[HTML][HTML] Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes

M Deponte - Biochimica et Biophysica Acta (BBA)-General Subjects, 2013 - Elsevier
BACKGROUND: Glutathione-dependent catalysis is a metabolic adaptation to chemical
challenges encountered by all life forms. In the course of evolution, nature optimized …

Thioredoxins, glutaredoxins, and peroxiredoxins—molecular mechanisms and health significance: from cofactors to antioxidants to redox signaling

EM Hanschmann, JR Godoy, C Berndt… - Antioxidants & redox …, 2013 - liebertpub.com
Abstract Thioredoxins (Trxs), glutaredoxins (Grxs), and peroxiredoxins (Prxs) have been
characterized as electron donors, guards of the intracellular redox state, and “antioxidants” …

Role of glutathione, glutathione transferase, and glutaredoxin in regulation of redox-dependent processes

EV Kalinina, NN Chernov, MD Novichkova - Biochemistry (Moscow), 2014 - Springer
Over the last decade fundamentally new features have been revealed for the participation of
glutathione and glutathione-dependent enzymes (glutathione transferase and glutaredoxin) …

Thioredoxin and glutaredoxin systems in plants: molecular mechanisms, crosstalks, and functional significance

Y Meyer, C Belin, V Delorme-Hinoux… - Antioxidants & redox …, 2012 - liebertpub.com
Abstract Thioredoxins (Trx) and glutaredoxins (Grx) constitute families of thiol
oxidoreductases. Our knowledge of Trx and Grx in plants has dramatically increased during …

Glutaredoxin systems

CH Lillig, C Berndt, A Holmgren - Biochimica et Biophysica Acta (BBA) …, 2008 - Elsevier
Glutaredoxins utilize the reducing power of glutathione to maintain and regulate the cellular
redox state and redox-dependent signaling pathways, for instance, by catalyzing reversible …

Molecular Mechanisms and Clinical Implications of Reversible Protein S-Glutathionylation

JJ Mieyal, MM Gallogly, S Qanungo… - Antioxidants & redox …, 2008 - liebertpub.com
Sulfhydryl chemistry plays a vital role in normal biology and in defense of cells against
oxidants, free radicals, and electrophiles. Modification of critical cysteine residues is an …

Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress

MM Gallogly, JJ Mieyal - Current opinion in pharmacology, 2007 - Elsevier
Reversible protein S-glutathionylation (protein-SSG) is an important post-translational
modification, providing protection of protein cysteines from irreversible oxidation and serving …

[PDF][PDF] Cytosolic monothiol glutaredoxins function in intracellular iron sensing and trafficking via their bound iron-sulfur cluster

U Mühlenhoff, S Molik, JR Godoy, MA Uzarska… - Cell metabolism, 2010 - cell.com
Iron is an essential nutrient for cells. It is unknown how iron, after its import into the cytosol, is
specifically delivered to iron-dependent processes in various cellular compartments. Here …

[HTML][HTML] Redox regulation via glutaredoxin-1 and protein S-glutathionylation

R Matsui, B Ferran, A Oh, D Croteau… - Antioxidants & Redox …, 2020 - el.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 …

Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system

C Berndt, CH Lillig, A Holmgren - American Journal of …, 2007 - journals.physiology.org
Reactive oxygen species (ROS) and the cellular thiol redox state are crucial mediators of
multiple cell processes like growth, differentiation, and apoptosis. Excessive ROS production …