Chemical methods for mapping cysteine oxidation
Cysteine residues in proteins are subject to diverse redox chemistry. Oxidation of cysteine to
S-nitrosocysteine, cysteine sulfenic and sulfinic acids, disulfides and persulfides are a few …
S-nitrosocysteine, cysteine sulfenic and sulfinic acids, disulfides and persulfides are a few …
Assessment of glutathione/glutathione disulphide ratio and S-glutathionylated proteins in human blood, solid tissues, and cultured cells
D Giustarini, G Colombo, ML Garavaglia… - Free Radical Biology …, 2017 - Elsevier
Glutathione (GSH) is the major non-protein thiol in humans and other mammals, which is
present in millimolar concentrations within cells, but at much lower concentrations in the …
present in millimolar concentrations within cells, but at much lower concentrations in the …
Redox Regulation via Glutaredoxin-1 and Protein S-Glutathionylation
R Matsui, B Ferran, A Oh, D Croteau… - Antioxidants & Redox …, 2020 - liebertpub.com
Significance: Over the past several years, oxidative post-translational modifications of
protein cysteines have been recognized for their critical roles in physiology and …
protein cysteines have been recognized for their critical roles in physiology and …
Redox homeostasis in photosynthetic organisms: novel and established thiol-based molecular mechanisms
Significance: Redox homeostasis consists of an intricate network of reactions in which
reactive molecular species, redox modifications, and redox proteins act in concert to allow …
reactive molecular species, redox modifications, and redox proteins act in concert to allow …
Emerging chemistry and biology in protein glutathionylation
DSK Kukulage, NNJM Don, YH Ahn - Current opinion in chemical biology, 2022 - Elsevier
Protein S-glutathionylation serves a regulatory role in proteins and modulates distinct
biological processes implicated in health and diseases. Despite challenges in analyzing the …
biological processes implicated in health and diseases. Despite challenges in analyzing the …
Redox systems biology: harnessing the sentinels of the cysteine redoxome
JM Held - Antioxidants & redox signaling, 2020 - liebertpub.com
Significance: Cellular redox processes are highly interconnected, yet not in equilibrium, and
governed by a wide range of biochemical parameters. Technological advances continue …
governed by a wide range of biochemical parameters. Technological advances continue …
[HTML][HTML] Stochiometric quantification of the thiol redox proteome of macrophages reveals subcellular compartmentalization and susceptibility to oxidative perturbations
Posttranslational modifications of protein cysteine thiols play a significant role in redox
regulation and the pathogenesis of human diseases. Herein, we report the characterization …
regulation and the pathogenesis of human diseases. Herein, we report the characterization …
Defining the S-glutathionylation proteome by biochemical and mass spectrometric approaches
Protein S-glutathionylation (SSG) is a reversible post-translational modification (PTM)
featuring the conjugation of glutathione to a protein cysteine thiol. SSG can alter protein …
featuring the conjugation of glutathione to a protein cysteine thiol. SSG can alter protein …
Dysregulation of the glutaredoxin/S-glutathionylation redox axis in lung diseases
Glutathione is a major redox buffer, reaching millimolar concentrations within cells and high
micromolar concentrations in airways. While glutathione has been traditionally known as an …
micromolar concentrations in airways. While glutathione has been traditionally known as an …
Characterization of cellular oxidative stress response by stoichiometric redox proteomics
The thiol redox proteome refers to all proteins whose cysteine thiols are subjected to various
redox-dependent posttranslational modifications (PTMs) including S-glutathionylation …
redox-dependent posttranslational modifications (PTMs) including S-glutathionylation …