Evidence map›Paper›PMID 28451306›Full record

ArticleChemical science2017

Accessing human selenoproteins through chemical protein synthesis.

L Dery, P Sai Reddy, S Dery, R Mousa, O Ktorza, A Talhami, N Metanis

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
7.0field-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

24 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Selenium in Peptide Chemistry.Molecules (Basel, Switzerland) · 2023
    Review
  6. A versatileChemical science · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Selenocysteine-Mediated Expressed Protein Ligation of SELENOM.Methods in molecular biology (Clifton, N.J.) · 2018
    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

7 authors at 2 institutions in 1 country.

L DeryInstitute of Chemistry , The Hebrew University of Jerusalem , Edmond J. Safra, Givat Ram , Jerusalem 91904 , Israel . Email: Metanis@mail.huji.ac.il.
P Sai ReddyInstitute of Chemistry , The Hebrew University of Jerusalem , Edmond J. Safra, Givat Ram , Jerusalem 91904 , Israel . Email: Metanis@mail.huji.ac.il.
S DeryInstitute of Chemistry , The Hebrew University of Jerusalem , Edmond J. Safra, Givat Ram , Jerusalem 91904 , Israel . Email: Metanis@mail.huji.ac.il.
R MousaInstitute of Chemistry , The Hebrew University of Jerusalem , Edmond J. Safra, Givat Ram , Jerusalem 91904 , Israel . Email: Metanis@mail.huji.ac.il.
O KtorzaInstitute of Chemistry , The Hebrew University of Jerusalem , Edmond J. Safra, Givat Ram , Jerusalem 91904 , Israel . Email: Metanis@mail.huji.ac.il.
A TalhamiInstitute of Chemistry , The Hebrew University of Jerusalem , Edmond J. Safra, Givat Ram , Jerusalem 91904 , Israel . Email: Metanis@mail.huji.ac.il.
N MetanisInstitute of Chemistry , The Hebrew University of Jerusalem , Edmond J. Safra, Givat Ram , Jerusalem 91904 , Israel . Email: Metanis@mail.huji.ac.il.
Hebrew University of Jerusalem · ILJerusalem College of Technology · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human body contains 25 selenoproteins, which contain in their sequence the twenty-first encoded amino acid, selenocysteine. About a dozen of these proteins remain functionally uncharacterized or poorly studied. Challenges in accessing these selenoproteins using traditional recombinant expressions have prevented biological characterization thus far. Chemical protein synthesis has the potential to overcome these hurdles. Here we report the first total chemical syntheses of two human selenoproteins, selenoprotein M (SELM) and selenoprotein W (SELW). The synthesis of the more challenging protein SELM was enabled using recent advances in the field of selenocysteine chemistry. This approach allows the preparation of selenoproteins in milligram quantities and in homogenous form, which should open new horizons for future studies to pursue a fuller biological understanding of their role in health and disease.

Identifiers

PMID28451306
PMCPMC5364654
OpenAlexW2547137510

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.