Results 31 to 40 of about 53,702 (285)
Endoplasmic reticulum H₂O₂ : Ero1-driven generation and GPx-mediated detoxification [PDF]
Endoplasmic reticulum (ER) oxidoreductin 1 alpha (Ero1alpha) is an ER-resident oxidase, which utilizes molecular oxygen (O2) as terminal electron acceptor to produce disulfide bonds and hydrogen peroxide (H2O2).
Ramming, Thomas
core +1 more source
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
Intracellular glutathione pools are heterogeneously concentrated [PDF]
Glutathione is present in millimolar concentrations in the cell, but its relative distribution among cellular compartments remains elusive. We have chosen the endoplasmic reticulum (ER) as an example organelle to study compartment-specific glutathione ...
Christine Tachibana +8 more
core +1 more source
An Orally Bioavailable (Mice) Prodrug of Glutathione
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
Glutathione treatment protects the rat liver against injury after warm ischemia and Kupffer cell activation [PDF]
Background/Aim: The generation of reactive oxygen species by activated Kupffer cells (KC) may contribute to reperfusion injury of the liver during liver transplantation or resection.
Schauer, R. +11 more
core +1 more source
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
CydDC-mediated reductant export in Escherichia coli controls the transcriptional wiring of energy metabolism and combats nitrosative stress [PDF]
The glutathione/cysteine exporter CydDC maintains redox balance in Escherichia coli. A cydD mutant strain was used to probe the influence of CydDC upon reduced thiol export, gene expression, metabolic perturbations, intracellular pH homeostasis, and ...
Sanguinetti, Guido +17 more
core +1 more source
The physiological functions of mammalian endoplasmic oxidoreductin 1: on disulfides and more [PDF]
Significance: The oxidative process of disulfide-bond formation is essential for the folding of most secretory and membrane proteins in the endoplasmic reticulum (ER).
Ramming, Thomas +1 more
core +1 more source
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
Dithiophosphate-Induced Redox Conversions of Reduced and Oxidized Glutathione
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

