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In this paper, a two-step high pressure reducing system for FCEV is proposed.
We also demonstrate that TXNL6 is a novel reducing system for MsrA repair of cellular proteins whose lost functions upon methionine oxidation contribute to eye lens cataract formation.
The ability of TXNL6 to serve as a reducing system for MsrA-repair of α-crystallin/sHSP was also evaluated using CNBr.
To date, only DTT has been used as a reducing system for MsrA repair of cyt c and α-crystallin/sHSP in vitro [26] [27].
We chose to examine TXNL6 as a potential reducing system for the action of MsrA based on recent studies showing its importance in maintaining the viability of retinal cells in mice [38] [39].
Here, we provide evidence that a novel thioredoxin-like protein called thioredoxin-like 6 (TXNL6) can serve as a reducing system for MsrA repair of the essential lens chaperone α-crystallin/sHSP and mitochondrial cytochrome c.
Similar(34)
Mechanisms for aerosol formation, aerosol growth, emissions related to aerosol formation and in particular the development and testing of aerosol emission reducing systems for amine based post-combustion, are presently under study.
While rectangular flaps have been widely studied as both passive add-ons and in active drag reducing systems for bluff bodies, changing the basic geometry of the flap has not been explored in literature.
Given the important role for MsrA in lens function and the maintenance of key lens proteins, we sought to identify additional lens reducing systems for the MsrA function.
They also suggest that MsrA uses multiple reducing systems for its repair activity that may augment its function under different cellular conditions.
Of these, TXNL1, TXNL5 and TXNL6 contain the thioredoxin CXXC domain and therefore could also act on MsrA and as reducing systems for other Trx dependent enzymes.
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