Evidence map›Paper›PMID 35510539›Full record

ReviewChemical Society reviews2022

Challenges in the use of sortase and other peptide ligases for site-specific protein modification.

Holly E Morgan, W Bruce Turnbull, Michael E Webb

Abstract readReview
In one paragraph

Review in Chemical Society reviews, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Amino acid variants at the P94 position inbioRxiv : the preprint server for biology · 2026
    Article
  10. Review
  11. A Putative Interaction between the Transmembrane Domains ofThe journal of physical chemistry. B · 2025
    Article
  12. Article
  13. Helicity-Dependent Enzymatic Peptide Cyclization.Journal of peptide science : an official publication of the European Peptide Society · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Structural Basis of High-Precision Protein Ligation and Its Application.Journal of the American Chemical Society · 2025
    Article
  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

3 authors.

Holly E MorganSchool of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, Woodhouse Lane, Leeds, LS2 9JT, UK. w.b.turnbull@leeds.ac.uk.ORCID http://orcid.org/0000-0002-9259-5237
W Bruce TurnbullSchool of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, Woodhouse Lane, Leeds, LS2 9JT, UK. w.b.turnbull@leeds.ac.uk.ORCID http://orcid.org/0000-0002-7352-0360
Michael E WebbSchool of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, Woodhouse Lane, Leeds, LS2 9JT, UK. w.b.turnbull@leeds.ac.uk.ORCID http://orcid.org/0000-0003-3574-4686

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Site-specific protein modification is a widely-used biochemical tool. However, there are many challenges associated with the development of protein modification techniques, in particular, achieving site-specificity, reaction efficiency and versatility. The engineering of peptide ligases and their substrates has been used to address these challenges. This review will focus on sortase, peptidyl asparaginyl ligases (PALs) and variants of subtilisin; detailing how their inherent specificity has been utilised for site-specific protein modification. The review will explore how the engineering of these enzymes and substrates has led to increased reaction efficiency mainly due to enhanced catalytic activity and reduction of reversibility. It will also describe how engineering peptide ligases to broaden their substrate scope is opening up new opportunities to expand the biochemical toolkit, particularly through the development of techniques to conjugate multiple substrates site-specifically onto a protein using orthogonal peptide ligases.

Indexed as

Cysteine EndopeptidasesLigasesBacterial ProteinsCatalysisPeptidesProtein EngineeringProtein Processing, Post-TranslationalSubstrate SpecificityBacterial ProteinsCysteine EndopeptidasesLigasesPeptides

Identifiers

PMID35510539
PMCPMC9126251

What OpenQuestion holds

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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.