Evidence map›Paper›PMID 39433956›Full record

ReviewNature reviews. Chemistry2024

Reprogramming the genetic code with flexizymes.

Takayuki Katoh, Hiroaki Suga

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. RaPID Selection of Backbone Macrocyclic Peptides Targeting Akt2.Angewandte Chemie (International ed. in English) · 2026
    Article
  7. Article
  8. Article
  9. De novo discovery of bicyclic cysteine-rich peptides targeting gasdermin D.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  10. Article
  11. Efficient Assembly of Functional RNA byJournal of the American Chemical Society · 2025
    Article
  12. Article
  13. PEARLs of wisdom for ribosome-independent peptide bond synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    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

2 authors.

Takayuki KatohDepartment of Chemistry, Graduate School of Science, University of Tokyo, Tokyo, Japan. katoh@chem.s.u-tokyo.ac.jp.ORCID http://orcid.org/0000-0001-6550-6203
Hiroaki SugaDepartment of Chemistry, Graduate School of Science, University of Tokyo, Tokyo, Japan. hsuga@chem.s.u-tokyo.ac.jp.ORCID http://orcid.org/0000-0002-5298-9186

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the canonical genetic code, the 61 sense codons are assigned to the 20 proteinogenic amino acids. Advancements in genetic code manipulation techniques have enabled the ribosomal incorporation of nonproteinogenic amino acids (npAAs). The critical molecule for translating messenger RNA (mRNA) into peptide sequences is aminoacyl-transfer RNA (tRNA), which recognizes the mRNA codon through its anticodon. Because aminoacyl-tRNA synthetases (ARSs) are highly specific for their respective amino acid-tRNA pairs, it is not feasible to use natural ARSs to prepare npAA-tRNAs. However, flexizymes are adaptable aminoacylation ribozymes that can be used to prepare diverse aminoacyl-tRNAs at will using amino acids activated with suitable leaving groups. Regarding recognition elements, flexizymes require only an aromatic ring in either the leaving group or side chain of the activated amino acid, and the conserved 3'-end CCA of the tRNA. Therefore, flexizymes allow virtually any amino acid to be charged onto any tRNA. The flexizyme system can handle not only L-α-amino acids with side chain modifications but also various backbone-modified npAAs. This Review describes the development of flexizyme variants and discusses their structure and mechanism and their applications in genetic code reprogramming for the synthesis of unique peptides and proteins.

Indexed as

Genetic CodeAmino AcidsAmino Acyl-tRNA SynthetasesRNA, CatalyticRNA, Transfer, Amino AcylAmino AcidsAmino Acyl-tRNA SynthetasesRNA, CatalyticRNA, Transfer, Amino Acyl

Identifiers

PMID39433956

What OpenQuestion holds

Textmetadata
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.