Formation of mixed disulfides between glutathione and the cysteines of some proteins (glutathionylation)
has been suggested as a mechanism through which protein functions can be …

Protein glutathionylation is a post‐translational modification consisting of the formation of a
mixed disulfide between protein cysteines and glutathione (GSH). To identify proteins …

Tumor-infiltrating immune cells can be conditioned by molecules released within the
microenvironment to thwart antitumor immune responses, thereby facilitating tumor growth. Among …

To identify proteins undergoing glutathionylation (formation of protein-glutathione mixed
disulfides) in human T cell blasts, we radiolabeled the glutathione pool with 35 S, exposed cells …

Objective— To better understand the role of lecithin:cholesterol acyltransferase (LCAT) in
lipoprotein metabolism through the genetic and biochemical characterization of families …

A prolonged sojourn above 5500 m induces muscle deterioration and accumulation of
lipofuscin in Caucasians, probably because of overproduction of reactive oxygen species (ROS). …

Correct folding is critical for the biological activities of proteins. As a contribution to a better
understanding of the protein (un)folding problem, we studied the effect of temperature and of …

Background and Purpose—A high degree of proteinuria has been reported in stroke-prone
spontaneously hypertensive rats (SHRSP). We studied the effect of salt loading on the …

The first sections of this review compile and discuss strategies and protocols for managing
plasma/serum as a source of biomarkers relevant to human disease. In many such cases, …

We show here that exposure to oxidative stress induces glutathione (GSH) modification of
protein cysteinyl residues (glutathionylation) in T cell blasts. Treating the cells with the oxidant …