Results 51 to 60 of about 8,445 (200)
S-glutathionylation in cancer: from fundamental mechanisms to clinical applications
Pharmacological ResearchGlutathione (GSH) is a thiol-containing antioxidant composed of glutamic acid, cysteine and glycine. GSH can form a disulfide bond with the cysteine sulfhydryl group of a protein, resulting in S-glutathionylation (-SSG).
Shuai Dong +4 more
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Glutathionylation of
mBio, 2017 Glutathionylation, the formation of reversible mixed disulfides between glutathione and protein cysteine residues, is a posttranslational modification previously observed for intracellular proteins of bacteria.
Anthony Mitchell +7 more
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BMC Plant Biology, 2021 Background Flexibility of plant metabolism is supported by redox regulation of enzymes via posttranslational modification of cysteine residues, especially in plastids.
Stefanie J. Müller-Schüssele +5 more
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Metal‐dependent regulated cell death: Molecular architecture and translational frontiers
iMeta, EarlyView.Intracellular metal dyshomeostasis orchestrates distinct regulated cell death programs, including iron‐driven ferroptosis, copper‐mediated cuproptosis, calcicoptosis, newly designated zincoptosis, mnoptosis, and coptosis. This review systematically delineates their molecular architectures—spanning from Sorafenib‐induced lipid peroxidation and ...
Haoliang Hu +20 more
wiley +1 more source
GSTpi regulates VE-cadherin stabilization through promoting S-glutathionylation of Src
Redox Biology, 2020 GSTpi is a Phase II metabolic enzyme which is originally considered as an important facilitator of cellular detoxification. Here, we found that GSTpi stabilized VE-cadherin in endothelial cell membrane through inhibiting VE-cadherin phosphorylation and ...
Yang Yang +10 more
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Cells, 2022 Cellular redox homeostasis is precisely balanced by generation and elimination of reactive oxygen species (ROS). ROS are not only capable of causing oxidation of proteins, lipids and DNA to damage cells but can also act as signaling molecules to modulate
Hong Zhang +3 more
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Ion Activation Methods for Top‐Down Proteomics
Mass Spectrometry Reviews, EarlyView.ABSTRACT Mass spectrometry (MS) has emerged as a premier method used to characterize the sequences of proteins. Top‐down proteomics aims to capture the multiple sources of structural diversity reflected in proteins, such as those that arise from alternative RNA splicing events or the addition of post‐translational modifications. Tandem MS (i.e., MS/MS)
Jada N. Walker, Jennifer S. Brodbelt
wiley +1 more source
Molecular mechanisms and potential clinical significance of S-glutathionylation
, 2008 Protein S-glutathionylation, the reversible binding of glutathione to protein thiols (PSH), is involved in protein redox regulation, storage of glutathione, and protection of PSH from irreversible oxidation.
A. Milzani +11 more
core +2 more sources
Russian wheat aphid: a model for genomic plasticity and a challenge to breeders
Insect Science, EarlyView.Invasive foundress finds suitable habitat and reproduces through pathogenesis. Wingless females produce life offspring quickly, which leads to high population densities. High population densities result in competition, which may induce epigenetic changes and wing development for dispersal.
Astrid Jankielsohn +8 more
wiley +1 more source
Glutathionylation of the Na K Pump [PDF]
Biophysical Journal, 2014 Reversible oxidative modifications of proteins are of importance for the normal cell functioning, e.g. for the receptor-coupled signaling. The formation of a disulfide bond between a protein and a glutathione tripeptide (Glu-Cys-Gly,) is an oxidative, posttranslational modification that might be involved in the cellular signaling.
Kopec, Wojciech +2 more
openaire +1 more source