Results 101 to 110 of about 8,996 (206)
BiomoleculesThe oxidation of cysteines in crystallins is a major age-related modification associated with cataract formation. The purpose of this research was to determine the susceptibility of γS-crystallin to glutathionylation-induced oxidation and disulfide bond ...
Kate Halverson-Kolkind +5 more
doaj +1 more source
Cytosolic Isocitrate Dehydrogenase from Arabidopsis thaliana Is Regulated by Glutathionylation
Antioxidants, 2019 NADP-dependent (Nicotinamide Adénine Dinucléotide Phosphate-dependent) isocitrate dehydrogenases (NADP-ICDH) are metabolic enzymes involved in 2-oxoglutarate biosynthesis, but they also supply cells with NADPH. Different NADP-ICDH genes are
Adnan Khan Niazi +6 more
doaj +1 more source
Glutathionylation of Actin in the Dictyostelium Cytoskeleton
, 2015 Glutathione (GSH) is the most abundant antioxidant in living organisms. It is a small tripeptide composed of three amino acid residues; glutamate, cysteine and glycine.
Grosberg, Benjamin
core
Cross-Linking Protein Glutathionylation Mediated by O2‑Arylated Bis-Diazeniumdiolate “Double JS-K”
, 2016 Attachment of glutathione (GSH) to cysteine residues in proteins (S-glutathionylation) is a reversible post-translational modification that can profoundly alter protein structure and function.
Varun Kumar (400717) +7 more
core +1 more source
Effects of Cadmium on Actin Glutathionylation and Focal Adhesions [PDF]
, 2013 The toxic metal ion cadmium (Cd2+) is pro-oxidant and specifically disrupts the actin cytoskeleton in renal mesangial cells. This study investigated the role of Cd2+-mediated redox modulation of actin through protein S-glutathionylation and the effects ...
Choong, Grace Mei Yee
core
S-Glutathionylation in Monocyte and Macrophage (Dys)Function
, 2013 Atherosclerosis is a chronic inflammatory disease involving the accumulation of monocytes and macrophages in the vascular wall. Monocytes and macrophages play a central role in the initiation and progression of atherosclerotic lesion development ...
Reto Asmis, Hong Kim, Sarah Ullevig
core +1 more source
Reversible and Irreversible Protein Glutathionylation: Biological and Clinical Aspects
, 2011 INTRODUCTION: Depending in part on the glutathione:glutathione disulfide ratio, reversible protein glutathionylation to a mixed disulfide may occur.
Patrick S Callery +5 more
core +1 more source
Actin S-glutathionylation: evidence against a thiol-disulphide exchange mechanism
, 2003 Many proteins, including actin, are targets for S-glutathionylation, the reversible formation of mixed disulphides between protein cysteinyl thiol groups and glutathione (GSH) that can be induced in cells by oxidative stress.
A. Milzani +9 more
core +1 more source
, 2012 Protein glutathionylation in response to oxidative stress can affect both the stability and activity of target proteins. Mitochondrial thymidine kinase 2 (TK2) is a key enzyme in mitochondrial DNA precursor synthesis.
Sun, Ren, +3 more
core +1 more source
Nature CommunicationsThe presence of redox-active molecules containing catenated sulfur atoms (supersulfides) in living organisms has led to a review of the concepts of redox biology and its translational strategy.
Akiyuki Nishimura +15 more
doaj +1 more source