Results 21 to 30 of about 48,461 (279)

An Orally Bioavailable (Mice) Prodrug of Glutathione

open access: yesAntioxidants, 2021
L-Cysteine-glutathione mixed disulfide (CySSG), a prodrug of glutathione (GSH), was found to be orally bioavailable in mice, and protected mice against a toxic dose of acetaminophen.
Daune L. Crankshaw   +3 more
doaj   +1 more source

Hepatocyte Hyperproliferation upon Liver-Specific Co-disruption of Thioredoxin-1, Thioredoxin Reductase-1, and Glutathione Reductase

open access: yesCell Reports, 2017
Energetic nutrients are oxidized to sustain high intracellular NADPH/NADP+ ratios. NADPH-dependent reduction of thioredoxin-1 (Trx1) disulfide and glutathione disulfide by thioredoxin reductase-1 (TrxR1) and glutathione reductase (Gsr), respectively ...
Justin R. Prigge   +16 more
doaj   +1 more source

Dithiophosphate-Induced Redox Conversions of Reduced and Oxidized Glutathione

open access: yesMolecules, 2021
Phosphorus species are potent modulators of physicochemical and bioactive properties of peptide compounds. O,O-diorganyl dithiophoshoric acids (DTP) form bioactive salts with nitrogen-containing biomolecules; however, their potential as a peptide ...
Rezeda A. Ishkaeva   +8 more
doaj   +1 more source

Differential activity of rice protein disulfide isomerase family members for disulfide bond formation and reduction

open access: yesFEBS Open Bio, 2014
Protein disulfide isomerases (PDIs), a family of thiol-disulfide oxidoreductases that are ubiquitous in all eukaryotes, are the principal catalysts for disulfide bond formation. Here, we investigated three rice (Oryza sativa) PDI family members (PDIL1;1,
Yayoi Onda, Yohei Kobori
doaj   +1 more source

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

open access: yeseLife, 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   +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

open access: yesMolecules, 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

Glutathione Peroxide and Glutathione to Disulfide Glutathione Ratio in Presbycusis: a Case-control Study

open access: yesMedical Archives, 2022
Background: Presbycusis is a gradual hearing loss caused by the ageing process. This is a chronic condition that affects the elderly population, and sensorineural progressive bilateral symmetry occurs with predominantly high-frequency hearing loss. The ability to discriminate speech decreases; hence, most of the affected patients have conversation ...
Hasansulama, Wijana   +3 more
openaire   +2 more sources

Capillary Isotachophoresis Determination of Trace Oxidized Glutathione in Blood

open access: yesHungarian 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   +3 more
doaj   +1 more source

Energy‐linked cardiac transport system for glutathione disulfide [PDF]

open access: yesFEBS Letters, 1986
The relationship between the rate of glutathione disulfide (GSSG) export and the energy state was studied in isolated perfused rat heart. The intracellular GSSG level was maintained at saturation for transport (7.5 nmol GSSG · min−1 · g heart−1) by continuous perfusion with 20 μM t‐butyl hydroperoxide. GSSG release was substantially restricted upon the
Ishikawa, T., Zimmer, M., Sies, H.
openaire   +2 more sources

Glutaredoxin catalysis requires two distinct glutathione interaction sites

open access: yesNature 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   +4 more
doaj   +1 more source

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