Evidence map›Paper›PMID 37400596›Full record

ArticleNature chemistry2023

Site-specific bioorthogonal protein labelling by tetrazine ligation using endogenous β-amino acid dienophiles.

Daniel Richter, Edgars Lakis, Jörn Piel

Open access · hybridAbstract read
In one paragraph

Article in Nature chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

16 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
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  6. Peptide Backbone Editing via Post-Translational O to C Acyl Shift.Journal of the American Chemical Society · 2025
    Article
  7. Article
  8. Metagenomic study of lake microbial mats reveals protease-inhibiting antiviral peptides from a core microbiome member.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Bioorthogonal Reactions in Bioimaging.Topics in current chemistry (Cham) · 2024
    Review
  16. 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

3 authors at 1 institution in 1 country.

Daniel Richter *Institute of Microbiology, Eidgenössische Technische Hochschule (ETH) Zürich, Zürich, Switzerland.ORCID 0000-0003-2583-520X
Edgars Lakis *Institute of Microbiology, Eidgenössische Technische Hochschule (ETH) Zürich, Zürich, Switzerland.ORCID 0000-0002-9371-5560
Jörn PielInstitute of Microbiology, Eidgenössische Technische Hochschule (ETH) Zürich, Zürich, Switzerland. jpiel@ethz.ch.ORCID 0000-0002-2282-8154
Board of the Swiss Federal Institutes of Technology · CH

Funding

EC | EC Seventh Framework Programm | FP7 Ideas: European Research Council (FP7-IDEAS-ERC - Specific Programme: "Ideas" Implementing the Seventh Framework Programme of the European Community for Research, Technological Development and Demonstration Activities (2007 to 2013)) 742739Eidgenössische Technische Hochschule Zürich (Federal Institute of Technology Zurich) ETH-21 21-2
6 · The paper itself

Abstract

The tetrazine ligation is an inverse electron-demand Diels-Alder reaction widely used for bioorthogonal modifications due to its versatility, site specificity and fast reaction kinetics. A major limitation has been the incorporation of dienophiles in biomolecules and organisms, which relies on externally added reagents. Available methods require the incorporation of tetrazine-reactive groups by enzyme-mediated ligations or unnatural amino acid incorporation. Here we report a tetrazine ligation strategy, termed TyrEx (tyramine excision) cycloaddition, permitting autonomous dienophile generation in bacteria. It utilizes a unique aminopyruvate unit introduced by post-translational protein splicing at a short tag. Tetrazine conjugation occurs rapidly with a rate constant of 0.625 (15) M

Indexed as

Amino AcidsBacterial ProteinsHeterocyclic Compounds, 1-RingCycloaddition ReactionCytoskeletal ProteinsErb-b2 Receptor Tyrosine KinasesHumansAmino AcidsBacterial ProteinsCytoskeletal ProteinsErb-b2 Receptor Tyrosine KinasesFtsZ protein, BacteriaHeterocyclic Compounds, 1-Ring

Identifiers

PMID37400596
PMCPMC10533398
OpenAlexW4382989488

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.