2023
DOI: 10.3390/antiox12111906
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Deciphering the Role of Selenoprotein M

Lance G. A. Nunes,
Antavius Cain,
Cody Comyns
et al.

Abstract: Selenocysteine (Sec), the 21st amino acid, is structurally similar to cysteine but with a sulfur to selenium replacement. This single change retains many of the chemical properties of cysteine but often with enhanced catalytic and redox activity. Incorporation of Sec into proteins is unique, requiring additional translation factors and multiple steps to insert Sec at stop (UGA) codons. These Sec-containing proteins (selenoproteins) are found in all three domains of life where they often are involved in cellula… Show more

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Cited by 3 publications
(1 citation statement)
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“…Sec is considered the 21st amino acid ("stop codon-UGA") and is structurally like cysteine, but selenium replaces sulfur. This change enhances the catalytic and redox properties of selenocysteine [91,92]. tRNA-Sec regulates the synthesis of selenocysteine, which plays crucial role in the oxygen resilience (reducing reactive oxygen species) of OA G20.…”
Section: Discussionmentioning
confidence: 99%
“…Sec is considered the 21st amino acid ("stop codon-UGA") and is structurally like cysteine, but selenium replaces sulfur. This change enhances the catalytic and redox properties of selenocysteine [91,92]. tRNA-Sec regulates the synthesis of selenocysteine, which plays crucial role in the oxygen resilience (reducing reactive oxygen species) of OA G20.…”
Section: Discussionmentioning
confidence: 99%