Evidence map›Paper›PMID 29723718›Full record

ReviewCurrent opinion in chemical biology2018

Synthesis and semisynthesis of selenopeptides and selenoproteins.

Jun Liu, Rujin Cheng, Sharon Rozovsky

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

14 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Biomimetic Construction of Artificial Selenoenzymes.Biomimetics (Basel, Switzerland) · 2023
    Review
  7. Selenoprotein: Potential Player in Redox Regulation inAntioxidants (Basel, Switzerland) · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. The algal selenoproteomes.BMC genomics · 2020
    Article
  12. Article
  13. Efficient Generation of Hydrazides in Proteins by RadA Split Intein.Chembiochem : a European journal of chemical biology · 2020
    Article
  14. Review
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 2 institutions in 1 country.

Jun LiuUniversity of California, San Francisco, Department of Pharmaceutical Chemistry, 555 Mission Bay Blvd. South, San Francisco, CA 94158, United States. Electronic address: jun.liu@ucsf.edu.
Rujin ChengUniversity of Delaware, Department of Chemistry and Biochemistry, Newark, DE 19716, United States.
Sharon RozovskyUniversity of Delaware, Department of Chemistry and Biochemistry, Newark, DE 19716, United States. Electronic address: rozovsky@udel.edu.
University of Delaware · USUniversity of California, San Francisco · US

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

The versatile chemistry of the genetically encoded amino acid selenocysteine (Sec) is employed in Nature to expand the reactivity of enzymes. In addition to, its role in biology, Sec is used in protein engineering to modify folding, stability, and reactivity of proteins, to introduce conjugations and to facilitate reactions. However, due to limitations related to Sec's insertion mechanism in Nature, much of the production of Sec containing peptides and proteins relies on synthesis and semisynthesis. Here, we review recent advances that have enabled the assembly of complicated selenoproteins, including novel uses of protecting groups for solid phase peptide synthesis, rapid selenoester driven chemical ligations and versatile expressed protein ligations.

Indexed as

AnimalsBiocatalysisHumansModels, MolecularPeptidesProtein FoldingProtein StabilityRecombinant ProteinsSelenocysteineSelenoproteinsSolid-Phase Synthesis TechniquesPeptidesRecombinant ProteinsSelenocysteineSelenoproteins

Identifiers

PMID29723718
PMCPMC6195835
OpenAlexW2800248440

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.