Results 191 to 200 of about 8,996 (206)
Some of the next articles are maybe not open access.
Regulation of protein function by glutathionylation.
Free radical research, 2005The main function of reduced glutathione (GSH) is to protect from oxidative stress as a reactive oxygen scavenger. However, in the context of redox regulation, the ratio between GSH and its oxidized form (GSSG) determines the redox state of redox-sensitive cysteines in some proteins and, thus, acts as a signaling system.
openaire +2 more sources
Oxidized GAPDH transfers -glutathionylation to a nuclear protein Sirtuin-1 leading to apoptosis
Free Radical Biology and Medicine, 2021Naomi Hamburg +2 more
exaly
Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation
Molecules, 2021Maria Novichkova, Elena Kalinina
exaly
Analysis of glutathionylated proteins
Plant and Cell Physiology Supplement, 2003Ito, Hisashi +2 more
openaire +1 more source
S-Glutathionylation signaling in cell biology: Progress and prospects
European Journal of Pharmaceutical Sciences, 2012Anna Pastore, Fiorella Piemonte
exaly
Regulation by Reversible S-Glutathionylation: Molecular Targets Implicated in Inflammatory Diseases
Molecules and Cells, 2008John J Mieyal
exaly
DETECTION OF GLUTATHIONYLATED PROTEINS
2008JANSSEN-HEININGER YVONNE M +1 more
openaire +4 more sources
A Role for Glutathione Transferase Omega 1 (GSTO1-1) in the Glutathionylation Cycle
Journal of Biological Chemistry, 2013Deepthi Menon
exaly

