Evidence map›Paper›PMID 33837709›Full record

ArticleThe Enzymes2020

Engineering aminoacyl-tRNA synthetases for use in synthetic biology.

Natalie Krahn, Jeffery M Tharp, Ana Crnković, Dieter Söll

Abstract read
In one paragraph

Article in The Enzymes, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
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

27 citing papers in PubMed.

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  15. Article
  16. Article
  17. Tuning tRNAs for improved translation.Frontiers in genetics · 2024
    Review
  18. Biosynthesis, Engineering, and Delivery of Selenoproteins.International journal of molecular sciences · 2023
    Review
  19. Article
  20. 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.

Natalie KrahnDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, United States.
Jeffery M TharpDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, United States.
Ana CrnkovićDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, United States.
Dieter SöllDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, United States. Electronic address: dieter.soll@yale.edu.

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

Within the broad field of synthetic biology, genetic code expansion (GCE) techniques enable creation of proteins with an expanded set of amino acids. This may be invaluable for applications in therapeutics, bioremediation, and biocatalysis. Central to GCE are aminoacyl-tRNA synthetases (aaRSs) as they link a non-canonical amino acid (ncAA) to their cognate tRNA, allowing ncAA incorporation into proteins on the ribosome. The ncAA-acylating aaRSs and their tRNAs should not cross-react with 20 natural aaRSs and tRNAs in the host, i.e., they need to function as an orthogonal translating system. All current orthogonal aaRS•tRNA pairs have been engineered from naturally occurring molecules to change the aaRS's amino acid specificity or assign the tRNA to a liberated codon of choice. Here we discuss the importance of orthogonality in GCE, laboratory techniques employed to create designer aaRSs and tRNAs, and provide an overview of orthogonal aaRS•tRNA pairs for GCE purposes.

Indexed as

Amino Acyl-tRNA SynthetasesSynthetic BiologyAmino AcidsGenetic CodeRNA, TransferAmino AcidsAmino Acyl-tRNA SynthetasesRNA, TransferAminoacyl-tRNA synthetasesEvolutionGenetic code expansionNon-canonical amino acidSuppressorSynthetic biologytRNA

Identifiers

PMID33837709
PMCPMC8086897

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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.