Evolutionarily Conserved Role of Thioredoxin Systems in Determining Longevity
Antioxidants, 2023 Thioredoxin and thioredoxin reductase are evolutionarily conserved antioxidant enzymes that protect organisms from oxidative stress. These proteins also play roles in redox signaling and can act as a redox-independent cellular chaperone.
Abdelrahman Alokda +2 more
exaly +4 more sources
Physiological functions of thioredoxin and thioredoxin reductase [PDF]
FEBS Journal, 2000 Thioredoxin, thioredoxin reductase and NADPH, the thioredoxin system, is ubiquitous from Archea to man. Thioredoxins, with a dithiol/disulfide active site (CGPC) are the major cellular protein disulfide reductases; they therefore also serve as electron donors for enzymes such as ribonucleotide reductases, thioredoxin peroxidases (peroxiredoxins) and ...
Elias S J Arner, Arne Holmgren
exaly +3 more sources
FEBS Journal, 2000 The mammalian thioredoxin reductases (TrxRs) are a family of selenium-containing pyridine nucleotide-disulphide oxidoreductases with mechanistic and sequence identity, including a conserved -Cys-Val-Asn-Val-Gly-Cys- redox catalytic site, to glutathione reductases.
Charles H Williams +2 more
exaly +3 more sources
Fluorogenic probes for thioredoxin reductase activity
Results in Chemistry, 2021 The thioredoxin system is vital in maintaining the cellular redox state and is implicated in various cancers and other diseases. It comprises of thioredoxin reductase, thioredoxin and NADPH.
Tendai J. Mafireyi +2 more
doaj +3 more sources
Dual-Target Insight into Drug Discovery from Natural Products as Modulators of GLP-1 and the TXNIP–Thioredoxin Antioxidant System in Metabolic Syndrome [PDF]
AntioxidantsMetabolic Syndrome (MetS), a cluster of interconnected metabolic abnormalities, poses a growing global health burden. A well-established therapeutic target for the diseases is the incretin hormone glucagon-like peptide-1 (GLP-1); however, synthetic ...
Peter Chinedu Agu +2 more
doaj +2 more sources
The over expression of thioredoxin during malignancies [PDF]
Reviews in Clinical Medicine, 2014 Thioredoxin system comprised of thiorexin and NADPH dependent thiorexin reductase, is responsible for redox regulation of cells by controlling the apoptosis, proliferation and other vital processes of cells.
Shahaboddin Shabani +2 more
doaj +3 more sources
JS-K, a nitric oxide prodrug, has enhanced cytotoxicity in colon cancer cells with knockdown of thioredoxin reductase 1. [PDF]
PLoS ONE, 2010 The selenoenzyme thioredoxin reductase 1 has a complex role relating to cell growth. It is induced as a component of the cellular response to potentially mutagenic oxidants, but also appears to provide growth advantages to transformed cells by inhibiting
Kornelia Edes +3 more
doaj +1 more source
The Cellular Thioredoxin-1/Thioredoxin Reductase-1 Driven Oxidoreduction Represents a Chemotherapeutic Target for HIV-1 Entry Inhibition. [PDF]
PLoS ONE, 2016 BACKGROUND:The entry of HIV into its host cell is an interesting target for chemotherapeutic intervention in the life-cycle of the virus. During entry, reduction of disulfide bridges in the viral envelope glycoprotein gp120 by cellular oxidoreductases is
Kathrin Reiser +9 more
doaj +1 more source
Tissue Distribution and Activity of Thioredoxin Reductase in Pancreatic Carcinoma [PDF]
Middle East Journal of Cancer, 2019 Background: Thioredoxin, NADPH, and thioredoxin reductase form the thioredoxinsystem which exists in all living cells. Oxidants have a major role in cancer pathogenesis;therefore, it is necessary to study the role of redox-active compounds such as ...
Faezeh Sadrabadi Haghighi +3 more
doaj +1 more source
Redox Regulation by Thioredoxin and Thioredoxin‐Binding Proteins [PDF]
IUBMB Life, 2001 AbstractRecent works have shown the importance of reduction/oxidation (redox) regulation in various biological phenomena. Thioredoxin is a 12‐kDa protein with redox‐active dithiol in the active site ‐Cys‐Gly‐Pro‐Cys‐ and constitutes a major thiol reducing system, the thioredoxin system.
A, Nishiyama +4 more
openaire +2 more sources