Evidence map›Paper›PMID 35912579›Full record

ReviewJournal of the American Chemical Society2022

Chemical and Enzymatic Methods for Post-Translational Protein-Protein Conjugation.

Ross J Taylor, Michael B Geeson, Toby Journeaux, Gonçalo J L Bernardes

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of the American Chemical Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
6.3field-weighted citation impact, top 2% 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

35 citing papers in PubMed, 74 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Review
  6. Review
  7. Article
  8. Advances in Proximity-Assisted Bioconjugation.Accounts of chemical research · 2025
    Review
  9. Review
  10. Article
  11. Orthogonal Site-Specific Dual Bioconjugation of Aryl and Alkyl Thiols.Journal of the American Chemical Society · 2025
    Article
  12. Review
  13. One-Step Maleimide-Based Dual Functionalization of Protein N-Termini.Angewandte Chemie (International ed. in English) · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. 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

4 authors at 2 institutions in 2 countries.

Ross J TaylorDepartment of Chemistry, University of Cambridge, Lensfield Road, CB2 1EW Cambridge, U.K.
Michael B GeesonDepartment of Chemistry, University of Cambridge, Lensfield Road, CB2 1EW Cambridge, U.K.ORCID 0000-0002-9228-7947
Toby JourneauxDepartment of Chemistry, University of Cambridge, Lensfield Road, CB2 1EW Cambridge, U.K.ORCID 0000-0003-4561-1828
Gonçalo J L BernardesDepartment of Chemistry, University of Cambridge, Lensfield Road, CB2 1EW Cambridge, U.K.
University of Cambridge · GBUniversity of Lisbon · PT

Funding

Biotechnology and Biological Sciences Research Council BB/M01194
6 · The paper itself

Abstract

Fusion proteins play an essential role in the biosciences but suffer from several key limitations, including the requirement for N-to-C terminal ligation, incompatibility of constituent domains, incorrect folding, and loss of biological activity. This perspective focuses on chemical and enzymatic approaches for the post-translational generation of well-defined protein-protein conjugates, which overcome some of the limitations faced by traditional fusion techniques. Methods discussed range from chemical modification of nucleophilic canonical amino acid residues to incorporation of unnatural amino acid residues and a range of enzymatic methods, including sortase-mediated ligation. Through summarizing the progress in this rapidly growing field, the key successes and challenges associated with using chemical and enzymatic approaches are highlighted and areas requiring further development are discussed.

Indexed as

Amino AcidsProteinsProtein Processing, Post-TranslationalAmino AcidsProteins

Identifiers

PMID35912579
PMCPMC9389620
OpenAlexW4289131482

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.