Evidence map›Paper›PMID 22332041›Full record

ReviewAdvances in nutrition (Bethesda, Md.)2011

Biosynthesis of selenocysteine, the 21st amino acid in the genetic code, and a novel pathway for cysteine biosynthesis.

Anton A Turanov, Xue-Ming Xu, Bradley A Carlson, Min-Hyuk Yoo, Vadim N Gladyshev, Dolph L Hatfield

Open access · greenAbstract readReview
In one paragraph

Review in Advances in nutrition (Bethesda, Md.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
5.9field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

62 citing papers in PubMed, 174 citations in OpenAlex.

  1. Review
  2. Global loss of selenocysteine lyase in mice drives lipid accumulation in brown adipocytes.American journal of physiology. Endocrinology and metabolism · 2026
    Article
  3. Review
  4. Review
  5. Article
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  7. Article
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  11. Article
  12. Review
  13. Article
  14. Biological Activity of Selenium and Its Impact on Human Health.International journal of molecular sciences · 2023
    Review
  15. Review
  16. Review
  17. Article
  18. SEPHS1: Its evolution, function and roles in development and diseases.Archives of biochemistry and biophysics · 2022
    Article
  19. Selenoprotein: Potential Player in Redox Regulation inAntioxidants (Basel, Switzerland) · 2022
    Article
  20. Review

2 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Anton A TuranovDivision of Genetics, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA.
Xue-Ming Xu
Bradley A Carlson
Min-Hyuk Yoo
Vadim N Gladyshev
Dolph L Hatfield
National Institutes of Health · USBrigham and Women's Hospital · US

Funding

IDENTITY OF TERMINATOR AND SELENOCYSTEINE UGA CODONSR01GM061603 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI GLADYSHEV, VADIM N. · 2000 to 2016
$4.0M
Biosynthesis of Selenocysteine and Its Incorporation into ProteinZIABC010767 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI HATFIELD, DOLPH · 2009 to 2014
$2.0M
Intramural NIH HHSNIGMS NIH HHS R01 GM061603
6 · The paper itself

Abstract

The biosynthetic pathway for selenocysteine (Sec), the 21st amino acid in the genetic code whose codeword is UGA, was recently determined in eukaryotes and archaea. Sec tRNA, designated tRNA([Ser]Sec), is initially aminoacylated with serine by seryl-tRNA synthetase and the resulting seryl moiety is converted to phosphoserine by O-phosphoseryl-tRNA kinase to form O-phosphoseryl-tRNA([Ser]Sec). Sec synthase (SecS) then uses O-phosphoseryl-tRNA([Ser]Sec) and the active donor of selenium, selenophosphate, to form Sec-tRNA([Ser]Sec). Selenophosphate is synthesized from selenide and ATP by selenophosphate synthetase 2 (SPS2). Sec was the last protein amino acid in eukaryotes whose biosynthesis had not been established and the only known amino acid in eukaryotes whose biosynthesis occurs on its tRNA. Interestingly, sulfide can replace selenide to form thiophosphate in the SPS2-catalyzed reaction that can then react with O-phosphoseryl-tRNA([Ser]Sec) in the presence of SecS to form cysteine-(Cys-)tRNA([Ser]Sec). This novel pathway of Cys biosynthesis results in Cys being decoded by UGA and replacing Sec in normally selenium-containing proteins (selenoproteins). The selenoprotein, thioredoxin reductase 1 (TR1), was isolated from cells in culture and from mouse liver for analysis of Cys/Sec replacement by MS. The level of Cys/Sec replacement in TR1 was proportional to the level of selenium in the diet of the mice. Elucidation of the biosynthesis of Sec and Sec/Cys replacement provides novel ways of regulating selenoprotein functions and ultimately better understanding of the biological roles of dietary selenium.

Indexed as

AnimalsArchaeaCysteineEukaryotaGenetic CodeGenomicsMiceSelenocysteineSelenoproteinsCysteineSelenocysteineSelenoproteins

Identifiers

PMID22332041
PMCPMC3065758
OpenAlexW2149005038

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.