Results 41 to 50 of about 53,702 (285)

Destroy and exploit: catalyzed removal of hydroperoxides from the endoplasmic reticulum [PDF]

, 2013
Peroxidases are enzymes that reduce hydroperoxide substrates. In many cases, hydroperoxide reduction is coupled to the formation of a disulfide bond, which is transferred onto specific acceptor molecules, the so-called reducing substrates.
Thomas Ramming, Ramming, Thomas, Appenzeller-Herzog, Christian, Christian Appenzeller-Herzog   +3 more
core   +1 more source

Intact protein folding in the glutathione-depleted endoplasmic reticulum implicates alternative protein thiol reductants

eLife, 2014
Protein folding homeostasis in the endoplasmic reticulum (ER) requires efficient protein thiol oxidation, but also relies on a parallel reductive process to edit disulfides during the maturation or degradation of secreted proteins.
Satoshi Tsunoda, Edward Avezov, Alisa Zyryanova, Tasuku Konno, Leonardo Mendes-Silva, Eduardo Pinho Melo, Heather P Harding, David Ron   +7 more
doaj   +1 more source

The Redox Potential of the β-⁹³-Cysteine Thiol Group in Human Hemoglobin Estimated from In Vitro Oxidant Challenge Experiments

Molecules, 2021
Glutathionyl hemoglobin is a minor form of hemoglobin with intriguing properties. The measurement of the redox potential of its reactive β-93-Cysteine is useful to improve understanding of the response of erythrocytes to transient and chronic conditions ...
Federico Maria Rubino
doaj   +1 more source

Capillary Isotachophoresis Determination of Trace Oxidized Glutathione in Blood

Hungarian Journal of Industry and Chemistry, 2018
A capillary isotachophoresis (CITP) method performed in a column-coupling apparatus has been developed for the simultaneous determination of glutathione (GSH) and glutathione disulfide (GSSG) concentrations in blood samples. The determination of GSSG and
Bodor Robert, Nečasová Andrea, Pechová Alena, Masár Marián   +3 more
doaj   +1 more source

Glutaredoxin catalysis requires two distinct glutathione interaction sites

Nature Communications, 2017
Glutaredoxins have important roles in redox processes. Here the authors show that the enzymatic activity of glutaredoxins requires two distinct glutathione interactions sites, one recognizing the glutathione disulfide substrate and one activating ...
Patricia Begas, Linda Liedgens, Anna Moseler, Andreas J. Meyer, Marcel Deponte   +4 more
doaj   +1 more source

Pathogenic effects of plasma thiols in patients with psoriasis on background of arterial hypertension

Aktualʹnì Pitannâ Farmacevtičnoï ì Medičnoï Nauki ta Praktiki, 2016
Objective: to study the features of metabolism of nitric oxide and thiol-disulfide balance parameters in patients with psoriasis combined with essential hypertension. Materials and metods.
G. I. Makurina
doaj   +1 more source

Environmental toxicity, redox signaling and lung inflammation:the role of glutathione [PDF]

, 2009
Glutathione (gamma-glutamyl-cysteinyl-glycine, GSH) is the most abundant intracellular antioxidant thiol and is central to redox defense during oxidative stress.
Saibal K. Biswas, Biswas, Saibal K, Rahman, Irfan, Irfan Rahman   +3 more
core   +1 more source

Thiol−Disulfide Exchange between Glutaredoxin and Glutathione

, 2016
Glutaredoxins are ubiquitous thiol−disulfide oxidoreductases which catalyze the reduction of glutathione−protein mixed disulfides. Belonging to the thioredoxin family, they contain a conserved active site CXXC motif.
Kristine Steen Jensen (1885651), Bent W. Sigurskjold (2321731), Jakob R. Winther (559350), Rasmus Iversen (780323), Peter Anders Andersen (2321728)   +4 more
core   +2 more sources

Mitochondrial thiol-disulfide system under acute hypoxia and hypoxic-hyperoxic adaptation [PDF]

The Ukrainian Biochemical Journal, 2014
The authors investigated the state of mitochondrial glutathione pool (reduced and oxidized glutathione, protein-GSH mixed disulfides), content of carbonyl groups and free sulfhydryl groups of proteins, protein expression of key mitochondrial antioxidant ...
O. A. Gonchar, I. N. Mankovska
doaj   +1 more source

The Eye Lens Protein, γS Crystallin, Undergoes Glutathionylation-Induced Disulfide Bonding Between Cysteines 22 and 26

Biomolecules
The 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, David C. Thorn, Martin Tovar-Ramirez, Eugene Shakhnovich, Larry David, Kirsten Lampi   +5 more
doaj   +1 more source