21 papers · ranked by Valyu relevance
Emmanuel Mukwevho, Zané Ferreira, Ademola Ayeleso, Noriyuki Nagahara
All forms of life maintain a reducing environment (homeostasis) within their cells. Perturbations in the normal redox state can lead to an oxidative environment which has deleterious effects, especially in health. In biological systems, metabolic activities are dependent mainly on mitochondrial oxidative…
Haseena P. A., Latha Diwakar, Vijayalakshmi Ravindranath, Stanley Omaye
'Stanley Omaye'] Oxidative stress has been implicated in the pathogenesis and progression of many neurodegenerative disorders including Parkinson’s disease and Alzheimer’s disease. One of the major enzyme systems involved in the defense against reactive oxygen species are the tripeptide glutathione and oxidoreductase…
Mannix Burns, Syed Husain Mustafa Rizvi, Yuko Tsukahara, David R. Pimentel + 4 more
'David R. Pimentel' 'Ivan Luptak' 'Naomi M. Hamburg' 'Reiko Matsui' 'Markus M. Bachschmid'] Cardiovascular diseases are the leading cause of death worldwide, and as rates continue to increase, discovering mechanisms and therapeutic targets become increasingly important. An underlying cause of most cardiovascular…
Ana M. Sánchez-Riego, Luis López-Maury, Francisco J. Florencio
Glutaredoxins are small redox proteins able to reduce disulfides and mixed disulfides between GSH and proteins. Synechocystis sp. PCC 6803 contains three genes coding for glutaredoxins: ssr2061 (grxA) and slr1562 (grxB) code for dithiolic glutaredoxins while slr1846 (grxC) codes for a monothiolic glutaredoxin. We have…
Yuh-Cherng Chai, John J. Mieyal, Stanley Omaye
This Special Issue of Antioxidants on Glutathione (GSH) and Glutaredoxin (Grx) was designed to collect review articles and original research studies focused on advancing the current understanding of the roles of the GSH/Grx system in cellular homeostasis and disease processes. The tripeptide glutathione (GSH) is the…
Thomas Leeper, Suxin Zhang, Wesley C. Van Voorhis, Peter J. Myler + 1 more
'Gabriele Varani'] NMR structures of the glutaredoxin (GLXR) domains from Br. melitensis and Ba. henselae have been determined as part of the SSGCID initiative. Comparison of the domains with known structures reveals overall structural similarity between these proteins and previously determined E. coli GLXR structures…
Fernando T. Ogata, Vasco Branco, Filipa F. Vale, Lucia Coppo
Glutaredoxin, Grx, is a small protein containing an active site cysteine pair and was discovered in 1976 by Arne Holmgren. The Grx system, comprised of Grx, glutathione, glutathione reductase, and NADPH, was first described as an electron donor for Ribonucleotide Reductase but, from the first discovery in E.coli, the…
Fabian Geissel, Lukas Lang, Britta Husemann, Bruce Morgan + 1 more
Glutaredoxins catalyze the reduction of disulfides and are key players in redox metabolism and regulation. While important insights were gained regarding the reduction of glutathione disulfide substrates, the mechanism of non-glutathione disulfide reduction remains highly debated. Here we determined the rate constants…
R. M. Saravana Kumar, S.V. Ramesh, Z. Sun, Sugitha Thankappan + 1 more
Glutaredoxins (Grxs) are small, ubiquitous, multi-functional proteins present in different compartments of plant cells. A chloroplast targeted class I GRX (CcGRXS12) gene was isolated from Capsicum chinense during the pepper mild mottle virus (PMMoV) infection. Functional characterization of the gene was performed in…
Sreeshma Nellootil Sreekumar, Bhaba Krishna Das, Rahul Raina, Neethu Puthumadathil + 10 more
Glutaredoxins (Grxs) are single-domain redox enzymes of the thioredoxin superfamily, and primarily function as glutathione (GSH) dependent disulphide reductases. Whereas, the E. coli Glutaredoxin 2 (EcGrx2) encoded by grxB has two conserved GST-fold domains, it still lacks a classical Grx-like functions. In this study…
Inna Rozman Grinberg, Daniel Lundin, Margareta Sahlin, Mikael Crona + 3 more
