Evidence map›Paper›PMID 36241082›Full record

ReviewArchives of biochemistry and biophysics2022

Selenoprotein S: A versatile disordered protein.

Farid Ghelichkhani, Fabio A Gonzalez, Mariia A Kapitonova, Stephanie Schaefer-Ramadan, Jun Liu, Rujin Cheng, Sharon Rozovsky

Open access · greenAbstract readReview
In one paragraph

Review in Archives of biochemistry and biophysics, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

20 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. The protective effects of selenium against NLRP3-mediated inflammation and pyroptosis: mechanisms and the potential health benefits.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Selenoprotein K at the intersection of cellular pathways.Archives of biochemistry and biophysics · 2025
    Review
  13. Review
  14. Article
  15. Review
  16. Current understanding of essential trace elements in intrahepatic cholestasis of pregnancy.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024
    Review
  17. Article
  18. Article
  19. "Alphabet" Selenoproteins: Their Characteristics and Physiological Roles.International journal of molecular sciences · 2023
    Review
  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

7 authors at 4 institutions in 2 countries.

Farid GhelichkhaniDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE, 19716, USA.
Fabio A GonzalezDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE, 19716, USA.
Mariia A KapitonovaDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE, 19716, USA.
Stephanie Schaefer-RamadanDepartment of Genetic Medicine, Weill Cornell Medicine in Qatar, Doha, Qatar.
Jun LiuEnlaza Therapeutics, 11099 N. Torrey Pines Rd, suite 290, La Jolla, CA, 92037, USA.
Rujin ChengNGM Biopharmaceuticals, Inc., 333 Oyster Point Blvd, South San Francisco, CA, 94080, USA.
Sharon RozovskyDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE, 19716, USA. Electronic address: rozovsky@udel.edu.
University of Delaware · USNGM Biopharmaceuticals (United States) · USTorrey Pines Institute For Molecular Studies · USWeill Cornell Medical College in Qatar · QA

Funding

Selenoproteins in the ER-associated protein degradation pathwayR01GM121607 · NIGMS · UNIVERSITY OF DELAWARE · PI ROZOVSKY, SHARON · 2017 to 2021
$1.1M
NIGMS NIH HHS R01 GM121607
6 · The paper itself

Abstract

Selenoprotein S (selenos) is a small, intrinsically disordered membrane protein that is associated with various cellular functions, such as inflammatory processes, cellular stress response, protein quality control, and signaling pathways. It is primarily known for its contribution to the ER-associated degradation (ERAD) pathway, which governs the extraction of misfolded proteins or misassembled protein complexes from the ER to the cytosol for degradation by the proteasome. However, selenos's other cellular roles in signaling are equally vital, including the control of transcription factors and cytokine levels. Consequently, genetic polymorphisms of selenos are associated with increased risk for diabetes, dyslipidemia, and cardiovascular diseases, while high expression levels correlate with poor prognosis in several cancers. Its inhibitory role in cytokine secretion is also exploited by viruses. Since selenos binds multiple protein complexes, however, its specific contributions to various cellular pathways and diseases have been difficult to establish. Thus, the precise cellular functions of selenos and their interconnectivity have only recently begun to emerge. This review aims to summarize recent insights into the structure, interactome, and cellular roles of selenos.

Indexed as

Membrane ProteinsSelenoproteinsCytokinesCytokinesMembrane ProteinsSelenoproteinsSELENOSSelSSEPS1TANISVIMP

Identifiers

PMID36241082
PMCPMC10026367
OpenAlexW4304688958

What OpenQuestion holds

Textmetadata
LicenceTDM
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.