Evidence map›Paper›PMID 30933556›Full record

ArticleACS chemical biology2019

Engineered Aminoacyl-tRNA Synthetases with Improved Selectivity toward Noncanonical Amino Acids.

Hui Si Kwok, Oscar Vargas-Rodriguez, Sergey V Melnikov, Dieter Söll

Abstract read
In one paragraph

Article in ACS chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed, 1 pooled it
1.5field-weighted citation impact, top 18% 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

18 citing papers in PubMed, 1 synthesis or guideline pooled it, 26 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Update of the Pyrrolysyl-tRNA Synthetase/tRNAJournal of bacteriology · 2023
    Review
  8. Split aminoacyl-tRNA synthetases for proximity-induced stop codon suppression.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Directed Evolution of theInternational journal of molecular sciences · 2021
    Article
  15. Article
  16. Article
  17. Article
  18. 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

4 authors at 1 institution in 1 country.

Hui Si KwokDepartment of Molecular Biophysics and Biochemistry , Yale University , New Haven , Connecticut 06520 , United States.ORCID 0000-0002-2858-8876
Oscar Vargas-RodriguezDepartment of Molecular Biophysics and Biochemistry , Yale University , New Haven , Connecticut 06520 , United States.
Sergey V MelnikovDepartment of Molecular Biophysics and Biochemistry , Yale University , New Haven , Connecticut 06520 , United States.
Dieter SöllDepartment of Molecular Biophysics and Biochemistry , Yale University , New Haven , Connecticut 06520 , United States.ORCID 0000-0002-3077-8986
Yale University · US

Funding

Studies of Transfer RNAR35GM122560 · NIGMS · YALE UNIVERSITY · PI SOLL, DIETER · 2017 to 2022
$5.6M
NIGMS NIH HHS R35 GM122560
6 · The paper itself

Abstract

A wide range of noncanonical amino acids (ncAAs) can be incorporated into proteins in living cells by using engineered aminoacyl-tRNA synthetase/tRNA pairs. However, most engineered tRNA synthetases are polyspecific; that is, they can recognize multiple rather than one ncAA. Polyspecificity of engineered tRNA synthetases imposes a limit to the use of genetic code expansion because it prevents specific incorporation of a desired ncAA when multiple ncAAs are present in the growth media. In this study, we employed directed evolution to improve substrate selectivity of polyspecific tRNA synthetases by developing substrate-selective readouts for flow-cytometry-based screening with the simultaneous presence of multiple ncAAs. We applied this method to improve the selectivity of two commonly used tRNA synthetases, p-cyano-l-phenylalanyl aminoacyl-tRNA synthetase ( pCNFRS) and N

Indexed as

Protein EngineeringAmino AcidsAmino Acyl-tRNA SynthetasesAmino AcidsAmino Acyl-tRNA Synthetases

Identifiers

PMID30933556
PMCPMC6642615
OpenAlexW2927651188

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.