Results 1 to 10 of about 77,313 (353)

Glutathione Disulfide Liposomes - a Research Tool for the Study of Glutathione Disulfide Associated Functions and Dysfunctions. [PDF]

Biochem Biophys Rep, 2016
Glutathione disulfide (GSSG) is the oxidized form of glutathione (GSH). GSH is a tripeptide present in the biological system in mM concentration and is the major antioxidant in the body. An increase in GSSG reflects an increase in intracellular oxidative stress and is associated with disease sates.
Sadhu SS, Xie J, Zhang H, Perumal O, Guan X.   +4 more
europepmc   +5 more sources

Mechanistic insights on the reduction of glutathione disulfide by protein disulfide isomerase. [PDF]

Proc Natl Acad Sci U S A, 2017
Significance Protein disulfide isomerase (PDI) is a ubiquitous enzyme involved in disulfide bond formation during protein folding. It has been related to neurological diseases (Parkinson or Alzheimer’s) because of unfolded protein response phenomena.
Neves RPP, Fernandes PA, Ramos MJ.
europepmc   +5 more sources

NOV-002, a mimetic of glutathione disulfide [PDF]

Expert Opinion on Investigational Drugs, 2008
Oxidative signaling to modulate redox-sensitive cell functions is a heretofore unexploited approach to developing new drugs for poorly treated oncology indications, where current therapies are often only palliative and accompanied by severe toxicities.Clinical and non-clinical findings with NOV-002 (a mimetic of glutathione disulfide that represents ...
Danyelle M. Townsend, Christopher J. Pazoles, Kenneth D. Tew   +2 more
openaire   +4 more sources

Disulphide production by Ero1alpha-PDI relay is rapid and effectively regulated [PDF]

, 2010
The molecular networks that control endoplasmic reticulum (ER) redox conditions in mammalian cells are incompletely understood. Here, we show that after reductive challenge the ER steady-state disulphide content is restored on a time scale of seconds ...
Appenzeller-Herzog, Christian, Chin, King-Tung, Ellgaard, Lars, Riemer, Jan, Ron, David, Spiess, Martin, Zito, Ester   +6 more
core   +3 more sources

Cytosolic thioredoxin reductase 1 is required for correct disulfide formation in the ER [PDF]

, 2017
Folding of proteins entering the secretory pathway in mammalian cells frequently requires the insertion of disulfide bonds. Disulfide insertion can result in covalent linkages found in the native structure as well as those that are not, so‐called non ...
Elias SJ Arnér, Fourie AM, Greg J Poet, Marcel Lith, Marie Anne Pringle, Neil J Bulleid, Ojore BV Oka, Philip J Robinson, Zhenbo Cao   +8 more
core   +2 more sources

Redox linked flavin sites in extracellular decaheme proteins involved in microbe-mineral electron transfer [PDF]

, 2015
Extracellular microbe-mineral electron transfer is a major driving force for the oxidation of organic carbon in many subsurface environments. Extracellular multi-heme cytochromes of the Shewenella genus play a major role in this process but the mechanism
A Okamoto, AC Mitchell, AGW Leslie, AM Waterhouse, AS Beliaev, CL Reardon, D Coursolle, D Ghosal, DE Ross, DJ Richardson, DJ Richardson, DJ Richardson, DK Thompson, E Marsili, ED Brutinel, F Sievers, GF White, GM Boratyn, GN Murshudov, I Letunic, JK Fredrickson, L Shi, L Shi, MJ Daly, MJ Daly, MJ Edwards, MJ Edwards, MJ Edwards, MY El-Naggar, P Taylor, PD Adams, RJ Morris, RS Hartshorne, S Bailey, S Pirbadian, TA Clarke   +35 more
core   +1 more source

Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation [PDF]

, 2008
The activation of initiator protein tissue factor (TF) is likely to be a crucial step in the blood coagulation process, which leads to fibrin formation. The stimuli responsible for inducing TF activation are largely undefined.
Altmann, Berid, Dlugai, Silke, Engelmann, Bernd, Grahl, Lenka, Hess, Sonja, Konrad, Aldiko, Lorenz, Michael, Mackman, Nigel, Manukyan, Davit, Massberg, Steffen, Orschiedt, Lena, Reinhardt, Christoph, Ruddock, Lloyd, von Brühl, Marie Luise   +13 more
core   +3 more sources

The binding of the retro-analogue of glutathione disulfide to glutathione reductase. [PDF]

Journal of Biological Chemistry, 1990
The retro-analogue of glutathione disulfide was bound to the GSSG binding site of crystalline glutathione reductase. The binding mode revealed why the analogue is a very poor substrate in enzyme catalysis. The observed binding mode difference between natural substrate and retro-analogue is explained.
Georg E. Schulz, W Janes
openaire   +2 more sources

Cytosolic redox components regulate protein homeostasis via additional localisation in the mitochondrial intermembrane space [PDF]

, 2017
Oxidative protein folding is confined to the bacterial periplasm, endoplasmic reticulum and the mitochondrial intermembrane space. Maintaining a redox balance requires the presence of reductive pathways.
Cardenas-Rodriguez, Mauricio, Tokatlidis, Konstantinos   +1 more
core   +1 more source

Synthesis and structural characterization of a mimetic membrane-anchored prion protein [PDF]

, 2006
During pathogenesis of transmissible spongiform encephalopathies (TSEs) an abnormal form (PrPSc) of the host encoded prion protein (PrPC) accumulates in insoluble fibrils and plaques. The two forms of PrP appear to have identical covalent structures, but
Andrew C. Gill, Ansari AA, Atvinder K. Rullay, Bertozzi CR, Blanch EW, Borchelt D, Caughey B, Caughey B, Caughey B, Caughey BW, Critchley P, David H. Crout, Eberl H, Ferris A, Georges C, Gill AC, Govaerts C, Haire LF, Harris DA, Hornemann S, Ian D. Sylvester, Imanpreet K. Bath, Kazlauskaite J, Kazlauskaite J, Kenyon GL, King SA, Kirby L, Klein TR, Kocienski PJ, Legname G, Matthew R. Hicks, Mui B, Nosjean O, Pan KM, Poss AJ, Safar J, Seddon AM, Shyng SL, Stahl N, Stahl N, Teresa J. T. Pinheiro, Whitesell JK, Wuthrich K, Zahn R, Zhang ZY   +44 more
core   +1 more source