Evidence map›Paper›PMID 36685256›Full record

ArticleRSC chemical biology2023

Selectivity and stability of N-terminal targeting protein modification chemistries.

Lydia J Barber, Nicholas D J Yates, Martin A Fascione, Alison Parkin, Glyn R Hemsworth, Paul G Genever, Christopher D Spicer

Open access · goldAbstract read
In one paragraph

Article in RSC chemical biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.0field-weighted citation impact, top 21% 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

3 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. One-Step Maleimide-Based Dual Functionalization of Protein N-Termini.Angewandte Chemie (International ed. in English) · 2025
    Article
  3. 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

7 authors at 2 institutions in 1 country.

Lydia J BarberDepartment of Chemistry, University of York Heslington YO10 5DD UK chris.spicer@york.ac.uk.ORCID https://orcid.org/0000-0002-4997-9876
Nicholas D J YatesDepartment of Chemistry, University of York Heslington YO10 5DD UK chris.spicer@york.ac.uk.
Martin A FascioneDepartment of Chemistry, University of York Heslington YO10 5DD UK chris.spicer@york.ac.uk.ORCID https://orcid.org/0000-0002-0066-4419
Alison ParkinDepartment of Chemistry, University of York Heslington YO10 5DD UK chris.spicer@york.ac.uk.ORCID https://orcid.org/0000-0003-4715-7200
Glyn R HemsworthAstbury Centre for Structural Molecular Biology and School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds Leeds LS2 9JT UK.ORCID https://orcid.org/0000-0002-8226-1380
Paul G GeneverYork Biomedical Research Institute, University of York Heslington YO10 5DD UK.
Christopher D SpicerDepartment of Chemistry, University of York Heslington YO10 5DD UK chris.spicer@york.ac.uk.ORCID https://orcid.org/0000-0001-8787-578X
University of York · GBUniversity of Leeds · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein N-termini provide uniquely reactive motifs for single site protein modification. Though a number of reactions have been developed to target this site, the selectivity, generality, and stability of the conjugates formed has not been studied. We have therefore undertaken a comprehensive comparative study of the most promising methods for N-terminal protein modification, and find that there is no 'one size fits all' approach, necessitating reagent screening for a particular protein or application. Moreover, we observed limited stability in all cases, leading to a need for continued innovation and development in the bioconjugation field.

Identifiers

PMID36685256
PMCPMC9811658
OpenAlexW4311082207

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Registered trials

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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.