Class I ribonucleotide reductase (RNR) consists of a catalytic subunit (NrdA) and a radical-generating subunit (NrdB) that together catalyse reduction of the four ribonucleotides to their corresponding deoxyribonucleotides. Facklamia ignava NrdB is an unprecedented fusion protein with N-terminal add-ons of a…
Anja Maren Pelizaeus, Corinna Thurow, Lisa Oskam, Ben Moritz Hoßbach + 3 more
In Arabidopsis thaliana, nitrogen (N) starvation leads to increased synthesis of CEPD (C-TERMINALLY ENCODED PEPTIDE DOWNSTREAM) proteins in the shoot. CEPDs travel to the roots, where they activate expression of genes required for high affinity nitrate transport. CEPDs belong to a plant-specific class of…
Lisa R. Knoke, Maik Muskietorz, Lena Kühn, Lars I. Leichert
Glutathione is the major thiol-based antioxidant in a wide variety of biological systems, ranging from bacteria to eukaryotes. As a redox couple, consisting of reduced glutathione (GSH) and oxidized glutathione disulfide (GSSG), it is crucial for the maintenance of the cellular redox balance. Glutathione transport out…
Qianhui Dou, Anton A. Turanov, Marco Mariotti, Jae Yeon Hwang + 7 more
Thioredoxin/glutathione reductase (TGR, TXNRD3) is a thiol oxidoreductase of unknown function composed of thioredoxin reductase and glutaredoxin domains. This NADPH-dependent enzyme evolved by gene duplication within the Txnrd family, is expressed in the testes and can reduce both thioredoxin and glutathione in vitro.…
Lukas Zeisel, Jan G. Felber, Lena Poczka, Karoline Scholzen + 5 more
Dynamically driven cellular redox networks power a broad range of physiological cellular processes, and additionally are often dysregulated in various pathologies including cancer and inflammatory diseases. Therefore it is vital to be able to image and to respond to the turnover of the key players in redox homeostasis…
Samrat Roy Choudhury, Arunava Goswami
The antifungal effects of orthorhombic (~10 nm; spherical) and monoclinic (~50 nm; tetrapod) sulfur nanoparticles (SNPs) were studied against the NADPH-dependent glutathione reductase (GR) mediated xenobiotic detoxification system (GSH-GSSG) in filamentous fungi (Aspergillus niger as a model organism). Both the SNPs…
Vishnu R. Chari, Raghu Nath Behera
In the search for small organoselenium-based mimics of the glutathione peroxidase (GPx) enzyme, it has been observed that selenenyl sulfides (RSeSG) derived from amine-based GPx mimics have the potential to be reduced at the catalytic site of glutathione reductase (GR), thereby enhancing the catalytic efficiency of…
Vincent Nivière, Marc Fontecave
For more than thirty years, the only enzymatic system known to catalyze the elimination of superoxide was superoxide dismutase, SOD. SOD has been found in almost all organisms living in the presence of oxygen, including some anaerobic bacteria, supporting the notion that superoxide is a key and general component of…
Chad K. Park, Nancy C. Horton
Filament formation by non-cytoskeletal enzymes has been known for decades, yet only relatively recently has its wide-spread role in enzyme regulation and biology come to be appreciated. This comprehensive review summarizes what is known for each enzyme confirmed to form filamentous structures in vitro, and for the many…
Authors not listed
Electrochemiluminescence (ECL) enables highly sensitive bioanalytical detection; however, its practical application is constrained by strong optical absorption in colored or optically dense samples, which significantly attenuates the emitted signal. In this study, we address this limitation by employing transparent…
Qingyang Hu, Hantian You, Kenan Li, Luhua Lai + 1 more
Ferroptosis is a form of cell death discovered in recent years, induced by excessive peroxidation of phospholipids. Glutathione peroxidase 4 (GPx4) is an intracellular enzyme that can repair the peroxidized phospholipids on membranes, thus regulating ferroptosis. By combining multiscale molecular dynamics (MD)…