Evidence map›Paper›PMID 23696641›Full record

ArticleThe Journal of biological chemistry2013

Translational redefinition of UGA codons is regulated by selenium availability.

Michael T Howard, Bradley A Carlson, Christine B Anderson, Dolph L Hatfield

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
5.5field-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

63 citing papers in PubMed, 105 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. The cell biology of ferroptosis.Nature reviews. Molecular cell biology · 2024
    Review
  6. Article
  7. "Alphabet" Selenoproteins: Their Characteristics and Physiological Roles.International journal of molecular sciences · 2023
    Review
  8. "Alphabet" Selenoproteins: Implications in Pathology.International journal of molecular sciences · 2023
    Review
  9. α-lipoic acid ameliorates consequences of copper overload by up-regulating selenoproteins and decreasing redox misbalance.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. A brain-specificLife science alliance · 2021
    Article
  17. The Effect of tRNAInternational journal of molecular sciences · 2021
    Article
  18. Ferroptosis: mechanisms and links with diseases.Signal transduction and targeted therapy · 2021
    Review
  19. Article
  20. Article

3 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

4 authors at 2 institutions in 1 country.

Michael T HowardDepartment of Human Genetics, University of Utah, Salt Lake City, Utah 84112, USA. mhoward@genetics.utah.edu
Bradley A Carlson
Christine B Anderson
Dolph L Hatfield
Center for Cancer Research · USUniversity of Utah · US

Funding

Biosynthesis of Selenocysteine and Its Incorporation into ProteinZIABC010767 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI HATFIELD, DOLPH · 2009 to 2014
$2.0M
Translational control of selenoprotein synthesisR21ES022716 · NIEHS · UNIVERSITY OF UTAH · PI HOWARD, MICHAEL T · 2013 to 2014
$408k
Intramural NIH HHSNIEHS NIH HHS R21 ES022716NIEHS NIH HHS R21ES022716
6 · The paper itself

Abstract

Incorporation of selenium into ~25 mammalian selenoproteins occurs by translational recoding whereby in-frame UGA codons are redefined to encode the selenium containing amino acid, selenocysteine (Sec). Here we applied ribosome profiling to examine the effect of dietary selenium levels on the translational mechanisms controlling selenoprotein synthesis in mouse liver. Dietary selenium levels were shown to control gene-specific selenoprotein expression primarily at the translation level by differential regulation of UGA redefinition and Sec incorporation efficiency, although effects on translation initiation and mRNA abundance were also observed. Direct evidence is presented that increasing dietary selenium causes a vast increase in ribosome density downstream of UGA-Sec codons for a subset of selenoprotein mRNAs and that the selenium-dependent effects on Sec incorporation efficiency are mediated in part by the degree of Sec-tRNA([Ser]Sec) Um34 methylation. Furthermore, we find evidence for translation in the 5'-UTRs for a subset of selenoproteins and for ribosome pausing near the UGA-Sec codon in those mRNAs encoding the selenoproteins most affected by selenium availability. These data illustrate how dietary levels of the trace element selenium can alter the readout of the genetic code to affect the expression of an entire class of proteins.

Indexed as

Dietary SupplementsAnimalsCodon, TerminatorLiverMaleMiceMice, TransgenicProtein BiosynthesisRNA, Transfer, Amino Acid-SpecificSeleniumSelenocysteineSelenoproteinsCodon, TerminatorRNA, Transfer, Amino Acid-SpecificSeleniumSelenocysteineSelenoproteinstRNA, selenocysteine-RecodingRibosome ProfilingSeleniumSelenocysteineSelenoproteinTransfer RNA (tRNA)Translation Control

Identifiers

PMID23696641
PMCPMC3707644
OpenAlexW2049093658

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.