass thiol within most cell types. Protein S-glutathionylation is promoted by oxidative or nitrosative stress but also occurs in unstressed cells.
I. Dalle Donne +4 more
core +6 more sources
Redox Biology, 2016 Background: Oxidative stress is implicated in increased vascular permeability associated with metabolic disorders, but the underlying redox mechanism is poorly defined.
Jingyan Han +11 more
doaj +2 more sources
Redox Biology, 2023 Oxidative stress drives protein S-glutathionylation, which regulates the structure and function of target proteins and is implicated in the pathogenesis of many diseases.
Chenshuang Li +6 more
doaj +2 more sources
Protocol for detecting protein S-glutathionylation in Arabidopsis thaliana under oxidative stress using a non-transgenic chemical toolkit [PDF]
STAR ProtocolsSummary: 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