Results 41 to 50 of about 135,439,936 (222)

Atomic resolution crystal structure of glutaredoxin 1 fromPlasmodium falciparumand comparison with other glutaredoxins [PDF]

open access: yesActa Crystallographica Section D Biological Crystallography, 2013
Glutaredoxins (Grxs) are redox proteins that use glutathione ((γ)Glu-Cys-Gly; GSH) as a cofactor. Plasmodium falciparum has one classic dithiol (CXXC) glutaredoxin (glutaredoxin 1; PfGrx1) and three monothiol (CXXS) Grx-like proteins (GLPs), which have five residue insertions prior to the active-site Cys.
Manickam, Yogavel   +7 more
openaire   +2 more sources

Corrigendum to “NF‐κB inactivation attenuates the M1 macrophage polarization in experimental necrotizing enterocolitis by glutaredoxin‐1 deficiency.”

open access: yesCell Biology International, 2023
Luo, Y., Mo, D., Guo, H., Ye, C., Chen, B., Zhu, H., Deng, C., Deng, Q., Guo, C., & Qiu, L. (2022). NF‐κB inactivation attenuates the M1 macrophage polarization in experimental necrotizing enterocolitis by glutaredoxin‐1 deficiency.

semanticscholar   +1 more source

The mammalian peroxisomal membrane is permeable to both GSH and GSSG – Implications for intraperoxisomal redox homeostasis

open access: yesRedox Biology, 2023
Despite the large amounts of H2O2 generated in mammalian peroxisomes, cysteine residues of intraperoxisomal proteins are maintained in a reduced state.
Maria J. Ferreira   +6 more
doaj   +1 more source

Disturbances of the Lung Glutathione System in Adult Guinea Pigs Following Neonatal Vitamin C or Cysteine Deficiency

open access: yesAntioxidants, 2023
In premature infants receiving parenteral nutrition, oxidative stress is a trigger for the development of bronchopulmonary dysplasia, which is an important factor in the development of adult lung diseases. Neonatal vitamin C and glutathione deficiency is
Vitor Teixeira   +2 more
doaj   +1 more source

Hypoxia Affects the Antioxidant Activity of Glutaredoxin 3 in Scylla paramamosain through Hypoxia Response Elements

open access: yesAntioxidants, 2022
Hypoxia is a major environmental stressor that can damage the oxidation metabolism of crustaceans. Glutaredoxin (Grx) is a key member of the thioredoxin superfamily and plays an important role in the host’s defense against oxidative stress.
Yu-Kun Jie   +6 more
doaj   +1 more source

Intracellular glutathione pools are heterogeneously concentrated [PDF]

open access: yes, 2013
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   +12 more
core   +1 more source

Structural Aspects of the Distinct Biochemical Properties of Glutaredoxin 1 and Glutaredoxin 2 from Saccharomyces cerevisiae

open access: yesJournal of Molecular Biology, 2009
Glutaredoxins (Grxs) are small (9-12 kDa) heat-stable proteins that are ubiquitously distributed. In Saccharomyces cerevisiae, seven Grx enzymes have been identified. Two of them (yGrx1 and yGrx2) are dithiolic, possessing a conserved Cys-Pro-Tyr-Cys motif.
Discola, Karen Fulan   +8 more
openaire   +3 more sources

Lack of the antioxidant glutathione peroxidase-1 does not increase atherosclerosis in C57BL/J6 mice fed a high-fat diet

open access: yesJournal of Lipid Research, 2006
Oxidative stress is thought to contribute to the initiation and progression of atherosclerosis. As glutathione peroxidase-1 (Gpx1) is an antioxidant enzyme that detoxifies lipid hydroperoxides, we tested the impact of Gpx1 deficiency on atherosclerotic ...
Judy B. de Haan   +7 more
doaj   +1 more source

Impaired cross-talk between the thioredoxin and glutathione systems is related to ASK-1 mediated apoptosis in neuronal cells exposed to mercury

open access: yesRedox Biology, 2017
Mercury (Hg) compounds target both cysteine (Cys) and selenocysteine (Sec) residues in peptides and proteins. Thus, the components of the two major cellular antioxidant systems – glutathione (GSH) and thioredoxin (Trx) systems – are likely targets for ...
Vasco Branco   +6 more
doaj   +1 more source

Evidence for the dimerization-mediated catalysis of methionine sulfoxide reductase A from Clostridium oremlandii. [PDF]

open access: yesPLoS ONE, 2015
Clostridium oremlandii MsrA (CoMsrA) is a natively selenocysteine-containing methionine-S-sulfoxide reductase and classified into a 1-Cys type MsrA. CoMsrA exists as a monomer in solution.
Eun Hye Lee   +6 more
doaj   +1 more source

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