Evidence map›Paper›PMID 25063811›Full record

ArticleThe Journal of biological chemistry2014

Regulation of selenocysteine incorporation into the selenium transport protein, selenoprotein P.

Sumangala P Shetty, Ravi Shah, Paul R Copeland

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
5.8field-weighted citation impact, top 4% 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

31 citing papers in PubMed, 54 citations in OpenAlex.

  1. Targeted extracellular degradation of LRP8 promotes ferroptosis in cancer cells.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Selenoprotein P as anJournal of clinical biochemistry and nutrition · 2020
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Molecular mechanism of selenoprotein P synthesis.Biochimica et biophysica acta. General subjects · 2018
    Review
  18. Review
  19. Article
  20. Article
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

3 authors at 1 institution in 1 country.

Sumangala P ShettyFrom the Department of Biochemistry and Molecular Biology, Rutgers Robert Wood Johnson Medical School, Piscataway, New Jersey 08854.
Ravi ShahFrom the Department of Biochemistry and Molecular Biology, Rutgers Robert Wood Johnson Medical School, Piscataway, New Jersey 08854.
Paul R CopelandFrom the Department of Biochemistry and Molecular Biology, Rutgers Robert Wood Johnson Medical School, Piscataway, New Jersey 08854 paul.copeland@rutgers.edu.
Rutgers, The State University of New Jersey · US

Funding

Functional Analysis of SBP2 and Selenocysteine IncorporationR01GM077073 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI COPELAND, PAUL R · 2006 to 2022
$5.5M
NIGMS NIH HHS GM077073NIGMS NIH HHS R01 GM077073
6 · The paper itself

Abstract

Selenoproteins are unique as they contain selenium in their active site in the form of the 21st amino acid selenocysteine (Sec), which is encoded by an in-frame UGA stop codon. Sec incorporation requires both cis- and trans-acting factors, which are known to be sufficient for Sec incorporation in vitro, albeit with low efficiency. However, the abundance of the naturally occurring selenoprotein that contains 10 Sec residues (SEPP1) suggests that processive and efficient Sec incorporation occurs in vivo. Here, we set out to study native SEPP1 synthesis in vitro to identify factors that regulate processivity and efficiency. Deletion analysis of the long and conserved 3'-UTR has revealed that the incorporation of multiple Sec residues is inherently processive requiring only the SECIS elements but surprisingly responsive to the selenium concentration. We provide evidence that processive Sec incorporation is linked to selenium utilization and that reconstitution of known Sec incorporation factors in a wheat germ lysate does not permit multiple Sec incorporation events, thus suggesting a role for yet unidentified mammalian-specific processes or factors. The relationship between our findings and the channeling theory of translational efficiency is discussed.

Indexed as

3' Untranslated RegionsAnimalsCell-Free SystemHep G2 CellsHumansLuciferasesModels, GeneticMutationProtein BiosynthesisRabbitsRatsRegulatory Sequences, Nucleic AcidRNA, MessengerRNA, Transfer, Amino AcylSeleniumSelenocysteine3' Untranslated RegionsLuciferasesRNA, MessengerRNA, Transfer, Amino AcylSeleniumSelenocysteineselenocysteinyl-tRNASelenoprotein PChannelingSeleniumSelenocysteineSelenocysteine Insertion Sequence (SECIS)SelenoproteinSEPP1Translation

Identifiers

PMID25063811
PMCPMC4155693
OpenAlexW2030210530

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.