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Thioredoxin reductase 1 (TR1) is a major redox regulator in mammalian cells.
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It has been recently shown that TXNIP binds to TRX and regulates the activity of this protein as a major cellular redox regulator [ 9, 10].
Thioredoxin reductase 1 (TR1) is one of 24 known selenoproteins in rodents [4], is a major antioxidant and redox regulator in mammalian cells [5,6 and references therein] and has an essential role in mammalian development [7].
The brain tissue displayed the greatest magnitude of response for redox regulators, with 7 of 8 redox regulators up-regulated 2-fold or greater compared to the liver in which only 5 were found up-regulated and only 1 redox regulator up-regulated 2-fold or more.
Glutathione (GSH) is the major cellular redox-regulator and antioxidant.
However, it presents a redox motif (CXXU), where U is a selenocysteine, and may also function as redox regulator because its decreased or increased expression regulated by dietary selenium alters redox homeostasis.
We show that the TRX redox regulator is a physiologically relevant trigger of autolysis and identify the major autolytic forms, which are in good correlation with previous observations.
In addition, mutations of sod2/3 or the redox regulator daf-16 abolished the negative correlation between ROS and paraquat levels, suggesting major effects of the excessive response was contributed by the antioxidant system (Ren et al., 2017).
GSH is the chief endogenous redox regulator and is drastically reduced under oxidative stress.
This HSA implication in disulfides formation supports a relevant function of HSA-SH as an extracellular redox regulator (Figure 1) [42].
H2S can undergo a number of abiotic side reactions with other major redox species (Table 1).
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